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14453238
|
3',5'-cyclic-GMP phosphodiesterase
|
Class of enzymes
The enzyme 3′,5′-cyclic-GMP phosphodiesterase (EC 3.1.4.35) catalyzes the reaction
guanosine 3′,5′-cyclic phosphate + H2O formula_0 guanosine 5′-phosphate
This enzyme belongs to the family of hydrolases, specifically those acting on phosphoric diester bonds. The systematic name is 3′,5′-cyclic-GMP 5'-nucleotidohydrolase. Other names in common use include guanosine cyclic 3',5'-phosphate phosphodiesterase, cyclic GMP phosphodiesterase, cyclic 3′,5′-GMP phosphodiesterase, cyclic guanosine 3′,5′-monophosphate phosphodiesterase, cyclic guanosine 3′,5′-phosphate phosphodiesterase, cGMP phosphodiesterase, cGMP-PDE, and cyclic guanosine 3′,5′-phosphate phosphodiesterase.
Structural studies.
As of late 2007, 5 structures have been solved for this class of enzymes, with PDB accession codes 1MC0, 2CHM, 2H40, 2H42, and 2H44.
References.
<templatestyles src="Reflist/styles.css" />
|
[
{
"math_id": 0,
"text": "\\rightleftharpoons"
}
] |
https://en.wikipedia.org/wiki?curid=14453238
|
14453256
|
3-deoxy-manno-octulosonate-8-phosphatase
|
Class of enzymes
The enzyme 3-deoxy-"manno"-octulosonate-8-phosphatase (EC 3.1.3.45) catalyzes the reaction
3-deoxy--"manno"-octulosonate 8-phosphate + H2O formula_0 3-deoxy--"manno"-octulosonate + phosphate
This enzyme belongs to the family of hydrolases, specifically those acting on phosphoric monoester bonds. The systematic name is 3-deoxy--"manno"-octulosonate-8-phosphate 8-phosphohydrolase. This enzyme participates in lipopolysaccharide biosynthesis.
References.
<templatestyles src="Reflist/styles.css" />
|
[
{
"math_id": 0,
"text": "\\rightleftharpoons"
}
] |
https://en.wikipedia.org/wiki?curid=14453256
|
14453272
|
3-hydroxyisobutyryl-CoA hydrolase
|
Class of enzymes
The enzyme 3-hydroxyisobutyryl-CoA hydrolase (EC 3.1.2.4) catalyzes the reaction
3-hydroxy-2-methylpropanoyl-CoA + H2O formula_0 CoA + 3-hydroxy-2-methylpropanoate
This enzyme belongs to the family of hydrolases, specifically those acting on thioester bonds. The systematic name is 3-hydroxy-2-methylpropanoyl-CoA hydrolase. Other names in common use include 3-hydroxy-isobutyryl CoA hydrolase, and HIB CoA deacylase. This enzyme participates in 3 metabolic pathways: valine, leucine and isoleucine degradation, β-alanine metabolism, and propanoate metabolism. 3-hydroxyisobutyryl-CoA hydrolase is encoded by "HIBCH" gene.
References.
<templatestyles src="Reflist/styles.css" />
|
[
{
"math_id": 0,
"text": "\\rightleftharpoons"
}
] |
https://en.wikipedia.org/wiki?curid=14453272
|
14453299
|
3'-nucleotidase
|
Class of enzymes
The enzyme 3′-nucleotidase (EC 3.1.3.6) the reaction
a 3′-ribonucleotide + H2O formula_0 a ribonucleoside + phosphate
This enzyme belongs to the family of hydrolases, specifically those acting on phosphoric monoester bonds. The systematic name is 3′-ribonucleotide phosphohydrolase. Other names in common use include 3′-mononucleotidase, 3′-phosphatase, and 3′-ribonucleotidase. This enzyme participates in purine and pyrimidine metabolism.
References.
