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14676433
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4-(cytidine 5'-diphospho)-2-C-methyl-D-erythritol kinase
|
InterPro Family
In enzymology, a 4-(cytidine 5'-diphospho)-2-C-methyl-D-erythritol kinase (EC 2.7.1.148) is an enzyme that catalyzes the chemical reaction
ATP + 4-diphosphocytidyl-2-C-methyl-D-erythritol 2-phosphate formula_0 ADP + 4-diphosphocytidyl-2-C-methyl-D-erythritol 2-phosphate
Thus, the two substrates of this enzyme are ATP and 4-diphosphocytidyl-2-C-methyl-D-erythritol 2-phosphate (CDP-ME), whereas its two products are ADP and 4-diphosphocytidyl-2-C-methyl-D-erythritol 2-phosphate (CDP-MEP).
This enzyme belongs to the family of transferases, specifically those transferring phosphorus-containing groups (phosphotransferases) with an alcohol group as acceptor. The systematic name of this enzyme class is ATP:4-(cytidine 5'-diphospho)-2-C-methyl-D-erythritol 2-phosphotransferase. This enzyme is also called CDP-ME kinase, and IspE. This enzyme participates in the MEP pathway (non-mevalonate pathway) of isoprenoid precursor biosynthesis.
Structural studies.
As of late 2007, 7 structures have been solved for this class of enzymes, with PDB accession codes 1OJ4, 1UEK, 2V2Q, 2V2V, 2V2Z, 2V34, and 2V8P.
References.
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https://en.wikipedia.org/wiki?curid=14676433
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14676450
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5-dehydro-2-deoxygluconokinase
|
Class of enzymes
In enzymology, a 5-dehydro-2-deoxygluconokinase (EC 2.7.1.92) is an enzyme that catalyzes the chemical reaction
ATP + 5-dehydro-2-deoxy-D-gluconate formula_0 ADP + 6-phospho-5-dehydro-2-deoxy-D-gluconate
Thus, the two substrates of this enzyme are ATP and 5-dehydro-2-deoxy-D-gluconate, whereas its two products are ADP and 6-phospho-5-dehydro-2-deoxy-D-gluconate.
This enzyme belongs to the family of transferases, specifically those transferring phosphorus-containing groups (phosphotransferases) with an alcohol group as acceptor. The systematic name of this enzyme class is ATP:5-dehydro-2-deoxy-D-gluconate 6-phosphotransferase. Other names in common use include 5-keto-2-deoxygluconokinase, 5-keto-2-deoxyglucono kinase (phosphorylating), and DKH kinase. This enzyme participates in inositol metabolism.
References.
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https://en.wikipedia.org/wiki?curid=14676450
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14676473
|
5-methyldeoxycytidine-5'-phosphate kinase
|
Class of enzymes
In enzymology, a 5-methyldeoxycytidine-5'-phosphate kinase (EC 2.7.4.19) is an enzyme that catalyzes the chemical reaction
ATP + 5-methyldeoxycytidine 5'-phosphate formula_0 ADP + 5-methyldeoxycytidine diphosphate
Thus, the two substrates of this enzyme are ATP and 5-methyldeoxycytidine 5'-phosphate, whereas its two products are ADP and 5-methyldeoxycytidine diphosphate.
This enzyme belongs to the family of transferases, specifically those transferring phosphorus-containing groups (phosphotransferases) with a phosphate group as acceptor. The systematic name of this enzyme class is ATP:5-methyldeoxycytidine-5'-phosphate phosphotransferase.
References.
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https://en.wikipedia.org/wiki?curid=14676473
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14676498
|
Acetate kinase (diphosphate)
|
Class of enzymes
In enzymology, an acetate kinase (diphosphate) (EC 2.7.2.12) is an enzyme that catalyzes the chemical reaction
diphosphate + acetate formula_0 phosphate + acetyl phosphate
Thus, the two substrates of this enzyme are diphosphate and acetate, whereas its two products are phosphate and acetyl phosphate.
This enzyme belongs to the family of transferases, specifically those transferring phosphorus-containing groups (phosphotransferases) with a carboxy group as acceptor. The systematic name of this enzyme class is diphosphate:acetate phosphotransferase. This enzyme is also called pyrophosphate-acetate phosphotransferase. This enzyme participates in pyruvate metabolism.
References.
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https://en.wikipedia.org/wiki?curid=14676498
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14676518
|
(acetyl-CoA carboxylase) kinase
|
Class of enzymes
In enzymology, a [acetyl-CoA carboxylase] kinase (EC 2.7.11.27) is an enzyme that catalyzes the chemical reaction
ATP + [acetyl-CoA carboxylase] formula_0 ADP + [acetyl-CoA carboxylase] phosphate
Thus, the two substrates of this enzyme are ATP and acetyl-CoA carboxylase, whereas its two products are ADP and acetyl-CoA carboxylase phosphate.
This enzyme belongs to the family of transferases, specifically those transferring a phosphate group to the sidechain oxygen atom of serine or threonine residues in proteins (protein-serine/threonine kinases). The systematic name of this enzyme class is ATP:[acetyl-CoA carboxylase] phosphotransferase. Other names in common use include acetyl coenzyme A carboxylase kinase (phosphorylating), acetyl-CoA carboxylase bound kinase, acetyl-CoA carboxylase kinase, acetyl-CoA carboxylase kinase (cAMP-independent), acetyl-CoA carboxylase kinase 2, acetyl-CoA carboxylase kinase-2, acetyl-CoA carboxylase kinase-3 (AMP-activated), acetyl-coenzyme A carboxylase kinase, ACK2, ACK3, AMPK, I-peptide kinase, and STK5.
References.
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https://en.wikipedia.org/wiki?curid=14676518
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14676532
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Acetylglutamate kinase
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Class of enzymes
In enzymology, an acetylglutamate kinase (EC 2.7.2.8) is an enzyme that catalyzes the chemical reaction:
ATP + N-acetyl-L-glutamate formula_0 ADP + N-acetyl-L-glutamyl 5-phosphate
Thus, the two substrates of this enzyme are ATP and N-acetyl-L-glutamate, whereas its two products are ADP and N-acetyl-L-glutamyl 5-phosphate.
This enzyme belongs to the family of transferases, specifically those transferring phosphorus-containing groups (phosphotransferases) with a carboxy group as acceptor. This enzyme participates in urea cycle and metabolism of amino groups.
Nomenclature.
The systematic name of this enzyme class is ATP:N-acetyl-L-glutamate 5-phosphotransferase. Other names in common use include:
Structural studies.
As of late 2007, 9 structures have been solved for this class of enzymes, with PDB accession codes 1GS5, 1GSJ, 1OH9, 1OHA, 1OHB, 2AP9, 2BTY, 2BUF, and 2RD5.
References.
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https://en.wikipedia.org/wiki?curid=14676532
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14676549
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Acylglycerol kinase
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Class of enzymes
In enzymology, an acylglycerol kinase (EC 2.7.1.94) is an enzyme that catalyzes the chemical reaction
ATP + acylglycerol formula_0 ADP + acyl-sn-glycerol 3-phosphate
The two substrates of this enzyme are ATP and acylglycerol, whereas its two products are ADP and acyl-sn-glycerol 3-phosphate.
This enzyme belongs to the family of transferases, specifically those transferring phosphorus-containing groups (phosphotransferases) with an alcohol group as acceptor. The systematic name of this enzyme class is ATP:acylglycerol 3-phosphotransferase. Other names in common use include monoacylglycerol kinase, monoacylglycerol kinase (phosphorylating), sn-2-monoacylglycerol kinase, MGK, monoglyceride kinase, and monoglyceride phosphokinase. This enzyme participates in glycerolipid metabolism.
References.
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https://en.wikipedia.org/wiki?curid=14676549
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14676564
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Acyl-phosphate—hexose phosphotransferase
|
Class of enzymes
In enzymology, an acyl-phosphate-hexose phosphotransferase (EC 2.7.1.61) is an enzyme that catalyzes the chemical reaction
acyl phosphate + D-hexose formula_0 an acid + D-hexose phosphate
Thus, the two substrates of this enzyme are acyl phosphate and D-hexose, whereas its two products are acid and D-hexose phosphate.
This enzyme belongs to the family of transferases, specifically those transferring phosphorus-containing groups (phosphotransferases) with an alcohol group as acceptor. The systematic name of this enzyme class is acyl-phosphate:D-hexose phosphotransferase. This enzyme is also called hexose phosphate:hexose phosphotransferase.
References.
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14676611
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Adenosylcobinamide kinase
|
Class of enzymes
In enzymology, an adenosylcobinamide kinase (EC 2.7.1.156) is an enzyme that catalyzes the chemical reaction
RTP + adenosylcobinamide formula_0 adenosylcobinamide phosphate + RDP
Thus, the two substrates of this enzyme are RTP and adenosylcobinamide, whereas its two products are adenosylcobinamide phosphate and RDP.
This enzyme belongs to the family of transferases, specifically those transferring phosphorus-containing groups (phosphotransferases) with an alcohol group as acceptor. The systematic name of this enzyme class is RTP:adenosylcobinamide phosphotransferase. Other names in common use include CobU, adenosylcobinamide kinase/adenosylcobinamide-phosphate, guanylyltransferase, and AdoCbi kinase/AdoCbi-phosphate guanylyltransferase. This enzyme participates in porphyrin and chlorophyll metabolism.
References.
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14676626
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Adenosylcobinamide-phosphate guanylyltransferase
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Class of enzymes
In enzymology, an adenosylcobinamide-phosphate guanylyltransferase (EC 2.7.7.62) is an enzyme that catalyzes the chemical reaction
GTP + adenosylcobinamide phosphate formula_0 diphosphate + adenosylcobinamide-GDP
The two substrates of this enzyme are GTP and adenosylcobinamide phosphate; its two products are diphosphate and adenosylcobinamide-GDP.
This enzyme belongs to the family of transferases, specifically those transferring phosphorus-containing nucleotide groups (nucleotidyltransferases). The systematic name of this enzyme class is GTP:adenosylcobinamide-phosphate guanylyltransferase. Other names in common use include CobU, adenosylcobinamide kinase/adenosylcobinamide-phosphate, guanylyltransferase, and AdoCbi kinase/AdoCbi-phosphate guanylyltransferase. This enzyme is part of the biosynthetic pathway to cobalamin (vitamin B12) in bacteria.
References.
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https://en.wikipedia.org/wiki?curid=14676626
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14676642
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Adenylylsulfate—ammonia adenylyltransferase
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Class of enzymes
In enzymology, an adenylylsulfate-ammonia adenylyltransferase (EC 2.7.7.51) is an enzyme that catalyzes the chemical reaction adenylyl sulfate + NH3 formula_0 adenosine 5'-phosphoramidate + sulfate.
Thus, the two substrates of this enzyme are adenylyl sulfate and NH3, whereas its two products are adenosine 5'-phosphoramidate and sulfate.
This enzyme belongs to the family of transferases, specifically those transferring phosphorus-containing nucleotide groups (nucleotidyltransferases). The systematic name of this enzyme class is adenylyl-sulfate:ammonia adenylyltransferase. Other names in common use include APSAT, and adenylylsulfate:ammonia adenylyltransferase.
References.
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14676653
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Adenylyl-sulfate kinase
|
In enzymology, an adenylyl-sulfate kinase (EC 2.7.1.25) is an enzyme that catalyzes the chemical reaction
ATP + adenylyl sulfate formula_0 ADP + 3'-phosphoadenylyl sulfate
Thus, the two substrates of this enzyme are ATP and adenylyl sulfate, whereas its two products are ADP and 3'-phosphoadenylyl sulfate.
This enzyme belongs to the family of transferases, specifically those transferring phosphorus-containing groups (phosphotransferases) with an alcohol group as acceptor. The systematic name of this enzyme class is ATP:adenylyl-sulfate 3'-phosphotransferase. Other names in common use include adenylylsulfate kinase (phosphorylating), 5'-phosphoadenosine sulfate kinase, adenosine 5'-phosphosulfate kinase, adenosine phosphosulfate kinase, adenosine phosphosulfokinase, adenosine-5'-phosphosulfate-3'-phosphokinase, and APS kinase. This enzyme participates in 3 metabolic pathways: purine metabolism, selenoamino acid metabolism, and sulfur metabolism.
This enzyme contains an ATP binding P-loop motif.
Structural studies.
As of late 2007, 11 structures have been solved for this class of enzymes, with PDB accession codes 1D6J, 1M7G, 1M7H, 1X6V, 1XJQ, 1XNJ, 2AX4, 2GKS, 2OFW, 2OFX, and 2PEY.
References.
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https://en.wikipedia.org/wiki?curid=14676653
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14676682
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ADP-specific glucokinase
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Protein-coding gene in the species Homo sapiens
In enzymology, an ADP-specific glucokinase (EC 2.7.1.147) also known as ADP-dependent glucokinase is an enzyme that catalyzes the chemical reaction
ADP + D-glucose formula_0 AMP + D-glucose 6-phosphate
Thus, the two substrates of this enzyme are ADP and D-glucose, whereas its two products are AMP and D-glucose 6-phosphate.
This enzyme belongs to the family of transferases, to be specific those transferring phosphorus-containing groups (phosphotransferases) with an alcohol group as acceptor.
In humans, the ADP-dependent glucokinase is encoded by the "ADPGK" gene.
Structural studies.
As of late 2007, only one structure has been solved for this class of enzymes, with the PDB accession code 1GC5.
References.
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Further reading.
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https://en.wikipedia.org/wiki?curid=14676682
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14676707
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ADP-specific phosphofructokinase
|
In enzymology, an ADP-specific phosphofructokinase (EC 2.7.1.146) is an enzyme that catalyzes the chemical reaction
ADP + D-fructose 6-phosphate formula_0 AMP + D-fructose 1,6-bisphosphate
Thus, the two substrates of this enzyme are ADP and D-fructose 6-phosphate, whereas its two products are AMP and D-fructose 1,6-bisphosphate.
This enzyme belongs to the family of transferases, specifically those transferring phosphorus-containing groups (phosphotransferases) with an alcohol group as acceptor. The systematic name of this enzyme class is ADP:D-fructose-6-phosphate 1-phosphotransferase. This enzyme is also called ADP-6-phosphofructokinase, ADP-dependent phosphofructokinase.
Structural studies.
As of late 2007, only one structure has been solved for this class of enzymes, with the PDB accession code 1U2X.
References.
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https://en.wikipedia.org/wiki?curid=14676707
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14676731
|
ADP—thymidine kinase
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Enzyme
In enzymology, an ADP—thymidine kinase (EC 2.7.1.118) is an enzyme that catalyzes the chemical reaction
ADP + thymidine formula_0 AMP + thymidine 5'-phosphate
Thus, the two substrates of this enzyme are ADP and thymidine, whereas its two products are AMP and thymidine 5'-phosphate.
This enzyme belongs to the family of transferases, specifically those transferring phosphorus-containing groups (phosphotransferases) with an alcohol group as acceptor. The systematic name of this enzyme class is ADP:thymidine 5'-phosphotransferase. Other names in common use include ADP:dThd phosphotransferase, and adenosine diphosphate-thymidine phosphotransferase.
References.
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14676748
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Agmatine kinase
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In enzymology, an agmatine kinase (EC 2.7.3.10) is an enzyme that catalyzes the chemical reaction
ATP + agmatine formula_0 ADP + N4-phosphoagmatine
Thus, the two substrates of this enzyme are ATP and agmatine, whereas its two products are ADP and N4-phosphoagmatine.
This enzyme belongs to the family of transferases, specifically those transferring phosphorus-containing groups (phosphotransferases) with a nitrogenous group as acceptor. The systematic name of this enzyme class is ATP:agmatine N4-phosphotransferase. Other names in common use include phosphagen phosphokinase, and ATP:agmatine 4-N-phosphotransferase.