<templatestyles src="Reflist/styles.css" />
|
[
{
"math_id": 0,
"text": "\\rightleftharpoons"
}
] |
https://en.wikipedia.org/wiki?curid=14453299
|
14453320
|
3-oxoadipate enol-lactonase
|
Class of enzymes
The enzyme 3-oxoadipate enol-lactonase (EC 3.1.1.24) catalyzes the reaction
3-oxoadipate enol-lactone + H2O formula_0 3-oxoadipate
This enzyme belongs to the family of hydrolases, specifically those acting on carboxylic ester bonds. The systematic name is 4-carboxymethylbut-3-en-4-olide enol-lactonohydrolase. Other names in common use include carboxymethylbutenolide lactonase, β-ketoadipic enol-lactone hydrolase, 3-ketoadipate enol-lactonase, 3-oxoadipic enol-lactone hydrolase, and β-ketoadipate enol-lactone hydrolase. This enzyme participates in benzoate degradation via hydroxylation.
References.
<templatestyles src="Reflist/styles.css" />
|
[
{
"math_id": 0,
"text": "\\rightleftharpoons"
}
] |
https://en.wikipedia.org/wiki?curid=14453320
|
14453340
|
3-phosphoglycerate phosphatase
|
Class of enzymes
The enzyme 3-phosphoglycerate phosphatase (EC 3.1.3.38) catalyzes the reaction
-glycerate 3-phosphate + H2O formula_0 -glycerate + phosphate
This enzyme belongs to the family of hydrolases, specifically those acting on phosphoric monoester bonds. The systematic name is -glycerate-3-phosphate phosphohydrolase. Other names in common use include -3-Phosphoglycerate phosphatase, and 3-PGA phosphatase. This enzyme participates in glycine, serine and threonine metabolism.
References.
<templatestyles src="Reflist/styles.css" />
|
[
{
"math_id": 0,
"text": "\\rightleftharpoons"
}
] |
https://en.wikipedia.org/wiki?curid=14453340
|
14453374
|
4-hydroxybenzoyl-CoA thioesterase
|
Class of enzymes
The enzyme 4-hydroxybenzoyl-CoA thioesterase (EC 3.1.2.23) catalyzes the reaction
4-hydroxybenzoyl-CoA + H2O formula_0 4-hydroxybenzoate + CoA
This enzyme belongs to the family of hydrolases, specifically those acting on thioester bonds. The systematic name is 4-hydroxybenzoyl-CoA hydrolase. This enzyme participates in 2,4-dichlorobenzoate degradation.
Structural studies.
As of late 2007, 7 structures have been solved for this class of enzymes, with PDB accession codes 1HN1, 1LO7, 1LO8, 1LO9, 1Q4S, 1Q4T, and 1Q4U.
References.
<templatestyles src="Reflist/styles.css" />
|
[
{
"math_id": 0,
"text": "\\rightleftharpoons"
}
] |
https://en.wikipedia.org/wiki?curid=14453374
|
14453410
|
4-methyloxaloacetate esterase
|
Class of enzymes
The enzyme 4-methyloxaloacetate esterase (EC 3.1.1.44) catalyzes the reaction
oxaloacetate 4-methyl ester + H2O formula_0 oxaloacetate + methanol
This enzyme belongs to the family of hydrolases, specifically those acting on carboxylic ester bonds. The systematic name is oxaloacetate-4-methyl-ester oxaloacetohydrolase.
References.
<templatestyles src="Reflist/styles.css" />
|
[
{
"math_id": 0,
"text": "\\rightleftharpoons"
}
] |
https://en.wikipedia.org/wiki?curid=14453410
|
14453439
|
4-nitrophenylphosphatase
|
Class of enzymes
The enzyme 4-nitrophenylphosphatase (EC 3.1.3.41) catalyzes the reaction
4-nitrophenyl phosphate + H2O formula_0 4-nitrophenol + phosphate
This enzyme belongs to the family of hydrolases, specifically those acting on phosphoric monoester bonds. The systematic name of this enzyme class is 4-nitrophenylphosphate phosphohydrolase. Other names in common use include nitrophenyl phosphatase, p"-nitrophenylphosphatase, para"-nitrophenyl phosphatase, K-pNPPase, NPPase, PNPPase, Ecto-p-nitrophenyl phosphatase, and "p"-nitrophenylphosphate phosphohydrolase. This enzyme participates in γ-hexachlorocyclohexane degradation.