References.
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14676762
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Aldose-1-phosphate adenylyltransferase
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In enzymology, an aldose-1-phosphate adenylyltransferase (EC 2.7.7.36) is an enzyme that catalyzes the chemical reaction
ADP + alpha-D-aldose 1-phosphate formula_0 phosphate + ADP-aldose
Thus, the two substrates of this enzyme are ADP and alpha-D-aldose 1-phosphate, whereas its two products are phosphate and ADP-aldose.
This enzyme belongs to the family of transferases, specifically those transferring phosphorus-containing nucleotide groups (nucleotidyltransferases). The systematic name of this enzyme class is ADP:alpha-D-aldose-1-phosphate adenylyltransferase. Other names in common use include sugar-1-phosphate adenylyltransferase, ADPaldose phosphorylase, adenosine diphosphosugar phosphorylase, ADP sugar phosphorylase, adenosine diphosphate glucose:orthophosphate adenylyltransferase, and ADP:aldose-1-phosphate adenylyltransferase.
References.
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14676776
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Aldose-1-phosphate nucleotidyltransferase
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In enzymology, an aldose-1-phosphate nucleotidyltransferase (EC 2.7.7.37) is an enzyme that catalyzes the chemical reaction
NDP + alpha-D-aldose 1-phosphate formula_0 phosphate + NDP-aldose
Thus, the two substrates of this enzyme are NDP and alpha-D-aldose 1-phosphate, whereas its two products are phosphate and NDP-aldose.
This enzyme belongs to the family of transferases, specifically those transferring phosphorus-containing nucleotide groups (nucleotidyltransferases). The systematic name of this enzyme class is NDP:alpha-D-aldose-1-phosphate nucleotidyltransferase. Other names in common use include sugar-1-phosphate nucleotidyltransferase, NDPaldose phosphorylase, glucose 1-phosphate inosityltransferase, NDP sugar phosphorylase, nucleoside diphosphosugar phosphorylase, sugar phosphate nucleotidyltransferase, nucleoside diphosphate sugar:orthophosphate nucleotidyltransferase, sugar nucleotide phosphorylase, and NDP:aldose-1-phosphate nucleotidyltransferase. This enzyme participates in nucleotide sugars metabolism.
References.
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14676793
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Alkylglycerol kinase
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In enzymology, an alkylglycerol kinase (EC 2.7.1.93) is an enzyme that catalyzes the chemical reaction
ATP + 1-O-alkyl-sn-glycerol formula_0 ADP + 1-O-alkyl-sn-glycerol 3-phosphate
Thus, the two substrates of this enzyme are ATP and 1-O-alkyl-sn-glycerol, whereas its two products are ADP and 1-O-alkyl-sn-glycerol 3-phosphate.
This enzyme belongs to the family of transferases, specifically those transferring phosphorus-containing groups (phosphotransferases) with an alcohol group as acceptor. The systematic name of this enzyme class is ATP:1-O-alkyl-sn-glycerol 3-phosphotransferase. Other names in common use include 1-alkylglycerol kinase (phosphorylating), ATP-alkylglycerol phosphotransferase, alkylglycerol phosphotransferase, and ATP: 1-alkyl-sn-glycerol phosphotransferase. This enzyme participates in ether lipid metabolism.
References.
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14676819
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Alkylglycerone kinase
|
In enzymology, an alkylglycerone kinase (EC 2.7.1.84) is an enzyme that catalyzes the chemical reaction
ATP + O-alkylglycerone formula_0 ADP + O-alkylglycerone phosphate
Thus, the two substrates of this enzyme are ATP and O-alkylglycerone, whereas its two products are ADP and O-alkylglycerone phosphate.
This enzyme belongs to the family of transferases, specifically those transferring phosphorus-containing groups (phosphotransferases) with an alcohol group as acceptor. The systematic name of this enzyme class is ATP:O-alkylglycerone phosphotransferase. Other names in common use include alkyldihydroxyacetone kinase (phosphorylating), and alkyldihydroxyacetone kinase.
References.
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https://en.wikipedia.org/wiki?curid=14676819
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14676841
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Allose kinase
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In enzymology, an allose kinase (EC 2.7.1.55) is an enzyme that catalyzes the chemical reaction
ATP + D-allose formula_0 ADP + D-allose 6-phosphate
Thus, the two substrates of this enzyme are ATP and D-allose, whereas its two products are ADP and D-allose 6-phosphate.
This enzyme belongs to the family of transferases, specifically those transferring phosphorus-containing groups (phosphotransferases) with an alcohol group as acceptor. The systematic name of this enzyme class is ATP:D-allose 6-phosphotransferase. Other names in common use include allokinase (phosphorylating), allokinase, D-allokinase, and D-allose-6-kinase.
References.
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14676861
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Alpha-glucan, water dikinase
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In enzymology, an alpha-glucan, water dikinase (EC 2.7.9.4) is an enzyme that catalyzes the chemical reaction
ATP + alpha-glucan + H2O formula_0 AMP + phospho-alpha-glucan + phosphate
The 3 substrates of this enzyme are ATP, alpha-glucan, and H2O, whereas its 3 products are AMP, phospho-alpha-glucan, and phosphate.
This enzyme belongs to the family of transferases, specifically those transferring phosphorus-containing groups (phosphotransferases) with paired acceptors (dikinases). The systematic name of this enzyme class is ATP:alpha-glucan, water phosphotransferase. This enzyme is also called starch-related R1 protein, GWD.
References.
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14676880
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Ammonia kinase
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In enzymology, an ammonia kinase (EC 2.7.3.8) is an enzyme that catalyzes the chemical reaction
ATP + NH3 formula_0 ADP + phosphoramide
Thus, the two substrates of this enzyme are ATP and NH3, whereas its two products are ADP and phosphoramide.
This enzyme belongs to the family of transferases, specifically those transferring phosphorus-containing groups (phosphotransferases) with a nitrogenous group as acceptor. The systematic name of this enzyme class is ATP:ammonia phosphotransferase. Other names in common use include phosphoramidate-adenosine diphosphate phosphotransferase, and phosphoramidate-ADP-phosphotransferase.
References.
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14676896
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AMP—thymidine kinase
|
In enzymology, an AMP—thymidine kinase (EC 2.7.1.114) is an enzyme that catalyzes the chemical reaction
AMP + thymidine formula_0 adenosine + thymidine 5'-phosphate
Thus, the two substrates of this enzyme are AMP and thymidine, whereas its two products are adenosine and thymidine 5'-phosphate.
This enzyme belongs to the family of transferases, specifically those transferring phosphorus-containing groups (phosphotransferases) with an alcohol group as acceptor. The systematic name of this enzyme class is AMP:thymidine 5'-phosphotransferase. This enzyme is also called adenylate-nucleoside phosphotransferase.
References.
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https://en.wikipedia.org/wiki?curid=14676896
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14676920
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Anthranilate adenylyltransferase
|
In enzymology, an anthranilate adenylyltransferase (EC 2.7.7.55) is an enzyme that catalyzes the chemical reaction
ATP + anthranilate formula_0 diphosphate + N-adenylylanthranilate
Thus, the two substrates of this enzyme are ATP and anthranilate, whereas its two products are diphosphate and N-adenylylanthranilate.
This enzyme belongs to the family of transferases, specifically those transferring phosphorus-containing nucleotide groups (nucleotidyltransferases). The systematic name of this enzyme class is ATP:anthranilate N-adenylyltransferase. This enzyme is also called anthranilic acid adenylyltransferase.
References.
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https://en.wikipedia.org/wiki?curid=14676920
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14676932
|
Arginine kinase
|
Class of enzymes
In enzymology, arginine kinase (EC 2.7.3.3) is an enzyme that catalyzes the chemical reaction
ATP + L-arginine formula_0 ADP + Nω-phospho-L-arginine
Thus, the two substrates of this enzyme are ATP and L-arginine, whereas its two products are ADP and Nω-phospho-L-arginine. Unlike the phosphoester bond, formed during the phosphorylation of serine, threonine or tyrosine residues, the phosphoramidate (P-N bond) in phospho-arginine is unstable at low pH (<8), making it difficult to detect with the traditional mass spectrometry protocols.
Arginine kinase belongs to the family of transferases, specifically those transferring phosphorus-containing groups (phosphotransferases) with a nitrogenous group as acceptor. This enzyme participates in arginine and proline metabolism.
Nomenclature.
The systematic name of this enzyme class is
Other names in common use include
Function.
In Gram-positive bacteria, such as "Bacillus subtilis", the arginine kinase McsB phosphorylates the arginine residues on incorrectly folded or aggregated proteins to target them for degradation by the bacterial protease ClpC-ClpP (ClpCP).The phospho-arginine (pArg) modification is recognised by the N-terminal domain of ClpC, the protein-unfolding subunit of the ClpCP protease. Following recognition, the target protein is degraded by the ClpP subunit which has protease activity. Since phosphorylation reverses arginine's charge, the pArg modification has an unfolding effect on the target protein, easing its proteolytic degradation. Arginine phosphorylation is a dynamic post-translational modification, which can also be reversed by pArg-specific phosphatases, such as the bacterial YwlE. The pArg-ClpCP mechanism for protein degradation in bacteria is analogous to the eukaryotic ubiquitin-proteasome system.
Several studies have reported the presence of arginine kinases in eukaryotes. A recent study identified arginine phosphorylation on 118 proteins in Jurkat cells, which were primarily proteins with DNA/RNA-binding activities. The function of arginine phosphorylation in eukaryotes however is still unknown.
Structural studies.
As of late 2007, 8 structures have been solved for this class of enzymes, with PDB accession codes 1BG0, 1M15, 1M80, 1P50, 1P52, 1RL9, 1SD0, and 2J1Q.
References.
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Further reading.
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https://en.wikipedia.org/wiki?curid=14676932
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14676953
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ATP adenylyltransferase
|
In enzymology, an ATP adenylyltransferase (EC 2.7.7.53) is an enzyme that catalyzes the chemical reaction
ADP + ATP formula_0 phosphate + P1,P4-bis(5'-adenosyl) tetraphosphate
Thus, the two substrates of this enzyme are ADP and ATP, whereas its two products are phosphate and P1,P4-bis(5'-adenosyl) tetraphosphate.
This enzyme belongs to the family of transferases, specifically those transferring phosphorus-containing nucleotide groups (nucleotidyltransferases). The systematic name of this enzyme class is ADP:ATP adenylyltransferase. Other names in common use include bis(5'-nucleosyl)-tetraphosphate phosphorylase (NDP-forming), diadenosinetetraphosphate alphabeta-phosphorylase, adenine triphosphate adenylyltransferase, diadenosine 5',5'"-P1,P4-tetraphosphate alphabeta-phosphorylase, (ADP-forming), and dinucleoside oligophosphate alphabeta-phosphorylase. This enzyme participates in purine metabolism.
References.
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14676968
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Beta-adrenergic-receptor kinase
|
Enzyme
In enzymology, a beta-adrenergic-receptor kinase (EC 2.7.11.15) is an enzyme that catalyzes the chemical reaction:
ATP + [beta-adrenergic receptor] formula_0 ADP + phospho-[beta-adrenergic receptor]
Thus, the two substrates of this enzyme are ATP and beta-adrenergic receptor, whereas its two products are ADP and phospho-beta-adrenergic receptor.
This enzyme belongs to the family of transferases, specifically those transferring a phosphate group to the sidechain oxygen atom of serine or threonine residues in proteins (protein-serine/threonine kinases). The systematic name of this enzyme class is ATP:[beta-adrenergic receptor] phosphotransferase. Other names in common use include ATP:beta-adrenergic-receptor phosphotransferase, [beta-adrenergic-receptor] kinase, beta-adrenergic receptor-specific kinase, beta-AR kinase, beta-ARK, beta-ARK 1, beta-ARK 2, beta-receptor kinase, GRK2, GRK3, beta-adrenergic-receptor kinase (phosphorylating), beta2ARK, betaARK1, beta-adrenoceptor kinase, beta-adrenoceptor kinase 1, beta-adrenoceptor kinase 2, ADRBK1, BARK1, adrenergic receptor kinase, and STK15. Several compounds are known to inhibit this enzyme, including Zinc, and Digitonin.
References.
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14676986
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Beta-glucoside kinase
|
In enzymology, a beta-glucoside kinase (EC 2.7.1.85) is an enzyme that catalyzes the chemical reaction
ATP + cellobiose formula_0 ADP + 6-phospho-beta-D-glucosyl-(1,4)-D-glucose
Thus, the two substrates of this enzyme are ATP and cellobiose, whereas its two products are ADP and 6-phospho-beta-D-glucosyl-(1,4)-D-glucose.
This enzyme belongs to the family of transferases, specifically those transferring phosphorus-containing groups (phosphotransferases) with an alcohol group as acceptor. The systematic name of this enzyme class is ATP:cellobiose 6-phosphotransferase. This enzyme is also called beta-D-glucoside kinase (phosphorylating).
References.
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14677000
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Branched-chain-fatty-acid kinase
|
Class of enzymes
In enzymology, a branched-chain-fatty-acid kinase (EC 2.7.2.14) is an enzyme that catalyzes the chemical reaction
ATP + 2-methylpropanoate formula_0 ADP + 2-methylpropanoyl phosphate
Thus, the two substrates of this enzyme are ATP and 2-methylpropanoate, whereas its two products are ADP and 2-methylpropanoyl phosphate.
This enzyme belongs to the family of transferases, specifically those transferring phosphorus-containing groups (phosphotransferases) with a carboxy group as acceptor. The systematic name of this enzyme class is ATP:branched-chain-fatty-acid 1-phosphotransferase. This enzyme is also called isobutyrate kinase.
References.
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14677010
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Butyrate kinase
|
Class of enzymes
In enzymology, a butyrate kinase (EC 2.7.2.7) is an enzyme that catalyzes the chemical reaction
ADP + butyryl-phosphate formula_0 ATP + butyrate
Thus, the two substrates of this enzyme are ADP and butyryl-phosphate, whereas its two products are ATP and butyrate.
This enzyme belongs to the family of transferases, specifically those transferring phosphorus-containing groups (phosphotransferases) with a carboxy group as acceptor. The systematic name of this enzyme class is ATP:butanoate 1-phosphotransferase. This enzyme participates in butyrate metabolism.
This enzyme is transcribed from the gene "buk", which is part of the ASKHA super family.
ADP + butyryl-phosphate formula_0 ATP + butyrate
Mechanism.
The reaction above is a nucleophilic substitution reaction. An electron pair from an oxygen on ADP attacks the phosphorus on butyryl-phosphate, breaking the bond between phosphorus and oxygen to create ATP and butyrate. The arrow-pushing mechanism is shown above.
The reaction can also occur in the reverse direction, as shown below, under certain fermentation conditions.
ATP + butyrate formula_0 ADP + butyryl-phosphate
Structure.
As of 2015, two structures have been solved for this class of enzymes, with PDB accession codes 1SAZ and 1X9J. The study conducted to solve 1SAZ was retracted in 2012 due to fact that the data was used without the permission of the sole custodian.
The investigators of the study that produced the crystallization of 1X9J hypothesized that the enzyme was an octomer formed from dimers. The crystallized form has a radius of 7.5 nm which corresponded to a molecular weight of 380 kDa. Because a monomer of "buk2" is about 43 kDa, it was believed that the enzyme itself was either an octomer or a nonamer. Investigators hypothesized that the enzyme was an octomer since most of the proteins within the ASHKA super family form dimers.
Function.