Structural studies.
As of late 2007, only one structure has been solved for this class of enzymes, with the PDB accession code PDB: 1VJR.
References.
<templatestyles src="Reflist/styles.css" />
|
[
{
"math_id": 0,
"text": "\\rightleftharpoons"
}
] |
https://en.wikipedia.org/wiki?curid=14453439
|
14453463
|
4-phytase
|
Class of enzymes
The enzyme 4-phytase (EC 3.1.3.26) catalyzes the following reaction:
"myo"-inositol hexakisphosphate + H2O formula_0 1-"myo"-inositol 1,2,3,5,6-pentakisphosphate + phosphate
"myo"-Inositol hexakisphosphate is also known as phytic acid.
These enzymes belongs to the family of hydrolases, specifically those acting on phosphoric monoester bonds. The systematic name of this enzyme class is "myo"-inositol-hexakisphosphate 4-phosphohydrolase. Other names in common use include 6-phytase (name based on 1-numbering system and not 1-numbering) and phytate 6-phosphatase.
Enzymes of this type participate in inositol phosphate metabolism.
References.
<templatestyles src="Reflist/styles.css" />
|
[
{
"math_id": 0,
"text": "\\rightleftharpoons"
}
] |
https://en.wikipedia.org/wiki?curid=14453463
|
14453492
|
4-pyridoxolactonase
|
Class of enzymes
The enzyme 4-pyridoxolactonase (EC 3.1.1.27) catalyzes the reaction
4-pyridoxolactone + H2O formula_0 4-pyridoxate
This enzyme belongs to the family of hydrolases, specifically those acting on carboxylic ester bonds. The systematic name is 4-pyridoxolactone lactonohydrolase. It participates in vitamin B6 metabolism.
References.
<templatestyles src="Reflist/styles.css" />
|
[
{
"math_id": 0,
"text": "\\rightleftharpoons"
}
] |
https://en.wikipedia.org/wiki?curid=14453492
|
14453525
|
5-(3,4-diacetoxybut-1-ynyl)-2,2'-bithiophene deacetylase
|
Class of enzymes
The enzyme 5-(3,4-diacetoxybut-1-ynyl)-2,2′-bithiophene deacetylase (EC 3.1.1.66) catalyzes the reaction
5-(3,4-diacetoxybut-1-ynyl)-2,2′-bithiophene + H2O formula_0 5-(3-hydroxy-4-acetoxybut-1-ynyl)-2,2′-bithiophene + acetate
This enzyme belongs to the family of hydrolases, specifically those acting on carboxylic ester bonds. The systematic name is 5-(3,4-diacetoxybut-1-ynyl)-2,2′-bithiophene acetylhydrolase. Other names in common use include diacetoxybutynylbithiophene acetate esterase, and 3,4-diacetoxybutinylbithiophene:4-acetate esterase.
References.
<templatestyles src="Reflist/styles.css" />
|
[
{
"math_id": 0,
"text": "\\rightleftharpoons"
}
] |
https://en.wikipedia.org/wiki?curid=14453525
|
14453587
|
6-acetylglucose deacetylase
|
Class of enzymes
The enzyme 6-acetylglucose deacetylase (EC 3.1.1.33) catalyzes the reaction
6-acetyl--glucose + H2O formula_0 -glucose + acetate
This enzyme belongs to the family of hydrolases, specifically those acting on carboxylic ester bonds. The systematic name of this enzyme class is 6-acetyl--glucose acetylhydrolase. This enzyme is also called 6-"O"-acetylglucose deacetylase.
References.