Butyrate kinase is active within the human colon. To form butyrate, two molecules of acetyl-CoA are combined and reduced to produce butyryl-CoA. Butyryl CoA is then converted into butyrate through two reactions. The first reaction converts butyryl-CoA to butyryl-phosphate by using the phosphotransbutyrylase enzyme. Butyryl-phosphate is then converted into butyrate by using butyrate kinase and in the process, releases ATP.
Butyrate plays an important role within cells as it affects cellular proliferation, differentiation, and apoptosis.
Because of the significant roles that butyrate plays within cells, it is essential that butyrate kinase is functioning correctly, which can be done through regulation of the enzyme. One study has previously found that butyrate kinase is not regulated by its end-products or other acids such as acetic acid, but more studies need to be conducted to further elucidate the regulation of butyrate kinase.
Disease relevance.
As stated in the previous section, butyrate is involved with multiple cellular functions. Because of its involvement with these functions, it is hypothesized that butyrate can act as a protective agent against colon cancer and various inflammatory bowel diseases. Butyrate plays a key role in colon cancer by switching its role concerning cellular proliferation and apoptosis depending on the state and conditions of the cell. Butyrate also possesses anti-inflammatory effects to decrease colonic inflammation such as ulcerative colitis. One study specifically identified the transcription factor NF-kB as a target of butyrate to decrease the number of pro-inflammatory cytokines.
References.
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Further reading.
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14677027
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Carbamate kinase
|
Enzyme
In enzymology, a carbamate kinase (EC 2.7.2.2) is an enzyme that catalyzes the chemical reaction
ATP + NH3 + CO2 formula_0 ADP + carbamoyl phosphate
The 3 substrates of this enzyme are ATP, NH3, and CO2, whereas its two products are ADP and carbamoyl phosphate.
This enzyme belongs to the family of transferases, specifically those transferring phosphorus-containing groups (phosphotransferases) with a carboxy group as acceptor. The systematic name of this enzyme class is ATP:carbamate phosphotransferase. Other names in common use include CKase, carbamoyl phosphokinase, and carbamyl phosphokinase. This enzyme participates in 4 metabolic pathways: purine metabolism, glutamate metabolism, arginine and proline metabolism, and nitrogen metabolism.
Structural studies.
As of late 2007, 3 structures have been solved for this class of enzymes, with PDB accession codes 1B7B, 1E19, and 2E9Y.
References.
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14677039
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Carboxyvinyl-carboxyphosphonate phosphorylmutase
|
In enzymology, a carboxyvinyl-carboxyphosphonate phosphorylmutase (EC 2.7.8.23) is an enzyme that catalyzes the chemical reaction
1-carboxyvinyl carboxyphosphonate formula_0 3-(hydrohydroxyphosphoryl)pyruvate + CO2
Hence, this enzyme has one substrate, 1-carboxyvinyl carboxyphosphonate, and two products, 3-(hydrohydroxyphosphoryl)pyruvate and CO2.
This enzyme belongs to the family of transferases, specifically those transferring non-standard substituted phosphate groups. The systematic name of this enzyme class is 1-carboxyvinyl carboxyphosphonate phosphorylmutase (decarboxylating).
Structural studies.
As of late 2007, only one structure has been solved for this class of enzymes, with the PDB accession code 2QIW.
References.
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https://en.wikipedia.org/wiki?curid=14677039
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14677057
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CDP-diacylglycerol—glycerol-3-phosphate 3-phosphatidyltransferase
|
InterPro Family
In enzymology, a CDP-diacylglycerol—glycerol-3-phosphate 3-phosphatidyltransferase (EC 2.7.8.5) is an enzyme that catalyzes the chemical reaction
CDP-diacylglycerol + sn-glycerol 3-phosphate formula_0 CMP + 3(3-sn-phosphatidyl)-sn-glycerol 1-phosphate
Thus, the two substrates of this enzyme are CDP-diacylglycerol and sn-glycerol 3-phosphate, whereas its two products are CMP and 3(3-sn-phosphatidyl)-sn-glycerol 1-phosphate.
This enzyme belongs to the family of transferases, specifically those transferring non-standard substituted phosphate groups. This enzyme participates in glycerophospholipid metabolism.
References.
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https://en.wikipedia.org/wiki?curid=14677057
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14677079
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CDP-diacylglycerol—inositol 3-phosphatidyltransferase
|
Transferase enzyme
In enzymology, a CDP-diacylglycerol—inositol 3-phosphatidyltransferase (EC 2.7.8.11) is an enzyme that catalyzes the chemical reaction
CDP-diacylglycerol + myo-inositol formula_0 CMP + phosphatidyl-1D-myo-inositol
Thus, the two substrates of this enzyme are CDP-diacylglycerol and myo-inositol, whereas its two products are CMP and phosphatidyl-1D-myo-inositol.
This enzyme belongs to the family of transferases, specifically those transferring non-standard substituted phosphate groups. The systematic name of this enzyme class is CDP-diacylglycerol:myo-inositol 3-phosphatidyltransferase. Other names in common use include CDP-diglyceride-inositol phosphatidyltransferase, phosphatidylinositol synthase, CDP-diacylglycerol-inositol phosphatidyltransferase, CDP-diglyceride:inositol transferase, cytidine 5'-diphospho-1,2-diacyl-sn-glycerol:myo-inositol, 3-phosphatidyltransferase, CDP-DG:inositol transferase, cytidine diphosphodiglyceride-inositol phosphatidyltransferase, CDP-diacylglycerol:myo-inositol-3-phosphatidyltransferase, CDP-diglyceride-inositol transferase, cytidine diphosphoglyceride-inositol phosphatidyltransferase, and cytidine diphosphoglyceride-inositol transferase. This enzyme participates in glycerophospholipid metabolism and phosphatidylinositol signaling system.
References.
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14677094
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CDP-diacylglycerol—serine O-phosphatidyltransferase
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Class of enzymes
In enzymology, a CDP-diacylglycerol—serine O-phosphatidyltransferase (EC 2.7.8.8) is an enzyme that catalyzes the chemical reaction
CDP-diacylglycerol + L-serine formula_0 CMP + (3-sn-phosphatidyl)-L-serine
Thus, the two substrates of this enzyme are CDP-diacylglycerol and L-serine, whereas its two products are CMP and (3-sn-phosphatidyl)-L-serine.
This enzyme belongs to the family of transferases, specifically those transferring non-standard substituted phosphate groups. The systematic name of this enzyme class is CDP-diacylglycerol:L-serine 3-sn-phosphatidyltransferase. Other names in common use include phosphatidylserine synthase, CDPdiglyceride-serine O-phosphatidyltransferase, PS synthase, cytidine 5'-diphospho-1,2-diacyl-sn-glycerol, (CDPdiglyceride):L-serine O-phosphatidyltransferase, phosphatidylserine synthetase, CDP-diacylglycerol-L-serine O-phosphatidyltransferase, cytidine diphosphoglyceride-serine O-phosphatidyltransferase, CDP-diglyceride-L-serine phosphatidyltransferase, CDP-diglyceride:serine phosphatidyltransferase, cytidine 5'-diphospho-1,2-diacyl-sn-glycerol:L-serine, O-phosphatidyltransferase, and CDP-diacylglycerol:L-serine 3-O-phosphatidyltransferase. This enzyme participates in glycine, serine and threonine metabolism and glycerophospholipid metabolism.
References.
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14677112
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CDP-glycerol glycerophosphotransferase
|
In enzymology, a CDP-glycerol glycerophosphotransferase (EC 2.7.8.12) is an enzyme that catalyzes the chemical reaction
CDP-glycerol + (glycerophosphate)n formula_0 CMP + (glycerophosphate)n+1
Thus, the two substrates of this enzyme are CDP-glycerol and (glycerophosphate)n, whereas its two products are CMP and (glycerophosphate)n+1.
This enzyme belongs to the family of transferases, specifically those transferring non-standard substituted phosphate groups. The systematic name of this enzyme class is CDP-glycerol:poly(glycerophosphate) glycerophosphotransferase. Other names in common use include teichoic-acid synthase, cytidine diphosphoglycerol glycerophosphotransferase, poly(glycerol phosphate) polymerase, teichoic acid glycerol transferase, glycerophosphate synthetase, and CGPTase.
References.
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14677138
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CDP-ribitol ribitolphosphotransferase
|
In enzymology, a CDP-ribitol ribitolphosphotransferase (EC 2.7.8.14) is an enzyme that catalyzes the chemical reaction
CDP-ribitol + (ribitol phosphate)n formula_0 CMP + (ribitol phosphate)n+1
Thus, the two substrates of this enzyme are CDP-ribitol and (ribitol phosphate)n, whereas its two products are CMP and (ribitol phosphate)n+1.
This enzyme belongs to the family of transferases, specifically those transferring non-standard substituted phosphate groups. The systematic name of this enzyme class is CDP-ribitol:poly(ribitol phosphate) ribitolphosphotransferase. Other names in common use include teichoic-acid synthase, polyribitol phosphate synthetase, teichoate synthetase, poly(ribitol phosphate) synthetase, polyribitol phosphate polymerase, and teichoate synthase.
References.
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14677159
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Ceramide cholinephosphotransferase
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In enzymology, a ceramide cholinephosphotransferase (EC 2.7.8.3) is an enzyme that catalyzes the chemical reaction
CDP-choline + N-acylsphingosine formula_0 CMP + sphingomyelin
Thus, the two substrates of this enzyme are CDP-choline and N-acylsphingosine, whereas its two products are CMP and sphingomyelin.
This enzyme belongs to the family of transferases, specifically those transferring non-standard substituted phosphate groups. The systematic name of this enzyme class is CDP-choline:N-acylsphingosine cholinephosphotransferase. This enzyme is also called phosphorylcholine-ceramide transferase. This enzyme participates in sphingolipid metabolism.
References.
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14677177
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Ceramide kinase
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In enzymology, a ceramide kinase, also abbreviated as CERK, (EC 2.7.1.138) is an enzyme that catalyzes the chemical reaction:
ATP + ceramide formula_0 ADP + ceramide 1-phosphate
Thus, the two substrates of this enzyme are ATP and ceramide, whereas its two products are ADP and ceramide-1-phosphate.
This enzyme belongs to the family of transferases, specifically those transferring phosphorus-containing groups (phosphotransferases) with an alcohol group as acceptor. The systematic name of this enzyme class is ATP:ceramide 1-phosphotransferase. This enzyme is also called acylsphingosine kinase. This enzyme participates in sphingolipid metabolism.
Gene.
CERK is encoded by the CERK gene. The CERK gene is located on human chromosome 22q13, contains 13 exons, and is approximately 4.5kb in length. CERK shares sequence homology with sphingosine kinase type I, including an N-terminal pleckstrin homology (PH) domain and a diacylglycerol kinase domain. BLAST searches of expressed sequence tag (ESTs) by Sugiura and colleagues have yielded results showing orthologous CERK genes in other eukaryotes including "Drosophila melanogaster", "Caenorhabditis elegans", and "Oryza sativa". A mouse homolog has been cloned as well.
The complete gene of human CERK contains 4459bp, which consists of a 123bp-5’-untranslated region, a 2772bp 3’-non-coding, and a 1611bp open reading frame. Sequence analysis of CERK putatively suggests that the following post-translational modification sites exist: 4 N-glycosylation sites, 15 phosphorylation sites, 5 prenylation sites, and 2 amidation sites. The complete gene of mouse CERK differed slightly, containing a 1593bp open reading frame. The decreased length of the open reading frame results in the loss of 2 prenylation sites and 1 amidation site.
In human "CERK", a retinoic acid response element (RARE)-like exists between -40bp and -28bp and contains the sequence: TCCCCG C CGCCCG. RARE-like plays a role in transcription regulation of CERK. It is suspected that in the presence of all-trans retinoic acid (ATRA), chicken ovalbumin upstream promoter transcription factor I (COUP-TFI), retinoic acid receptor (RARα), retinoid X receptor (RXRα) bind the RARE-like of CERK in 5H-SY5Y cells. However, CERK expression varies per cell line. In contrast to SH-SY5Y neuroblastoma cells, HL60 leukemia cells demonstrated no binding of CERK even in the presence of ATRA. This suggests that differential expression of RARα, RXRα, and COUP-PTI may determine transcription levels in various cell lines.
Protein.
CERK is a 537 amino acid enzyme in humans (531 in mice). CERK was first discovered in 1989 when it was co-purified with synaptic vesicles from brain cells. Upon discovery, CERK was proposed to be a ceramide kinase that functions in the presence of μM concentration of calcium anions. Since CERK lacks a calcium binding site, the regulatory mechanism of CERK was poorly understood. CERK was later confirmed to bind calmodulin in the presence of calcium, indicating the calmodulin first binds calcium and then CERK. Once bound, CERK becomes active and is capable of phosphorylating ceramides. Binding of calmodulin occurs between amino acids 420 and 437 in CERK at a putative 1-8-14B calmodulin binding motif. The binding motif in CERK contains leu-422, phe-429, and leu-435 which respectively correspond to the 1st, 8th, and 14th hydrophobic amino acids where calmodulin binds. Mutation of Phe-429 results in weak calmodulin binding, while mutations of Phe-331 or Phe-335 entirely preclude binding.
CERK activity has primarily been observed within human neutrophils, cerebrum granule cells, and epithelium-derived lung cells. When inactive, CERK is suspended within the cytosol of the cell. When CERK is activated by interleukin-1β, it is localized to the trans-golgi, and from there, possibly delivered to the plasma membrane. Activation may also to cause CERK to localize within endosomes. CERK’s PH domain plays an integral role in this localization. Once localized, to the trans-golgi CERK activates cytosolic phospholipase A2 (cPLA2) that has localized to the trans-golgi. Activation of cPLA2 results in hydrolysis of membrane phospholipids to produce arachidonic acid. Ceramide kinase has also been demonstrated to regulate localization and level of phosphatidylinositol 4,5-bisphosphate (PIP2) produced from NORPA, a phospholipase C homolog in "Drosophila melanogaster". In addition to endosomal and trans-golgi localization, CERK has been found to localize to outer mitochondrial membrane at the site of COX-2 localization in A549 cells.
Ceramide-1-phosphate.
As a lipid kinase CERK is responsible for the phosphorylation of ceramides. CERK is capable of phosphorylating multiple ceramide species. Though CERK will phosphorylate C2, C20, C22, and C24 ceramides, substrate specificity is quite poor. By contrast, CERK has the greatest substrate specificity for C6, C8, and C16 ceramides, indicating that the location of the sphingosine group plays a role in specificity. Dihydroceramide can also be phosphorylated by CERK, but to a lesser extent. In contrast to C6 ceramide, CERK has low specificity for C6 dihydroceramide, but retains high specificity for C8 dihydroceramide- Ceramide transport proteins (CERTs) transport ceramides to CERK for phosphorylation. Phosphorylation of ceramides to produce ceramide-1-phosphate (C-1-P) is believed to facilitate the localization of cPLA2 to the trans-golgi so that CERK can activate cPLA2.
Functions in molecular biology.
Cell survival and proliferation.
Production of C-1-P bolsters cell survival and proliferation. It has been shown that C-1-P promotes DNA synthesis in fibroblasts. C-1-P also prevents apoptosis by inhibiting the caspase-9/caspase-3 pathway and preventing DNA fragmentation in macrophages. This is thought to occur via C-1-P interacting with and blocking functionality of acid sphingomyelinase. This results in diminished ceramide production, which precludes apoptosis. Recently, phosphorylation of ceramide via CERK has been shown to stimulate myoblast proliferation. It was demonstrated that C-1-P perpetuates the phosphorylation of glycogen synthase kinase-3 β and retinoblastoma protein, which contributes to transition from the G1 phase to M phase of the cell cycle. Additionally, production of C-1-P appears to result in increased expression of Cyclin D. CERK has demonstrated an ability to activate phosphatidylinositol 3-kinase/Akt (PI3K/Akt), ERK1/2, and mTOR. CERKs ability to produce signaling molecules that facilitate the activation of cell proliferation as well as its interaction with PI3K/Akt, and mTOR indicate that disregulated CERK expression may lead to cancer. In "Drosophila" Dasgupta et al 2009 finds CerK increases proapoptotic ceramide activity, and this increases photoreceptor cell apoptotic turnover.
Other roles.
In addition to cell survival and proliferation, CERK has been implicated in many other processes. CERK is believed to participate in altering the lipid raft structure via C-1-P production, contributing to phagosome formation in polymorphonuclear leukocytes. CERK has also been found to participate in the calcium-dependent degranulation of mast cells.
References.
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14677194
|
Choline kinase
|
Choline kinase (also known as CK, ChoK and choline phosphokinase) is an enzyme which catalyzes the first reaction in the choline pathway for phosphatidylcholine (PC) biosynthesis. This reaction involves the transfer of a phosphate group from adenosine triphosphate (ATP) to choline in order to form phosphocholine.
ATP + choline formula_0 ADP + O-phosphocholine
Thus, the two substrates of this enzyme are ATP and choline, whereas its two products are adenosine diphosphate (ADP) and O-phosphocholine. Choline kinase requires magnesium ions (+2) as a cofactor for this reaction. This enzyme belongs to the family of transferases, specifically those transferring phosphorus-containing groups (phosphotransferases) with an alcohol group as acceptor. The first detailed investigation of the enzyme was conducted by McCamen in 1962, where it was shown that the brain is the richest source of the enzyme in mammalian tissue. A related enzyme, ethanolamine kinase, tends to co-purify with choline kinase leading to a suggestion that the two activities are mediated by two distinct active sites on a single protein. The systematic name of this enzyme class is ATP:choline phosphotransferase. These enzymes participate in glycine, serine and threonine metabolism and glycerophospholipid metabolism.
In mammalian cells, the enzyme exists as three isoforms: CKα-1, CKα-2 and CKβ. These isoforms are encoded by two separate genes, CHKA and CHKB and are only active in their homodimeric, heterodimeric and oligomeric forms.
Structural studies.
As of late 2007, six structures have been solved for this class of enzymes, with PDB accession codes 1NW1, 2CKO, 2CKP, 2CKQ, 2I7Q, and 2IG7.
CKα-2 originating from C. elegans, is a dimeric enzyme with each monomer being composed of two domains. The active site is located between the two domains (see figure below). Its overall structure is similar to members of the eukaryotic protein kinase family. Mammalian choline kinases exists in either dimeric or tetrameric forms in solution. Structural studies carried out on CKα-2 have implied that the conserved residues in the CK family of enzymes could possibly play a vital role in substrate binding as well as in the stabilization of catalytically important residues.
An enlarged view of the residues involved in the dimer interface between the S-shaped loop of the yellow subunit and the loop following helix A and strand 4 of the cyan subunit. Only residues that are involved in direct salt bridges, hydrogen bonds, or van der Waals interactions are shown. Salt bridges and hydrogen bonds, dashed lines; labels of residues from the yellow subunit, red; labels of residues from the cyan subunit, blue.
Mechanism.
Although not much is known about the mechanism by which choline kinase reacts, the recent advancement in the elucidation of the structure of the enzyme has provided scientists with much more insight than they had previously. Since the structure of CK is very similar to that of the eukaryotic protein kinase family, the location of ATP and choline binding pockets have been proposed. These are shown in the figures below.
Proposed ATP binding site.
In this figure, there is a similarity between APH(3′)-IIIa, an aminoglycoside phosphotransferase and CK.
Proposed choline binding site.
Propositions for this mechanism have been made based on mechanistic studies done on eukaryotic protein kinases. It has been proposed that in the CKα-2 mechanism, ATP binds first, followed by choline, and then the transfer of the phosphoryl group takes place. The product O-phosphocholine is then released, followed by the release of ADP.
Evolution.
After closely studying the structurally similar enzymes, CKα-2, APH(3′)-IIIa, and PKA, researchers observed that PKA had less insertions to its structural core compared to the other enzymes. Against this background, it is believed that CKα-2 have evolved from PKA to have more structural elements attached to it.
Biological function.
Choline kinase catalyzes the formation of phosphocholine, the committed step in phosphatidylcholine biosynthesis. Phosphatidylcholine is the major phospholipid in eukaryotic membranes. Phosphatidylcholine is important for a variety of function in eukaryotes such as facilitating the transport of cholesterol through the organism, acting as a substrate for the production of second messengers and as a cofactor for the activity of several membrane-related enzymes. CK also plays a vital role in the production of sphingomyelin, another important membrane phospholipid and in the regulation of cell growth.
The production of phosphocholine from CK is necessary for the signal transduction pathways related to mitogenesis. It has also been found that CK plays a critical role in the proliferation of human mammary epithelial cells.
Choline kinase α as protein chaperone.
Choline kinase α can act as a protein chaperone. Kinase can function as chaperone and there may be other kinases that may function as chaperone that are yet to be identified. Choline kinase α (CKα) is overexpressed in prostate cancer where it physically interacts with the androgen receptor (AR), a major driver of prostate cancer. By disabling the function of CHKA researchers were able to inhibit AR function and prostate cancer growth.
In vivo studies carried out using CKα-1 and CKβ isoforms suggest that each isoform might be involved in different biochemical pathways. CKβ plays a major role in the catalysis of the phosphorylation of ethanolamine while CKα-1 catalyzes the phosphorylation of both choline and ethanolamine. ShRNA mediated in vivo depletion of CKα has been shown to decrease the growth of prostate tumor xenografts
Disease relevance.
Oncogenic activity and CKα-1.
Overexpression of CKα-1 has been found to be associated with cancer. Recent studies carried out on cancer cell lines have shown that CKα-1 is over-expressed in breast cancer cells. This leads to an accumulation of phosphocholine in the breast and causes malignancy.
Studies using colon, human lung and prostate carcinomas also revealed that CK is upregulated by overexpression of CKα-1 in these cells compared to the normal, non-cancerous cells.
One possible explanation for this is that CKα-1 aids in the regulation of protein kinase B phosphorylation, particularly at the Serine-473 end. Consequently, high levels of expression and activity of CKα-1 promotes cell growth and survival. Based on the observation that increased activity of CKα-1 is related to cancer, CKα-1 has promising use as a tumor biomarker and in diagnosing and following the progression of tumors. All human cancer cells have shown increased levels of this particular enzyme.
Muscular dystrophy and CKβ.
It has been shown, using CKβ knockout mice models, that a defect in the CKβ activity leads to a decrease in the phosphatidylcholine (PC) content in the hindlimb muscle. This, however, does not affect the phosphoethanolamine (PE) content.
The net effect is then that the PC/PE ratio decreases and this leads to impaired membrane integrity in the liver. This compromised membrane potential leads to malfunctioning of the mitochondria. Although CK is required for the biosynthesis of PC, CK is normally present in excess and so is not generally considered the rate-limiting step. Researchers have concluded, however, that due to the reduced activity of CK seen in the hindlimb muscle of the CKβ knockout mice model, CK is probably the rate-limiting enzyme in skeletal muscles. This suggests that defect in CKβ may lead to a decrease in PC synthesis in the muscles resulting in muscular dystrophy. These results suggest that CK could possibly play a vital role in the homeostasis of PC.
References.
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Further reading.
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14677213
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Choline-phosphate cytidylyltransferase
|
Choline-phosphate cytidylyltransferase (EC 2.7.7.15) is an enzyme that catalyzes the chemical reaction
CTP + choline phosphate formula_0 diphosphate + CDP-choline
where the two substrates of this enzyme are CTP and choline phosphate, and the two products are diphosphate and CDP-choline. It is responsible for regulating phosphatidylcholine content in membranes.
This enzyme belongs to the family of transferases, specifically those transferring phosphorus-containing nucleotide groups (nucleotidyltransferases). The systematic name of this enzyme class is CTP:choline-phosphate cytidylyltransferase. Other names in common use include phosphorylcholine transferase, CDP-choline pyrophosphorylase, CDP-choline synthetase, choline phosphate cytidylyltransferase, CTP-phosphocholine cytidylyltransferase, CTP:phosphorylcholine cytidylyltransferase, cytidine diphosphocholine pyrophosphorylase, phosphocholine cytidylyltransferase, phosphorylcholine cytidylyltransferase, and phosphorylcholine:CTP cytidylyltransferase. This enzyme participates in aminophosphonate metabolism and glycerophospholipid metabolism.
Structural studies.
As of late 2007, two structures have been solved for this class of enzymes, with PDB accession codes 1PEH and 1PEI.
References.
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14677232
|
Cytidylate kinase
|
In enzymology, a cytidylate kinase (EC 2.7.4.14) is an enzyme that catalyzes the chemical reaction
ATP + (d)CMP formula_0 ADP + (d)CDP
Thus, the two substrates of this enzyme are ATP and dCMP, whereas its two products are ADP and dCDP.
This enzyme belongs to the family of transferases, specifically those transferring phosphorus-containing groups (phosphotransferases) with a phosphate group as acceptor. The systematic name of this enzyme class is ATP:CMP phosphotransferase. Other names in common use include: deoxycytidylate kinase, deoxycytidylate kinase, CMP kinase, CTP:CMP phosphotransferase, dCMP kinase, deoxycytidine monophosphokinase, UMP-CMP kinase, ATP:UMP-CMP phosphotransferase, and pyrimidine nucleoside monophosphate kinase. This enzyme participates in pyrimidine metabolism.
References.
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Further reading.
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14677257
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D-arabinokinase
|
In enzymology, a D-arabinokinase (EC 2.7.1.54) is an enzyme that catalyzes the chemical reaction
ATP + D-arabinose formula_0 ADP + D-arabinose 5-phosphate
Thus, the two substrates of this enzyme are ATP and D-arabinose, whereas its two products are ADP and D-arabinose 5-phosphate.
This enzyme belongs to the family of transferases, specifically those transferring phosphorus-containing groups (phosphotransferases) with an alcohol group as acceptor. The systematic name of this enzyme class is ATP:D-arabinose 5-phosphotransferase. This enzyme is also called D-arabinokinase (phosphorylating).
References.
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14677279
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Dehydrogluconokinase
|
Enzyme
In enzymology, a dehydrogluconokinase (EC 2.7.1.13) is an enzyme that catalyzes the chemical reaction
ATP + 2-dehydro-D-gluconate formula_0 ADP + 6-phospho-2-dehydro-D-gluconate
Thus, the two substrates of this enzyme are ATP and 2-dehydro-D-gluconate, whereas its two products are ADP and 6-phospho-2-dehydro-D-gluconate.
This enzyme belongs to the family of transferases, specifically those transferring phosphorus-containing groups (phosphotransferases) with an alcohol group as acceptor. The systematic name of this enzyme class is ATP:2-dehydro-D-gluconate 6-phosphotransferase. Other names in common use include ketogluconokinase, 2-ketogluconate kinase, ketogluconokinase (phosphorylating), and 2-ketogluconokinase. This enzyme participates in pentose phosphate pathway.
References.
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14677297
|
Deoxyadenosine kinase
|
In enzymology, a deoxyadenosine kinase (EC 2.7.1.76) is an enzyme that catalyzes the chemical reaction
ATP + deoxyadenosine formula_0 ADP + dAMP
Thus, the two substrates of this enzyme are ATP and deoxyadenosine, whereas its two products are ADP and dAMP.
This enzyme belongs to the family of transferases, specifically those transferring phosphorus-containing groups (phosphotransferases) with an alcohol group as acceptor. The systematic name of this enzyme class is ATP:deoxyadenosine 5'-phosphotransferase. This enzyme is also called purine-deoxyribonucleoside kinase. This enzyme participates in purine metabolism.
Structural studies.
As of late 2007, only one structure has been solved for this class of enzymes, with the PDB accession code 2JAQ.
References.
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14677314
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(deoxy)adenylate kinase
|
Class of enzymes
In enzymology, a (deoxy)adenylate kinase (EC 2.7.4.11) is an enzyme that catalyzes the chemical reaction
ATP + dAMP formula_0 ADP + dADP
Thus, the two substrates of this enzyme are ATP and dAMP, whereas its two products are ADP and dADP.
This enzyme belongs to the family of transferases, specifically those transferring phosphorus-containing groups (phosphotransferases) with a phosphate group as acceptor. The systematic name of this enzyme class is ATP:(d)AMP phosphotransferase. This enzyme participates in purine metabolism.
References.
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14677333
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Deoxyguanosine kinase
|
See DGUOK for a more thorough description of the human deoxyguanosine kinase.
Description of the catalyzed reaction and general features of deoxyguanosine kinases.
In enzymology, a deoxyguanosine kinase (EC 2.7.1.113) is an enzyme that catalyzes the chemical reaction
ATP + deoxyguanosine formula_0 ADP + dGMP
Thus, the two substrates of this enzyme are ATP and deoxyguanosine, whereas its two products are ADP and dGMP.
This enzyme belongs to the family of transferases, specifically those transferring phosphorus-containing groups (phosphotransferases) with an alcohol group as acceptor. The systematic name of this enzyme class is ATP:deoxyguanosine 5'-phosphotransferase. Other names in common use include deoxyguanosine kinase (phosphorylating), (dihydroxypropoxymethyl)guanine kinase, 2'-deoxyguanosine kinase, and NTP-deoxyguanosine 5'-phosphotransferase. This enzyme participates in purine metabolism.
Structural studies.
As of late 2007, 4 structures have been solved for this class of enzymes, with PDB accession codes 2JAQ, 2JAS, 2JAT, and 2OCP.
Clinical.
Mutations in this gene have been linked to inherited mitochondrial DNA depletion syndromes, neonatal liver failure, nystagmus and hypotonia.
References.
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14677349
|
Deoxynucleoside kinase
|
Deoxynucleoside kinases are generally grouped into two families based on structural homology:
TK1 family. This family has got its name from the human enzyme thymidine kinase 1. The substrate specificity is restricted to thymidine (and to lesser extent deoxyuridine) among the natural substrates. TK1 family members are widespread and found in eukaryotes as well as prokaryotes.
Non-TK1-like family. This family includes deoxycytidine kinase (cytosolic) as well as the two mitochondrial enzymes deoxyguanosine kinase and thymidine kinase 2 in humans. The base specificity is generally broader than for the TK-1 family. Non-TK1 family members are widespread and found in eukaryotes as well as prokaryotes. Also the herpesvirus thymidine kinase belongs to this family although it is not obvious from the sequence homology (it is still structurally related).
Catalyzed reaction.
In enzymology, a deoxynucleoside kinase (EC 2.7.1.145) is an enzyme that catalyzes the chemical reaction
ATP + 2'-deoxynucleoside formula_0 ADP + 2'-deoxynucleoside 5'-phosphate
Thus, the two substrates of this enzyme are ATP and 2'-deoxynucleoside, whereas its two products are ADP and 2'-deoxynucleoside 5'-phosphate.
This enzyme belongs to the family of transferases, specifically those transferring phosphorus-containing groups (phosphotransferases) with an alcohol group as acceptor. The systematic name of this enzyme class is ATP:deoxynucleoside 5'-phosphotransferase. Other names in common use include multispecific deoxynucleoside kinase, ms-dNK, multisubstrate deoxyribonucleoside kinase, multifunctional deoxynucleoside kinase, D. melanogaster deoxynucleoside kinase, and Dm-dNK.
Structural studies.
As of late 2007, 5 structures have been solved for this class of enzymes, with PDB accession codes 1OE0, 1OT3, 1ZM7, 1ZMX, and 2JCS.
References.
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14677371
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(deoxy)nucleoside-phosphate kinase
|
Class of enzymes
In enzymology, a (deoxy)nucleoside-phosphate kinase (EC 2.7.4.13) is an enzyme that catalyzes the chemical reaction
ATP + deoxynucleoside phosphate formula_0 ADP + deoxynucleoside diphosphate
Thus, the two substrates of this enzyme are ATP and deoxynucleoside phosphate, whereas its two products are ADP and deoxynucleoside diphosphate.
This enzyme belongs to the family of transferases, specifically those transferring phosphorus-containing groups (phosphotransferases) with a phosphate group as acceptor. The systematic name of this enzyme class is ATP:deoxynucleoside-phosphate phosphotransferase. Other names in common use include deoxynucleoside monophosphate kinase, deoxyribonucleoside monophosphokinase, and deoxynucleoside-5'-monophosphate kinase.
Structural studies.
As of late 2007, two structures have been solved for this class of enzymes, with PDB accession codes 1DEK and 1DEL.
References.
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14677395
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Dephospho-CoA kinase
|
In enzymology, a dephospho-CoA kinase (EC 2.7.1.24) is an enzyme that catalyzes the chemical reaction
ATP + dephospho-CoA formula_0 ADP + CoA
Thus, the two substrates of this enzyme are ATP and dephospho-CoA, whereas its two products are ADP and CoA.
This enzyme belongs to the family of transferases, specifically those transferring phosphorus-containing groups (phosphotransferases) with an alcohol group as acceptor. The systematic name of this enzyme class is ATP:dephospho-CoA 3'-phosphotransferase. Other names in common use include dephosphocoenzyme A kinase (phosphorylating), 3'-dephospho-CoA kinase, and dephosphocoenzyme A kinase. This enzyme participates in pantothenate and coa biosynthesis.
Structural studies.
As of late 2007, 8 structures have been solved for this class of enzymes, with PDB accession codes 1JJV, 1N3B, 1T3H, 1VHL, 1VHT, 1VIY, 2GRJ, and 2IF2.
References.
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14677415
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Dephospho-(reductase kinase) kinase
|
In enzymology, a dephospho-[reductase kinase] kinase (EC 2.7.11.3) is an enzyme that catalyzes the chemical reaction
ATP + dephospho-{[hydroxymethylglutaryl-CoA reductase (NADPH)] kinase} formula_0 ADP + {[hydroxymethylglutaryl-CoA reductase (NADPH)] kinase}
Thus, the two substrates of this enzyme are ATP and dephospho-{[hydroxymethylglutaryl-CoA reductase (NADPH)] kinase}, whereas its two products are ADP and {[hydroxymethylglutaryl-CoA reductase (NADPH)] kinase}.
This enzyme belongs to the family of transferases, specifically those transferring a phosphate group to the sidechain oxygen atom of serine or threonine residues in proteins (protein-serine/threonine kinases). The systematic name of this enzyme class is ATP:dephospho-{[hydroxymethylglutaryl-CoA reductase (NADPH)] kinase} phosphotransferase. Other names in common use include AMP-activated kinase, AMP-activated protein kinase kinase, hydroxymethylglutaryl coenzyme A reductase kinase kinase, hydroxymethylglutaryl coenzyme A reductase kinase kinase, (phosphorylating), reductase kinase, reductase kinase kinase, and STK30.
References.
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14677452
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Dihydrostreptomycin-6-phosphate 3'alpha-kinase
|
In enzymology, a dihydrostreptomycin-6-phosphate 3'alpha-kinase (EC 2.7.1.88) is an enzyme that catalyzes the chemical reaction
ATP + dihydrostreptomycin 6-phosphate formula_0 ADP + dihydrostreptomycin 3'alpha,6-bisphosphate
Thus, the two substrates of this enzyme are ATP and dihydrostreptomycin 6-phosphate, whereas its two products are ADP and dihydrostreptomycin 3'alpha,6-bisphosphate.
This enzyme belongs to the family of transferases, specifically those transferring phosphorus-containing groups (phosphotransferases) with an alcohol group as acceptor. The systematic name of this enzyme class is ATP:dihydrostreptomycin-6-phosphate 3'alpha-phosphotransferase. Other names in common use include dihydrostreptomycin 6-phosphate kinase (phosphorylating), and ATP:dihydrostreptomycin-6-P 3'alpha-phosphotransferase.
References.
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14677481
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Diphosphate—glycerol phosphotransferase
|
In enzymology, a diphosphate-glycerol phosphotransferase (EC 2.7.1.79) is an enzyme that catalyzes the chemical reaction
diphosphate + glycerol formula_0 phosphate + glycerol 1-phosphate
Thus, the two substrates of this enzyme are diphosphate and glycerol, whereas its two products are phosphate and glycerol 1-phosphate.
This enzyme belongs to the family of transferases, specifically those transferring phosphorus-containing groups (phosphotransferases) with an alcohol group as acceptor. The systematic name of this enzyme class is diphosphate:glycerol 1-phosphotransferase. Other names in common use include PPi-glycerol phosphotransferase, and pyrophosphate-glycerol phosphotransferase.
References.
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14677505
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Diphosphate-purine nucleoside kinase
|
In enzymology, a diphosphate-purine nucleoside kinase (EC 2.7.1.143) is an enzyme that catalyzes the chemical reaction
diphosphate + a purine nucleoside formula_0 phosphate + a purine mononucleotide
Thus, the two substrates of this enzyme are diphosphate and purine nucleoside, whereas its two products are phosphate and purine mononucleotide.
This enzyme belongs to the family of transferases, specifically those transferring phosphorus-containing groups (phosphotransferases) with an alcohol group as acceptor. The systematic name of this enzyme class is diphosphate:purine nucleoside phosphotransferase. This enzyme is also called pyrophosphate-purine nucleoside kinase.
References.
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14677519
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Diphosphate—serine phosphotransferase
|
In enzymology, a diphosphate-serine phosphotransferase (EC 2.7.1.80) is an enzyme that catalyzes the chemical reaction
diphosphate + L-serine formula_0 phosphate + O-phospho-L-serine
Thus, the two substrates of this enzyme are diphosphate and L-serine, whereas its two products are phosphate and O-phospho-L-serine.
This enzyme belongs to the family of transferases, specifically those transferring phosphorus-containing groups (phosphotransferases) with an alcohol group as acceptor. The systematic name of this enzyme class is diphosphate:L-serine O-phosphotransferase. Other names in common use include pyrophosphate-serine phosphotransferase, and pyrophosphate-L-serine phosphotransferase.
References.
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14677547
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Diphosphoinositol-pentakisphosphate kinase
|
In enzymology, a diphosphoinositol-pentakisphosphate kinase (EC 2.7.4.24) is an enzyme that catalyzes the chemical reaction
ATP + 1D-myo-inositol 5-diphosphate pentakisphosphate formula_0 ADP + 1D-myo-inositol bisdiphosphate tetrakisphosphate (isomeric configuration unknown)
Thus, the two substrates of this enzyme are ATP and 1D-myo-inositol 5-diphosphate pentakisphosphate, whereas its 3 products are ADP, 1D-myo-inositol bisdiphosphate tetrakisphosphate and (isomeric configuration unknown).
This enzyme belongs to the family of transferases, specifically those transferring phosphorus-containing groups (phosphotransferases) with a phosphate group as acceptor. The systematic name of this enzyme class is ATP:1D-myo-inositol-5-diphosphate-pentakisphosphate phosphotransferase. Other names in common use include PP-IP5 kinase, diphosphoinositol pentakisphosphate kinase, and ATP:5-diphospho-1D-myo-inositol-pentakisphosphate phosphotransferase.
References.
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14677572
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Dolichol kinase
|
Protein-coding gene in the species Homo sapiens
In enzymology, a dolichol kinase (EC 2.7.1.108) is an enzyme that catalyzes the chemical reaction
CTP + dolichol formula_0 CDP + dolichyl phosphate
Thus, the two substrates of this enzyme are CTP and dolichol, whereas its two products are CDP and dolichyl phosphate.
This enzyme belongs to the family of transferases, to be specific, those transferring phosphorus-containing groups (phosphotransferases) with an alcohol group as acceptor. The systematic name of this enzyme class is CTP:dolichol O-phosphotransferase. This enzyme is also called dolichol phosphokinase. This enzyme participates in "N"-glycan biosynthesis.
In humans dolichol kinase is encoded by the "DOLK" gene.
Function.
Dolichyl monophosphate is an essential glycosyl carrier lipid for C- and O-mannosylation and N-glycosylation of proteins and for biosynthesis of glycosylphosphatidylinositol anchors in endoplasmic reticulum (ER). Dolichol kinase catalyzes CTP-mediated phosphorylation of dolichol, the terminal step in de novo dolichyl monophosphate biosynthesis.
Clinical significance.
Mutations in DOLK cause a subtype of the congenital disorders of glycosylation, DOLK-CDG (CDG-Im).
References.
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Further reading.
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14677595
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Dolichyl-diphosphate—polyphosphate phosphotransferase
|
In enzymology, a dolichyl-diphosphate-polyphosphate phosphotransferase (EC 2.7.4.20) is an enzyme that catalyzes the chemical reaction
dolichyl diphosphate + (phosphate)n formula_0 dolichyl phosphate + (phosphate)n+1
Thus, the two substrates of this enzyme are dolichyl diphosphate and (phosphate)n, whereas its two products are dolichyl phosphate and (phosphate)n+1.
This enzyme belongs to the family of transferases, specifically those transferring phosphorus-containing groups (phosphotransferases) with a phosphate group as acceptor. The systematic name of this enzyme class is dolichyl-diphosphate:polyphosphate phosphotransferase. This enzyme is also called dolichylpyrophosphate:polyphosphate phosphotransferase.
References.
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14677609
|
D-ribitol-5-phosphate cytidylyltransferase
|
InterPro Family
In enzymology, a D-ribitol-5-phosphate cytidylyltransferase (EC 2.7.7.40) is an enzyme that catalyzes the chemical reaction
CTP + D-ribitol 5-phosphate formula_0 diphosphate + CDP-ribitol
Thus, the two substrates of this enzyme are CTP and D-ribitol 5-phosphate, whereas its two products are diphosphate and CDP-ribitol.
This enzyme belongs to the family of transferases, specifically those transferring phosphorus-containing nucleotide groups (nucleotidyltransferases). The systematic name of this enzyme class is CTP:D-ribitol-5-phosphate cytidylyltransferase. Other names in common use include CDP ribitol pyrophosphorylase, cytidine diphosphate ribitol pyrophosphorylase, ribitol 5-phosphate cytidylyltransferase, and cytidine diphosphoribitol pyrophosphorylase. This enzyme participates in pentose and glucuronate interconversions.
References.
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14677631
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D-ribulokinase
|
In enzymology, a D-ribulokinase (EC 2.7.1.47) is an enzyme that catalyzes the chemical reaction
ATP + D-ribulose formula_0 ADP + D-ribulose 5-phosphate
Thus, the two substrates of this enzyme are ATP and D-ribulose, whereas its two products are ADP and D-ribulose 5-phosphate.
This enzyme belongs to the family of transferases, specifically those transferring phosphorus-containing groups (phosphotransferases) with an alcohol group as acceptor. The systematic name of this enzyme class is ATP:D-ribulose 5-phosphotransferase. This enzyme is also called D-ribulokinase (phosphorylating). This enzyme participates in pentose and glucuronate interconversions.
References.
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14677703
|
Elongation factor 2 kinase
|
In enzymology, an elongation factor 2 kinase (EC 2.7.11.20) is an enzyme that catalyzes the chemical reaction:
ATP + [elongation factor 2] formula_0 ADP + [elongation factor 2] phosphate.
Thus, the two substrates of this enzyme are ATP and elongation factor 2, whereas its two products are adenosine diphosphate (ADP) and elongation factor 2 phosphate.
Nomenclature.
This enzyme belongs to the family of transferases, specifically those transferring a phosphate group to the sidechain oxygen atom of serine or threonine residues in proteins (protein-serine/threonine kinases). The systematic name of this enzyme class is "ATP:[elongation factor 2] phosphotransferase". Other names in common use include Ca/CaM-kinase III, calmodulin-dependent protein kinase III, CaM kinase III, eEF2 kinase, eEF-2K, eEF2K, EF2K, and STK19.
Function.
The only known physiological substrate of eEF-2K is eEF-2. Phosphorylation of eEF-2 at Thr-56 by eEF-2K leads to inhibition of the elongation phase of protein synthesis. Phosphorylation of Thr-56 is thought to reduce the affinity of eEF-2 for the ribosome, thereby slowing down the overall rate of elongation. However, there is growing evidence to suggest that translation of certain mRNAs is actually increased by phosphorylation of eEF-2 by eEF-2K, especially in a neuronal context.
Activation.
The activity of eEF-2K is dependent on calcium and calmodulin. Activation of eEF-2K proceeds by a sequential two-step mechanism. First, calcium-calmodulin binds with high affinity to activate the kinase domain, triggering rapid autophosphorylation of Thr-348. In the second step, autophosphorylation of Thr-348 leads to a conformational change in the kinase likely supported by the binding of phospho-Thr-348 to an allosteric phosphate binding pocket in the kinase domain. This increases the activity of eEF-2K against its substrate, elongation factor 2.
eEF-2K can gain calcium-independent activity through autophosphorylation of Ser-500. However, calmodulin must remain bound to the enzyme for its activity to be sustained.
Cancer.
eEF-2K expression is often upregulated in cancer cells, including breast and pancreatic cancers and promotes cell proliferation, survival, motility/migration, invasion and tumorigenesis.
References.
<templatestyles src="Reflist/styles.css" />
Further reading.
<templatestyles src="Refbegin/styles.css" />
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[
{
"math_id": 0,
"text": "\\rightleftharpoons"
}
] |
https://en.wikipedia.org/wiki?curid=14677703
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14677732
|
Erythritol kinase
|
In enzymology, an erythritol kinase (EC 2.7.1.27) is an enzyme that catalyzes the chemical reaction
ATP + erythritol formula_0 ADP + D-erythritol 4-phosphate
Thus, the two substrates of this enzyme are ATP and erythritol, whereas its two products are ADP and D-erythritol 4-phosphate.
This enzyme belongs to the family of transferases, specifically those transferring phosphorus-containing groups (phosphotransferases) with an alcohol group as acceptor. The systematic name of this enzyme class is ATP:erythritol 4-phosphotransferase. This enzyme is also called erythritol kinase (phosphorylating).
Structural studies.
As of late 2007, only one structure has been solved for this class of enzymes, with the PDB accession code 1V5S.
References.
<templatestyles src="Reflist/styles.css" />
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[
{
"math_id": 0,
"text": "\\rightleftharpoons"
}
] |
https://en.wikipedia.org/wiki?curid=14677732
|
14677772
|
Ethanolamine kinase
|
In enzymology, an ethanolamine kinase (EC 2.7.1.82) is an enzyme that catalyzes the chemical reaction
ATP + ethanolamine formula_0 ADP + O-phosphoethanolamine
Thus, the two substrates of this enzyme are ATP and ethanolamine, whereas its two products are ADP and O-phosphoethanolamine.
This enzyme belongs to the family of transferases, specifically those transferring phosphorus-containing groups (phosphotransferases) with an alcohol group as acceptor. The systematic name of this enzyme class is ATP:ethanolamine O-phosphotransferase. Other names in common use include ethanolamine kinase (phosphorylating), and ethanolamine phosphokinase. This enzyme participates in glycerophospholipid metabolism.
References.
<templatestyles src="Reflist/styles.css" />
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[
{
"math_id": 0,
"text": "\\rightleftharpoons"
}
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https://en.wikipedia.org/wiki?curid=14677772
|
14677790
|
Ethanolamine-phosphate cytidylyltransferase
|
In enzymology, an ethanolamine-phosphate cytidylyltransferase (EC 2.7.7.14) is an enzyme that catalyzes the chemical reaction
CTP + ethanolamine phosphate formula_0 diphosphate + CDP-ethanolamine
Thus, the two substrates of this enzyme are CTP and ethanolamine phosphate, whereas its two products are diphosphate and CDP-ethanolamine.
This enzyme belongs to the family of transferases, specifically those transferring phosphorus-containing nucleotide groups (nucleotidyltransferases). The systematic name of this enzyme class is CTP:ethanolamine-phosphate cytidylyltransferase. Other names in common use include phosphorylethanolamine transferase, ET, CTP-phosphoethanolamine cytidylyltransferase, phosphoethanolamine cytidylyltransferase, and ethanolamine phosphate cytidylyltransferase. This enzyme participates in aminophosphonate metabolism and glycerophospholipid metabolism.
References.
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[
{
"math_id": 0,
"text": "\\rightleftharpoons"
}
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https://en.wikipedia.org/wiki?curid=14677790
|
14677811
|
Diacylglycerol ethanolaminephosphotransferase
|
Class of enzymes
In enzymology, an ethanolaminephosphotransferase (EC 2.7.8.1) is an enzyme that catalyzes the chemical reaction
CDP-ethanolamine + 1,2-diacylglycerol formula_0 CMP + a phosphatidylethanolamine
Thus, the two substrates of this enzyme are CDP-ethanolamine and 1,2-diacylglycerol, whereas its two products are CMP and phosphatidylethanolamine.
This enzyme belongs to the family of transferases, specifically those transferring non-standard substituted phosphate groups. The systematic name of this enzyme class is CDP-ethanolamine:1,2-diacylglycerol ethanolaminephosphotransferase. Other names in common use include EPT, diacylglycerol ethanolaminephosphotransferase, CDPethanolamine diglyceride phosphotransferase, and phosphorylethanolamine-glyceride transferase. This enzyme participates in 3 metabolic pathways: aminophosphonate metabolism, glycerophospholipid metabolism, and ether lipid metabolism.
References.
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[
{
"math_id": 0,
"text": "\\rightleftharpoons"
}
] |
https://en.wikipedia.org/wiki?curid=14677811
|
14677837
|
Farnesyl-diphosphate kinase
|
In enzymology, a farnesyl-diphosphate kinase (EC 2.7.4.18) is an enzyme that catalyzes the chemical reaction
ATP + farnesyl diphosphate formula_0 ADP + farnesyl triphosphate
Thus, the two substrates of this enzyme are ATP and farnesyl diphosphate, whereas its two products are ADP and farnesyl triphosphate.
This enzyme belongs to the family of transferases, specifically those transferring phosphorus-containing groups (phosphotransferases) with a phosphate group as acceptor. The systematic name of this enzyme class is ATP:farnesyl-diphosphate phosphotransferase. This enzyme is also called farnesyl pyrophosphate kinase.
References.
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[
{
"math_id": 0,
"text": "\\rightleftharpoons"
}
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https://en.wikipedia.org/wiki?curid=14677837
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14677870
|
FMN adenylyltransferase
|
In enzymology, a FMN adenylyltransferase (EC 2.7.7.2) is an enzyme that catalyzes the chemical reaction
ATP + FMN formula_0 diphosphate + FAD
Thus, the two substrates of this enzyme are ATP and FMN, whereas its two products are diphosphate and FAD.
This enzyme belongs to the family of transferases, specifically those transferring phosphorus-containing nucleotide groups (nucleotidyltransferases). The systematic name of this enzyme class is ATP:FMN adenylyltransferase. This enzyme participates in riboflavin metabolism.
Other names.
Other names in common use include
References.
<templatestyles src="Reflist/styles.css" />
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[
{
"math_id": 0,
"text": "\\rightleftharpoons"
}
] |
https://en.wikipedia.org/wiki?curid=14677870
|
14677898
|
Formate kinase
|
Class of enzymes
In enzymology, a formate kinase (EC 2.7.2.6) is an enzyme that catalyzes the chemical reaction
ATP + formate formula_0 ADP + formyl phosphate
Thus, the two substrates of this enzyme are ATP and formate, whereas its two products are ADP and formyl phosphate.
This enzyme belongs to the family of transferases, specifically those transferring phosphorus-containing groups (phosphotransferases) with a carboxy group as acceptor. The systematic name of this enzyme class is ATP:formate phosphotransferase. This enzyme participates in glyoxylate and dicarboxylate metabolism.
References.
<templatestyles src="Reflist/styles.css" />
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[
{
"math_id": 0,
"text": "\\rightleftharpoons"
}
] |
https://en.wikipedia.org/wiki?curid=14677898
|
14677925
|
Fucokinase
|
In enzymology, a fucokinase (EC 2.7.1.52) is an enzyme that catalyzes the chemical reaction
ATP + L-fucose formula_0 ADP + beta-L-fucose 1-phosphate
Thus, the two substrates of this enzyme are ATP and L-fucose, whereas its two products are ADP and beta-L-fucose 1-phosphate.
This enzyme belongs to the family of transferases, specifically those transferring phosphorus-containing groups (phosphotransferases) with an alcohol group as acceptor. The systematic name of this enzyme class is ATP:beta-L-fucose 1-phosphotransferase. Other names in common use include fucokinase (phosphorylating), fucose kinase, L-fucose kinase, L-fucokinase, ATP:6-deoxy-L-fucose 1-phosphotransferase, and ATP:L-fucose 1-phosphotransferase. Fucokinase is commonly abbreviated as fuc-K. This enzyme participates in fructose and mannose metabolism. Fucokinase is the only enzyme that is converting L-fucose to fucose-1-phosphate and it can be further used for synthesizing GDP-fucose, which is the donor substrate for all fucosyltransferase.
L-Fucokinase activity can be detected in varied tissues within an animal. For instance, rats and mice contain L-fucokinase widely distributed throughout tissues especially higher in the brain. However, the levels of L-fucokinase in the brain is widely different among species.
References.
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[
{
"math_id": 0,
"text": "\\rightleftharpoons"
}
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https://en.wikipedia.org/wiki?curid=14677925
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14677947
|
Fucose-1-phosphate guanylyltransferase
|
In enzymology, a fucose-1-phosphate guanylyltransferase (EC 2.7.7.30) is an enzyme that catalyzes the chemical reaction
GTP + beta-L-fucose 1-phosphate formula_0 diphosphate + GDP-L-fucose
Thus, the two substrates of this enzyme are GTP and beta-L-fucose 1-phosphate, whereas its two products are diphosphate and GDP-L-fucose.
This enzyme belongs to the family of transferases, specifically those transferring phosphorus-containing nucleotide groups (nucleotidyltransferases). The systematic name of this enzyme class is GTP:beta-L-fucose-1-phosphate guanylyltransferase. Other names in common use include GDP fucose pyrophosphorylase, guanosine diphosphate L-fucose pyrophosphorylase, GDP-L-fucose pyrophosphorylase, GDP-fucose pyrophosphorylase, and GTP:L-fucose-1-phosphate guanylyltransferase. This enzyme participates in fructose and mannose metabolism.
References.
<templatestyles src="Reflist/styles.css" />
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[
{
"math_id": 0,
"text": "\\rightleftharpoons"
}
] |
https://en.wikipedia.org/wiki?curid=14677947
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14677971
|
Galactose-1-phosphate thymidylyltransferase
|
In enzymology, a galactose-1-phosphate thymidylyltransferase (EC 2.7.7.32) is an enzyme that catalyzes the chemical reaction
dTTP + alpha-D-galactose 1-phosphate formula_0 diphosphate + dTDP-galactose
Thus, the two substrates of this enzyme are dTTP and alpha-D-galactose 1-phosphate, whereas its two products are diphosphate and dTDP-galactose.
This enzyme belongs to the family of transferases, specifically those transferring phosphorus-containing nucleotide groups (nucleotidyltransferases). The systematic name of this enzyme class is dTTP:alpha-D-galactose-1-phosphate thymidylyltransferase. Other names in common use include dTDP galactose pyrophosphorylase, galactose 1-phosphate thymidylyl transferase, thymidine diphosphogalactose pyrophosphorylase, thymidine triphosphate:alpha-D-galactose 1-phosphate, and thymidylyltransferase. This enzyme participates in nucleotide sugars metabolism.
References.
<templatestyles src="Reflist/styles.css" />
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[
{
"math_id": 0,
"text": "\\rightleftharpoons"
}
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https://en.wikipedia.org/wiki?curid=14677971
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14677998
|
Galacturonokinase
|
In enzymology, a galacturonokinase (EC 2.7.1.44) is an enzyme that catalyzes the chemical reaction
ATP + D-galacturonate formula_0 ADP + 1-phospho-alpha-D-galacturonate
Thus, the two substrates of this enzyme are ATP and D-galacturonate, whereas its two products are ADP and 1-phospho-alpha-D-galacturonate.
This enzyme belongs to the family of transferases, specifically those transferring phosphorus-containing groups (phosphotransferases) with an alcohol group as acceptor. The systematic name of this enzyme class is ATP:D-galacturonate 1-phosphotransferase. This enzyme is also called galacturonokinase (phosphorylating) D-galacturonic acid kinase. This enzyme participates in nucleotide sugars metabolism.
References.
<templatestyles src="Reflist/styles.css" />
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[
{
"math_id": 0,
"text": "\\rightleftharpoons"
}
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https://en.wikipedia.org/wiki?curid=14677998
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14678026
|
Gentamicin 2"-nucleotidyltransferase
|
In enzymology, a gentamicin 2"-nucleotidyltransferase (EC 2.7.7.46) is an enzyme that catalyzes the chemical reaction
nucleoside triphosphate + gentamicin formula_0 diphosphate + 2"-nucleotidylgentamicin
Thus, the two substrates of this enzyme are nucleoside triphosphate and gentamicin, whereas its two products are diphosphate and 2"-nucleotidylgentamicin.
This enzyme belongs to the family of transferases, specifically those transferring phosphorus-containing nucleotide groups (nucleotidyltransferases). The systematic name of this enzyme class is NTP:gentamicin 2"-nucleotidyltransferase. Other names in common use include gentamicin 2"-adenylyltransferase, aminoglycoside adenylyltransferase, and gentamicin 2"-nucleotidyltransferase.
References.
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[
{
"math_id": 0,
"text": "\\rightleftharpoons"
}
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https://en.wikipedia.org/wiki?curid=14678026
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14678045
|
Gluconokinase
|
In enzymology, a gluconokinase (EC 2.7.1.12) is an enzyme that catalyzes the chemical reaction
ATP + D-gluconate formula_0 ADP + 6-phospho-D-gluconate
Thus, the two substrates of this enzyme are ATP and D-gluconate, whereas its two products are ADP and 6-phospho-D-gluconate.
This enzyme belongs to the family of transferases, specifically those transferring phosphorus-containing groups (phosphotransferases) with an alcohol group as acceptor. The systematic name of this enzyme class is ATP:D-gluconate 6-phosphotransferase. Other names in common use include gluconokinase (phosphorylating), and gluconate kinase. This enzyme participates in pentose phosphate pathway.
Structural studies.
As of late 2007, 6 structures have been solved for this class of enzymes, with PDB accession codes 1KNQ, 1KO1, 1KO4, 1KO5, 1KO8, and 1KOF.
References.
<templatestyles src="Reflist/styles.css" />
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[
{
"math_id": 0,
"text": "\\rightleftharpoons"
}
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https://en.wikipedia.org/wiki?curid=14678045
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14678074
|
Glucosamine kinase
|
In enzymology, a glucosamine kinase (EC 2.7.1.8) is an enzyme that catalyzes the chemical reaction
ATP + D-glucosamine formula_0 ADP + D-glucosamine phosphate
Thus, the two substrates of this enzyme are ATP and D-glucosamine, whereas its two products are ADP and D-glucosamine phosphate.
This enzyme belongs to the family of transferases, specifically those transferring phosphorus-containing groups (phosphotransferases) with an alcohol group as acceptor. The systematic name of this enzyme class is ATP:D-glucosamine phosphotransferase. Other names in common use include glucosamine kinase (phosphorylating), ATP:2-amino-2-deoxy-D-glucose-6-phosphotransferase, and aminodeoxyglucose kinase. This enzyme participates in aminosugars metabolism.
References.
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[
{
"math_id": 0,
"text": "\\rightleftharpoons"
}
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https://en.wikipedia.org/wiki?curid=14678074
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14678093
|
Glucose-1-phosphate adenylyltransferase
|
In enzymology, a glucose-1-phosphate adenylyltransferase (EC 2.7.7.27) is an enzyme that catalyzes the chemical reaction
ATP + alpha-D-glucose 1-phosphate formula_0 diphosphate + ADP-glucose
Thus, the two substrates of this enzyme are ATP and alpha-D-glucose 1-phosphate, whereas its two products are diphosphate and ADP-glucose.
This enzyme belongs to the family of transferases, specifically those transferring phosphorus-containing nucleotide groups (nucleotidyltransferases). The systematic name of this enzyme class is ATP:alpha-D-glucose-1-phosphate adenylyltransferase. Other names in common use include ADP glucose pyrophosphorylase, glucose 1-phosphate adenylyltransferase, adenosine diphosphate glucose pyrophosphorylase, adenosine diphosphoglucose pyrophosphorylase, ADP-glucose pyrophosphorylase, ADP-glucose synthase, ADP-glucose synthetase, ADPG pyrophosphorylase, ADP:alpha-D-glucose-1-phosphate adenylyltransferase and AGPase.
This enzyme participates in starch and sucrose metabolism and glycogen metabolism in bacteria. The rate limiting step in their synthesis appears to be regulated at the level of this enzyme. In many species glycolytic intermediates act to stimulate enzyme activity while AMP or phosphate inhibit enzyme activity.
In contrast, in many animals, the synthesis of alpha 1,4 glucans (glycogen) uses UDP-glucose as a glucose donor. In this case, the regulated step is instead the glycosyl transferase.
Structural studies.
As of late 2007, 3 structures have been solved for this class of enzymes, with PDB accession codes 1YP2, 1YP3, and 1YP4.
References.
<templatestyles src="Reflist/styles.css" />
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[
{
"math_id": 0,
"text": "\\rightleftharpoons"
}
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https://en.wikipedia.org/wiki?curid=14678093
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14678113
|
Glucose-1-phosphate cytidylyltransferase
|
In enzymology, a glucose-1-phosphate cytidylyltransferase (EC 2.7.7.33) is an enzyme that catalyzes the chemical reaction
CTP + alpha-D-glucose 1-phosphate formula_0 diphosphate + CDP-glucose
Thus, the two substrates of this enzyme are CTP and alpha-D-glucose 1-phosphate, whereas its two products are diphosphate and CDP-glucose.
This enzyme belongs to the family of transferases, specifically those transferring phosphorus-containing nucleotide groups (nucleotidyltransferases). The systematic name of this enzyme class is CTP:alpha-D-glucose-1-phosphate cytidylyltransferase. Other names in common use include CDP glucose pyrophosphorylase, cytidine diphosphoglucose pyrophosphorylase, cytidine diphosphate glucose pyrophosphorylase, cytidine diphosphate-D-glucose pyrophosphorylase, and CTP:D-glucose-1-phosphate cytidylyltransferase. This enzyme participates in starch and sucrose metabolism and nucleotide sugars metabolism.
Structural studies.
As of late 2007, two structures have been solved for this class of enzymes, with PDB accession codes 1TZF and 1WVC.
References.
<templatestyles src="Reflist/styles.css" />
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[
{
"math_id": 0,
"text": "\\rightleftharpoons"
}
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https://en.wikipedia.org/wiki?curid=14678113
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14678132
|
Glucose-1-phosphate guanylyltransferase
|
In enzymology, a glucose-1-phosphate guanylyltransferase (EC 2.7.7.34) is an enzyme that catalyzes the chemical reaction
GTP + alpha-D-glucose 1-phosphate formula_0 diphosphate + GDP-glucose
Thus, the two substrates of this enzyme are GTP and alpha-D-glucose 1-phosphate, whereas its two products are diphosphate and GDP-glucose.
This enzyme belongs to the family of transferases, specifically those transferring phosphorus-containing nucleotide groups (nucleotidyltransferases). The systematic name of this enzyme class is GTP:alpha-D-glucose-1-phosphate guanylyltransferase. Other names in common use include GDP glucose pyrophosphorylase, and guanosine diphosphoglucose pyrophosphorylase. This enzyme participates in starch and sucrose metabolism.
References.
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[
{
"math_id": 0,
"text": "\\rightleftharpoons"
}
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https://en.wikipedia.org/wiki?curid=14678132
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1467815
|
Computational indistinguishability
|
In computer science, relationship between two families of distributions
In computational complexity and cryptography, two families of distributions are computationally indistinguishable if no efficient algorithm can tell the difference between them except with negligible probability.
Formal definition.
Let formula_0 and formula_1 be two distribution ensembles indexed by a security parameter "n" (which usually refers to the length of the input); we say they are computationally indistinguishable if for any non-uniform probabilistic polynomial time algorithm "A", the following quantity is a negligible function in "n":
formula_2
denoted formula_3. In other words, every efficient algorithm "A"'s behavior does not significantly change when given samples according to "D""n" or "E""n" in the limit as formula_4. Another interpretation of computational indistinguishability, is that polynomial-time algorithms actively trying to distinguish between the two ensembles cannot do so: that any such algorithm will only perform negligibly better than if one were to just guess.
Related notions.
Implicit in the definition is the condition that the algorithm, formula_5, must decide based on a single sample from one of the distributions. One might conceive of a situation in which the algorithm trying to distinguish between two distributions, could access as many samples as it needed. Hence two ensembles that cannot be distinguished by polynomial-time algorithms looking at multiple samples are deemed indistinguishable by polynomial-time sampling. If the polynomial-time algorithm can generate samples in polynomial time, or has access to a random oracle that generates samples for it, then indistinguishability by polynomial-time sampling is equivalent to computational indistinguishability.
External links.
"This article incorporates material from computationally indistinguishable on PlanetMath, which is licensed under the ."
|
[
{
"math_id": 0,
"text": "\\scriptstyle\\{ D_n \\}_{n \\in \\mathbb{N}}"
},
{
"math_id": 1,
"text": "\\scriptstyle\\{ E_n \\}_{n \\in \\mathbb{N}}"
},
{
"math_id": 2,
"text": "\\delta(n) = \\left| \\Pr_{x \\gets D_n}[ A(x) = 1] - \\Pr_{x \\gets E_n}[ A(x) = 1] \\right|."
},
{
"math_id": 3,
"text": "D_n \\approx E_n"
},
{
"math_id": 4,
"text": "n\\to \\infty"
},
{
"math_id": 5,
"text": "A"
}
] |
https://en.wikipedia.org/wiki?curid=1467815
|
14678169
|
Glucose-1-phosphate thymidylyltransferase
|
In enzymology, a glucose-1-phosphate thymidylyltransferase (EC 2.7.7.24) is an enzyme that catalyzes the chemical reaction
dTTP + alpha--glucose 1-phosphate formula_0 diphosphate + dTDP-glucose
Thus, the two substrates of this enzyme are dTTP and alpha--glucose 1-phosphate, whereas its two products are pyrophosphate and dTDP-glucose.
This enzyme belongs to the family of transferases, to be specific, those transferring phosphorus-containing nucleotide groups (nucleotidyltransferases). This enzyme participates in 3 metabolic pathways: nucleotide sugars metabolism, streptomycin biosynthesis, and polyketide sugar unit biosynthesis.
Nomenclature.
The systematic name of this enzyme class is dTTP:alpha--glucose-1-phosphate thymidylyltransferase. Other names in common use include:
Structural studies.
As of late 2007, 19 structures have been solved for this class of enzymes, with PDB accession codes 1FXO, 1FZW, 1G0R, 1G1L, 1G23, 1G2V, 1G3L, 1H5R, 1H5S, 1H5T, 1IIM, 1IIN, 1LVW, 1MC3, 1MP3, 1MP4, 1MP5, 2GGO, and 2GGQ.
References.
<templatestyles src="Reflist/styles.css" />
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[
{
"math_id": 0,
"text": "\\rightleftharpoons"
}
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https://en.wikipedia.org/wiki?curid=14678169
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14678188
|
Glucuronate-1-phosphate uridylyltransferase
|
In enzymology, a glucuronate-1-phosphate uridylyltransferase (EC 2.7.7.44) is an enzyme that catalyzes the chemical reaction
UTP + 1-phospho-alpha-D-glucuronate formula_0 diphosphate + UDP-glucuronate
Thus, the two substrates of this enzyme are UTP and 1-phospho-alpha-D-glucuronate, whereas its two products are diphosphate and UDP-glucuronate.
This enzyme belongs to the family of transferases, specifically those transferring phosphorus-containing nucleotide groups (nucleotidyltransferases). The systematic name of this enzyme class is UTP:1-phospho-alpha-D-glucuronate uridylyltransferase. Other names in common use include UDP-glucuronate pyrophosphorylase, UDP-D-glucuronic acid pyrophosphorylase, UDP-glucuronic acid pyrophosphorylase, and uridine diphosphoglucuronic pyrophosphorylase. This enzyme participates in pentose and glucuronate interconversions and ascorbate and aldarate metabolism.
References.
<templatestyles src="Reflist/styles.css" />
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[
{
"math_id": 0,
"text": "\\rightleftharpoons"
}
] |
https://en.wikipedia.org/wiki?curid=14678188
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14678204
|
Glucuronokinase
|
In enzymology, a glucuronokinase (EC 2.7.1.43) is an enzyme that catalyzes the chemical reaction
ATP + D-glucuronate formula_0 ADP + 1-phospho-alpha-D-glucuronate
Thus, the two substrates of this enzyme are ATP and D-glucuronate, whereas its two products are ADP and 1-phospho-alpha-D-glucuronate.
This enzyme belongs to the family of transferases, specifically those transferring phosphorus-containing groups (phosphotransferases) with an alcohol group as acceptor. The systematic name of this enzyme class is ATP:D-glucuronate 1-phosphotransferase. Other names in common use include glucuronokinase (phosphorylating), and glucurono-glucuronokinase. This enzyme participates in pentose and glucuronate interconversions and ascorbate and aldarate metabolism.
References.
<templatestyles src="Reflist/styles.css" />
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[
{
"math_id": 0,
"text": "\\rightleftharpoons"
}
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https://en.wikipedia.org/wiki?curid=14678204
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14678233
|
Glutamate 1-kinase
|
Enzyme
In enzymology, a glutamate 1-kinase (EC 2.7.2.13) is an enzyme that catalyzes the chemical reaction
ATP + L-glutamate formula_0 ADP + alpha-L-glutamyl phosphate
Thus, the two substrates of this enzyme are ATP and L-glutamate, whereas its two products are ADP and alpha-L-glutamyl phosphate.
This enzyme belongs to the family of transferases, specifically those transferring phosphorus-containing groups (phosphotransferases) with a carboxy group as acceptor. The systematic name of this enzyme class is ATP:L-glutamate 1-phosphotransferase.
References.
<templatestyles src="Reflist/styles.css" />
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[
{
"math_id": 0,
"text": "\\rightleftharpoons"
}
] |
https://en.wikipedia.org/wiki?curid=14678233
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14678267
|
Glutamate 5-kinase
|
Enzyme
In enzymology, a glutamate 5-kinase (EC 2.7.2.11) is an enzyme that catalyzes the chemical reaction
ATP + L-glutamate formula_0 ADP + L-glutamate 5-phosphate
Thus, the two substrates of this enzyme are ATP and L-glutamate, whereas its two products are ADP and L-glutamate 5-phosphate.
This enzyme belongs to the family of transferases, specifically those transferring phosphorus-containing groups (phosphotransferases) with a carboxy group as acceptor. The systematic name of this enzyme class is ATP:L-glutamate 5-phosphotransferase. Other names in common use include ATP-L-glutamate 5-phosphotransferase, ATP:gamma-L-glutamate phosphotransferase, gamma-glutamate kinase, gamma-glutamyl kinase, and glutamate kinase. This enzyme participates in urea cycle and metabolism of amino groups.
Structural studies.
As of late 2007, 3 structures have been solved for this class of enzymes, with PDB accession codes 2AKO, 2J5T, and 2J5V.
References.
<templatestyles src="Reflist/styles.css" />
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[
{
"math_id": 0,
"text": "\\rightleftharpoons"
}
] |
https://en.wikipedia.org/wiki?curid=14678267
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14678293
|
(glutamate—ammonia-ligase) adenylyltransferase
|
Class of enzymes
In enzymology, a [glutamate—ammonia-ligase] adenylyltransferase (EC 2.7.7.42) is an enzyme that catalyzes the chemical reaction
ATP + [L-glutamate:ammonia ligase (ADP-forming)] formula_0 diphosphate + adenylyl-[L-glutamate:ammonia ligase (ADP-forming)]
Thus, the two substrates of this enzyme are ATP and , whereas its two products are diphosphate and ].
This enzyme belongs to the family of transferases, specifically those transferring phosphorus-containing nucleotide groups (nucleotidyltransferases). The systematic name of this enzyme class is ATP:[L-glutamate:ammonia ligase (ADP-forming)] adenylyltransferase. Other names in common use include glutamine-synthetase adenylyltransferase, ATP:glutamine synthetase adenylyltransferase, and adenosine triphosphate:glutamine synthetase adenylyltransferase.
Structural studies.
As of late 2007, only one structure has been solved for this class of enzymes, with the PDB accession code 1V4A.
References.
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{
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https://en.wikipedia.org/wiki?curid=14678293
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14678310
|
Glycerate kinase
|
In enzymology, a glycerate kinase (EC 2.7.1.31) is an enzyme that catalyzes the chemical reaction
ATP + (R)-glycerate formula_0 ADP + 3-phospho-(R)-glycerate
or
ATP + (R)-glycerate formula_0 ADP + 2-phospho-(R)-glycerate
Thus, the two substrates of this enzyme are ATP and (R)-glycerate, whereas its two products are ADP and either 3-phospho-(R)-glycerate or 2-phospho-(R)-glycerate.
This enzyme belongs to the family of transferases, specifically those transferring phosphorus-containing groups (phosphotransferases) with an alcohol group as acceptor. The systematic name of this enzyme class is ATP:(R)-glycerate 3-phosphotransferase. Other names in common use include glycerate kinase (phosphorylating), D-glycerate 3-kinase, D-glycerate kinase, glycerate-3-kinase, GK, D-glyceric acid kinase, and ATP:D-glycerate 2-phosphotransferase. This enzyme participates in 3 metabolic pathways: serine/glycine/threonine metabolism, glycerolipid metabolism, and glyoxylate-dicarboxylate metabolism.
This enzyme had been thought to produce 3-phosphoglycerate, but some glycerate kinases produce 2-phosphoglycerate instead.
Structural studies.
As of late 2007, 3 structures have been solved for this class of enzymes, with PDB accession codes 1TO6, 1X3L, and 2B8N.
References.
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https://en.wikipedia.org/wiki?curid=14678310
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14678327
|
Glycerol-3-phosphate cytidylyltransferase
|
In enzymology, a glycerol-3-phosphate cytidylyltransferase (EC 2.7.7.39) is an enzyme that catalyzes the chemical reaction
CTP + sn-glycerol 3-phosphate formula_0 diphosphate + CDP-glycerol
Thus, the two substrates of this enzyme are CTP and sn-glycerol 3-phosphate, whereas its two products are diphosphate and CDP-glycerol.
This enzyme belongs to the family of transferases, specifically those transferring phosphorus-containing nucleotide groups (nucleotidyltransferases). The systematic name of this enzyme class is CTP:sn-glycerol-3-phosphate cytidylyltransferase. Other names in common use include CDP-glycerol pyrophosphorylase, cytidine diphosphoglycerol pyrophosphorylase, cytidine diphosphate glycerol pyrophosphorylase, CTP:glycerol 3-phosphate cytidylyltransferase, and Gro-PCT. This enzyme participates in glycerophospholipid metabolism.
Structural studies.
As of late 2007, 3 structures have been solved for this class of enzymes, with PDB accession codes 1COZ, 1N1D, and 2B7L.
References.
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{
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https://en.wikipedia.org/wiki?curid=14678327
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14678346
|
Glycerol-3-phosphate—glucose phosphotransferase
|
In enzymology, a glycerol-3-phosphate-glucose phosphotransferase (EC 2.7.1.142) is an enzyme that catalyzes the chemical reaction
sn-glycerol 3-phosphate + D-glucose formula_0 glycerol + D-glucose 6-phosphate
Thus, the two substrates of this enzyme are sn-glycerol 3-phosphate and D-glucose, whereas its two products are glycerol and D-glucose 6-phosphate.
This enzyme belongs to the family of transferases, specifically those transferring phosphorus-containing groups (phosphotransferases) with an alcohol group as acceptor. The systematic name of this enzyme class is sn-glycerol-3-phosphate:D-glucose 6-phosphotransferase.
References.
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{
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https://en.wikipedia.org/wiki?curid=14678346
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14678382
|
Glycerone kinase
|
In enzymology, a glycerone kinase (EC 2.7.1.29) is an enzyme that catalyzes the chemical reaction
ATP + glycerone formula_0 ADP + glycerone phosphate
Thus, the two substrates of this enzyme are ATP and glycerone, whereas its two products are ADP and glycerone phosphate.
This enzyme belongs to the family of transferases, specifically those transferring phosphorus-containing groups (phosphotransferases) with an alcohol group as acceptor. The systematic name of this enzyme class is ATP:glycerone phosphotransferase. Other names in common use include dihydroxyacetone kinase, acetol kinase, and acetol kinase (phosphorylating). This enzyme participates in glycerolipid metabolism.
Structural studies.
As of late 2007, 6 structures have been solved for this class of enzymes, with PDB accession codes 1OI2, 1OI3, 1UN8, 1UN9, 1UOD, and 1UOE.
References.
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https://en.wikipedia.org/wiki?curid=14678382
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14678412
|
Goodpasture-antigen-binding protein kinase
|
In enzymology, a Goodpasture-antigen-binding protein kinase (EC 2.7.11.9) is an enzyme that catalyzes the chemical reaction
ATP + Goodpasture antigen-binding protein formula_0 ADP + [Goodpasture antigen-binding phosphoprotein]
Thus, the two substrates of this enzyme are ATP and Goodpasture antigen-binding protein, whereas its two products are ADP and Goodpasture antigen-binding phosphoprotein.
This enzyme belongs to the family of transferases, specifically those transferring a phosphate group to the sidechain oxygen atom of serine or threonine residues in proteins (protein-serine/threonine kinases). The systematic name of this enzyme class is ATP:[Goodpasture antigen-binding protein] phosphotransferase. Other names in common use include GPBPK, GPBP kinase, STK11, and Goodpasture antigen-binding protein kinase. This enzyme participates in mTOR signaling pathway and adipocytokine signaling pathway.
References.
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14678431
|
GTP diphosphokinase
|
Class of enzymes
In enzymology, a GTP diphosphokinase (EC 2.7.6.5) is an enzyme that catalyzes the chemical reaction
ATP + GTP formula_0 AMP + guanosine 3'-diphosphate 5'-triphosphate
Thus, the two substrates of this enzyme are ATP and GTP, whereas its two products are AMP and guanosine 3'-diphosphate 5'-triphosphate.
This enzyme belongs to the family of transferases, specifically those transferring two phosphorus-containing groups (diphosphotransferases). The systematic name of this enzyme class is ATP:GTP 3'-diphosphotransferase. Other names in common use include stringent factor, guanosine 3',5'-polyphosphate synthase, GTP pyrophosphokinase, ATP-GTP 3'-diphosphotransferase, guanosine 5',3'-polyphosphate synthetase, (p)ppGpp synthetase I, (p)ppGpp synthetase II, guanosine pentaphosphate synthetase, GPSI, and GPSII. This enzyme participates in purine metabolism.
Structural studies.
As of late 2007, 4 structures have been solved for this class of enzymes, with PDB accession codes 1E3H, 1E3P, 1VJ7, and 2BE3.
References.
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https://en.wikipedia.org/wiki?curid=14678431
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14678456
|
Guanidinoacetate kinase
|
In enzymology, a guanidinoacetate kinase (EC 2.7.3.1) is an enzyme that catalyzes the chemical reaction
ATP + guanidinoacetate formula_0 ADP + phosphoguanidinoacetate
Thus, the two substrates of this enzyme are ATP and guanidinoacetate, whereas its two products are ADP and phosphoguanidinoacetate.
Guanidinoacetate kinase belongs to the family of transferases, specifically those that transfer phosphorus-containing groups (phosphotransferases) with a nitrogenous group as acceptor. The systematic name of this enzyme class is ATP:guanidinoacetate N-phosphotransferase. This enzyme is also called glycocyamine kinase. This enzyme participates in arginine and proline metabolism.
References.
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14678474
|
Guanosine-triphosphate guanylyltransferase
|
In enzymology, a guanosine-triphosphate guanylyltransferase (EC 2.7.7.45) is an enzyme that catalyzes the chemical reaction
2 GTP formula_0 diphosphate + P1,P4-bis(5'-guanosyl) tetraphosphate
Hence, this enzyme has one substrate, GTP, and two products, diphosphate and P1,P4-bis(5'-guanosyl) tetraphosphate.
This enzyme belongs to the family of transferases, specifically those transferring phosphorus-containing nucleotide groups (nucleotidyltransferases). The systematic name of this enzyme class is GTP:GTP guanylyltransferase. Other names in common use include diguanosine tetraphosphate synthetase, GTP-GTP guanylyltransferase, Gp4G synthetase, and guanosine triphosphate-guanose triphosphate guanylyltransferase.
References.
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https://en.wikipedia.org/wiki?curid=14678474
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14678502
|
Guanylate kinase
|
Enzyme
In enzymology, a guanylate kinase (EC 2.7.4.8) is an enzyme that catalyzes the chemical reaction
ATP + GMP formula_0 ADP + GDP
Thus, the two substrates of this enzyme are ATP and GMP, whereas its two products are ADP and GDP.
This enzyme belongs to the family of transferases, specifically those transferring phosphorus-containing groups (phosphotransferases) with a phosphate group as acceptor. This enzyme participates in purine metabolism.
Guanylate kinase catalyzes the ATP-dependent phosphorylation of GMP into GDP. It is essential for recycling GMP and indirectly, cGMP. In prokaryotes (such as "Escherichia coli"), lower eukaryotes (such as yeast) and in vertebrates, GK is a highly conserved monomeric protein of about 200 amino acids. GK has been shown to be structurally similar to protein A57R (or SalG2R) from various strains of Vaccinia virus.
Systems biology analyses carried out by the team of Andreas Dräger also identified a pivotal role of this enzyme in the replication of SARS-CoV-2 within the human airways.
Nomenclature.
The systematic name of this enzyme class is ATP:(d)GMP phosphotransferase. Other names in common use include"
References.
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Further reading.
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14678521
|
Hamamelose kinase
|
Enzyme
In enzymology, a hamamelose kinase (EC 2.7.1.102) is an enzyme that catalyzes the chemical reaction
ATP + D-hamamelose formula_0 ADP + D-hamamelose 2'-phosphate
Thus, the two substrates of this enzyme are ATP and D-hamamelose, whereas its two products are ADP and D-hamamelose 2'-phosphate.
This enzyme belongs to the family of transferases, specifically those transferring phosphorus-containing groups (phosphotransferases) with an alcohol group as acceptor. The systematic name of this enzyme class is ATP:D-hamamelose 2'-phosphotransferase. Other names in common use include hamamelose kinase (phosphorylating), hamamelosekinase (ATP: hamamelose 2'-phosphotransferase), and ATP/hamamelose 2'-phosphotransferase.
References.
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14678550
|
Histidine kinase
|
Family of enzymes important in cell signaling
Histidine kinases (HK) are multifunctional, and in non-animal kingdoms, typically transmembrane, proteins of the transferase class of enzymes that play a role in signal transduction across the cellular membrane. The vast majority of HKs are homodimers that exhibit autokinase, phosphotransfer, and phosphatase activity. HKs can act as cellular receptors for signaling molecules in a way analogous to tyrosine kinase receptors (RTK). Multifunctional receptor molecules such as HKs and RTKs typically have portions on the outside of the cell (extracellular domain) that bind to hormone- or growth factor-like molecules, portions that span the cell membrane (transmembrane domain), and portions within the cell (intracellular domain) that contain the enzymatic activity. In addition to kinase activity, the intracellular domains typically have regions that bind to a secondary effector molecule or complex of molecules that further propagate signal transduction within the cell. Distinct from other classes of protein kinases, HKs are usually parts of a two-component signal transduction mechanisms in which HK transfers a phosphate group from ATP to a histidine residue within the kinase, and then to an aspartate residue on the receiver domain of a response regulator protein (or sometimes on the kinase itself). More recently, the widespread existence of protein histidine phosphorylation distinct from that of two-component histidine kinases has been recognised in human cells. In marked contrast to Ser, Thr and Tyr phosphorylation, the analysis of phosphorylated Histidine using standard biochemical and mass spectrometric approaches is much more challenging, and special procedures and separation techniques are required for their preservation alongside classical Ser, Thr and Tyr phosphorylation on proteins isolated from human cells.
In terms of enzymology, a histidine kinase (EC 2.7.13.3, "EnvZ", "histidine protein kinase", "protein histidine kinase", "protein kinase (histidine)", "HK1", "HP165", "Sln1p") is an enzyme that catalyzes the chemical reaction
ATP + protein L-histidine formula_0 ADP + protein N-phospho-L-histidine.
Thus, the two substrates of this enzyme are ATP and protein L-histidine, whereas its two products are ADP and protein N-phospho-L-histidine.
This type of enzyme is involved in signal transduction pathways upstream of many cellular processes including various metabolic, virulence, and homeostatic pathways.
Mechanism.
The mechanism for the reactions catalyzed by histidine kinase have not been completely elucidated, but current evidence suggests that the catalytic domain of one dimeric unit may rotate in such a way that the ATP binding pocket of that unit can come into contact with a particular histidine residue on the opposite unit and a nucleophilic addition results in a phosphorylated histidine.
Structure and function.
An HK is composed of several domains starting with a short N-terminal cytoplasmic portion connected to an extracellular sensing domain via a transmembrane α helix. A second transmembrane α helix connects the extracellular domain to the C-terminal cytoplasmic catalytic domain. HKs are known to serve roles in many different signal transduction pathways, so it is not surprising that the extracellular sensing domain is not very well conserved in the HK family. In contrast, the cytoplasmic domain tends to have high sequence homology and contains several well-known motifs. These motifs include the H, N, G1, F, and G2 boxes. The autophosphorylation H-box is contained in the N-terminal dimerization and histidine phosphotransfer (DHp) domain. In HK853-CD, crystallized from "Thermotoga maritima", this domain is a helical-hairpin and is formed by residues 232-317. The histidine phosphorylation site is located at His-260. The N, G1, F and G2 boxes are contained in the C-terminal catalytic and ATP-binding (CA) domain. This domain is formed by residues 323-489 and forms a structure known as an α/β sandwich fold. This particular fold has one layer composed of a 5-stranded β sheet and the other layer is made of three α helices.
The dimeric unit is held together by a four-helix bundle, formed when the C-terminal segments of the α1 helices on each subunit interact in an antiparallel manner with both α2 helices. The stability of the dimer is aided by several interactions at the interface between the DHps of each monomer. These include hydrophobic interactions between conserved hydrophobic residues as well as two hydrogen bonds (Thr-252...Glu-316’ and Arg-263...Asn-307’) and one salt bridge (Lys-270...Glu-303’). Further interactions are mediated via hydrogen bonds to water within a cavity inside the coiled coil and flanked by hydrophobic residues.
The nucleotide/ATP binding pocket is contained within the CA domain and the structural similarity of this pocket is high between most HKs. The cavity of CheA, also crystallized from T. maritima, is first formed by β sheet P4 in the rear and the sides of the cavity are formed by the 4 motifs mentioned earlier, the N, G1, F, and G2 boxes. The majority of the residues coming from the β sheet are hydrophobic with Asp449 being the exception. This residue is invariant and forms a hydrogen bond along with a water molecule to the adenine amine group. Three other water molecules form direct hydrogen bonds with the adenine base. A Mg2+ ion forms a bridge between all three phosphates and an invariant Asn residue. Finally, two more water molecules complete octahedral coordination with Mg2+ and are linked to Arg-408 and His-405. When the γ phosphate of ATP is destabilized, the Mg2+ is no longer observed due to its inability to octahedrally coordinate. Marina et al. argue that similar coordination of Mg2+ occurs in HK853 but that it is unobserved due to the usage of the ATP analog AMPPNP in the crystal structure. During crystallization, the analog was hydrolyzed into a product similar to ADP.
The final side of the ATP binding pocket is conveniently named the “ATP lid.” The stability of this structure is mediated by the presence of the γ phosphate and thus the Mg2+ ion in the binding site. Also the presence of the nucleotide base has proved to play a significant role in stabilization of the lid in a closed conformation. The ATP lid is connected via hydrophobic residues to the rest of the protein. The γ phosphate of ATP is somewhat exposed allowing for dephosphorylation.
Upon ATP binding in this pocket, it is believed that a conformational change occurs allowing the rotation of the CA domain to come into contact with the DHp of the other monomer and thus allowing the conserved His-260 to rest near the γ phosphate. The Nε of His-260 then attacks the γ phosphate of ATP in a nucleophilic addition and bumps off ADP as its leaving group.
Role in fungal infections.
A two-component system (TCSs), involving histidine kinase and a variable response regulator protein, may be critical to the virulence of some fungal strains such as "Candida albicans", which is often responsible for causing candidiasis in immunocompromised persons. "C. albicans" with a deletion of CHK1, the two-component histidine kinase gene, show defects in morphogenesis and a drastic decrease in the cell’s ability to resist elimination by human neutrophils. As humans lack this two-component system, it may be a good target for anti-microbial agents in order to treat candidiasis.
Role in bacteria infections.
Similar to fungus, Two component systems can also be found in several persistent bacteria infections. For example, "Staphylococcus aureus" was reported to use SrrAB TCSs consisting of a sensor HKs (SrrB), which would transfer phosphate group to an effector response regulator (SrrA), leading to the modification of SrrA activity including gene regulation. This TCSs has been used by "S. aureus" in order to sense changes of environmental condition and transmit the signal to an appropriate responding system, for example, "ica" genes is induced by SrrAB to mediate cell assembly and biofilm formation to survive under anaerobic condition.
References.
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Further reading.
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14678578
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Holo-ACP synthase
|
In enzymology, a holo-ACP synthase (EC 2.7.7.61) is an enzyme that catalyzes the chemical reaction
2'-(5"-triphosphoribosyl)-3'-dephospho-CoA + apo-citrate lyase formula_0 holo-citrate lyase + diphosphate
Thus, the two substrates of this enzyme are 2'-(5"-triphosphoribosyl)-3'-dephospho-CoA and apo-citrate lyase, whereas its two products are holo-citrate lyase and diphosphate.
This enzyme belongs to the family of transferases, specifically those transferring phosphorus-containing nucleotide groups (nucleotidyltransferases). The systematic name of this enzyme class is 2'-(5"-triphosphoribosyl)-3'-dephospho-CoA:apo-citrate lyase adenylyltransferase. Other names in common use include 2'-(5"-phosphoribosyl)-3'-dephospho-CoA transferase, 2'-(5"-triphosphoribosyl)-3'-dephospho-CoA:apo-citrate lyase, and CitX. This enzyme participates in two-component system - general.
Structural studies.
As of late 2007, only one structure has been solved for this class of enzymes, with the PDB accession code 2BDD.
References.
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https://en.wikipedia.org/wiki?curid=14678578
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14678600
|
Holo-(acyl-carrier-protein) synthase
|
In enzymology and molecular biology, a holo-[acyl-carrier-protein] synthase (ACPS, EC 2.7.8.7) is an enzyme that catalyzes the chemical reaction:
CoA-[4'-phosphopantetheine] + apo-acyl carrier protein formula_0 adenosine 3',5'-bisphosphate + holo-acyl carrier protein
This enzyme belongs to the family of transferases, specifically those transferring non-standard substituted phosphate groups. It is also known as 4'-phosphopantetheinyl transferase after the group it transfers.
Function.
All ACPS enzymes known so far are evolutionally related to each other in a single superfamily of proteins. It transfers a 4'-phosphopantetheine (4'-PP) moiety from coenzyme A (CoA) to an invariant serine in an acyl carrier protein (ACP), a small protein responsible for acyl group activation in fatty acid biosynthesis. This post-translational modification renders holo-ACP capable of acyl group activation via thioesterification of the cysteamine thiol of 4'-PP. This superfamily consists of two subtypes: the trimeric ACPS type such as "E. coli" ACPS and the monomeric Sfp (PCP-synthesizing) type such as "B. subtilis" SFP. Structures from both families are now known. The active site accommodates a magnesium ion. The most highly conserved regions of the protein are involved in binding the magnesium ion.
Nomenclature.
The systematic name of this enzyme class is CoA-[4'-phosphopantetheine]:apo-[acyl-carrier-protein] 4'-pantetheinephosphotransferase. Other names in common use, disregarding the synthetase/synthase spelling difference, include acyl carrier protein holoprotein synthetase, holo-ACP synthetase, coenzyme A:fatty acid synthetase apoenzyme 4'-phosphopantetheine, acyl carrier protein synthetase (ACPS), PPTase, acyl carrier protein synthase, P-pant transferase, and CoA:apo-[acyl-carrier-protein] pantetheinephosphotransferase.
Structural studies.
As of late 2007, 8 structures have been solved for this class of enzymes, with PDB accession codes 1F7L, 1F7T, 1F80, 1FTE, 1FTF, 1FTH, 2JBZ, and 2JCA.
References.
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Further reading.
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https://en.wikipedia.org/wiki?curid=14678600
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14678625
|
Homoserine kinase
|
Enzyme
In enzymology, a homoserine kinase (EC 2.7.1.39) is an enzyme that catalyzes the chemical reaction
ATP + L-homoserine formula_0 ADP + O-phospho-L-homoserine
Thus, the two substrates of this enzyme are ATP and L-homoserine, whereas its two products are ADP and O-phospho-L-homoserine.
This enzyme belongs to the family of transferases, specifically those transferring phosphorus-containing groups (phosphotransferases) with an alcohol group as acceptor. The systematic name of this enzyme class is ATP:L-homoserine O-phosphotransferase. Other names in common use include homoserine kinase (phosphorylating), and HSK. This enzyme participates in glycine, serine and threonine metabolism.
Structural studies.
As of late 2007, 6 structures have been solved for this class of enzymes, with PDB accession codes 1FWK, 1FWL, 1H72, 1H73, 1H74, and 2PPQ.
References.
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