<templatestyles src="Reflist/styles.css" />
|
[
{
"math_id": 0,
"text": "\\rightleftharpoons"
}
] |
https://en.wikipedia.org/wiki?curid=14453587
|
14453601
|
Acetoacetyl-CoA hydrolase
|
Class of enzymes
The enzyme acetoacetyl-CoA hydrolase (EC 3.1.2.11) catalyzes the reaction
acetoacetyl-CoA + H2O formula_0 CoA + acetoacetate
This enzyme belongs to the family of hydrolases, specifically those acting on thioester bonds. The systematic name is acetoacetyl-CoA hydrolase. Other names in common use include acetoacetyl coenzyme A hydrolase, acetoacetyl CoA deacylase, and acetoacetyl coenzyme A deacylase. This enzyme participates in butanoate metabolism.
References.
<templatestyles src="Reflist/styles.css" />
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[
{
"math_id": 0,
"text": "\\rightleftharpoons"
}
] |
https://en.wikipedia.org/wiki?curid=14453601
|
14453626
|
Acetoxybutynylbithiophene deacetylase
|
Class of enzymes
The enzyme acetoxybutynylbithiophene deacetylase (EC 3.1.1.54) catalyzes the reaction
5-(4-acetoxybut-1-ynyl)-2,2′-bithiophene + H2O formula_0 5-(4-hydroxybut-1-ynyl)-2,2′-bithiophene + acetate
This enzyme belongs to the family of hydrolases, specifically those acting on carboxylic ester bonds. The systematic name is 5-(4-acetoxybut-1-ynyl)-2,2′-bithiophene "O"-acetylhydrolase. Other names in common use include acetoxybutynylbithiophene esterase, and 5-(4-acetoxy-1-butynyl)-2,2′-bithiophene:acetate esterase.
References.
<templatestyles src="Reflist/styles.css" />
|
[
{
"math_id": 0,
"text": "\\rightleftharpoons"
}
] |
https://en.wikipedia.org/wiki?curid=14453626
|
14453654
|
Acetylalkylglycerol acetylhydrolase
|
Class of enzymes
The enzyme acetylalkylglycerol acetylhydrolase (EC 3.1.1.71) catalyzes the reaction
2-acetyl-1-alkyl-"sn"-glycerol + H2O formula_0 1-alkyl-"sn"-glycerol + acetate
This enzyme belongs to the family of hydrolases, specifically those acting on carboxylic ester bonds. The systematic name of this enzyme class is 2-acetyl-1-alkyl-"sn"-glycerol acetylhydrolase. This enzyme is also called alkylacetylglycerol acetylhydrolase.
References.
<templatestyles src="Reflist/styles.css" />
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[
{
"math_id": 0,
"text": "\\rightleftharpoons"
}
] |
https://en.wikipedia.org/wiki?curid=14453654
|
14453678
|
(acetyl-CoA carboxylase)-phosphatase
|
Class of enzymes
The enzyme [acetyl-CoA carboxylase]-phosphatase (EC 3.1.3.44) catalyzes the reaction
[acetyl-CoA carboxylase] phosphate + H2O formula_0 [acetyl-CoA carboxylase] + phosphate
This enzyme belongs to the family of hydrolases, specifically those acting on phosphoric monoester bonds. The systematic name is [acetyl-CoA:carbon-dioxide ligase (ADP-forming)]-phosphate phosphohydrolase.
References.
<templatestyles src="Reflist/styles.css" />
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[
{
"math_id": 0,
"text": "\\rightleftharpoons"
}
] |
https://en.wikipedia.org/wiki?curid=14453678
|
14453737
|
Acetylesterase
|
Class of enzymes which split acetic esters into alcohols and acetates
In biochemistry, an acetylesterase (EC 3.1.1.6) is a class of enzyme which catalyzes the hydrolysis of acetic esters into an alcohol and acetic acid:
formula_0
This enzyme belongs to the family of hydrolases, specifically those acting on carboxylic ester bonds (esterases). The systematic name of this enzyme class is acetic-ester acetylhydrolase. Other names in common use include C-esterase (in animal tissues), acetic ester hydrolase, chloroesterase, "p"-nitrophenyl acetate esterase, and citrus acetylesterase.
Structural studies.
As of late 2007, 3 structures have been solved for this class of enzymes, with PDB accession codes 1BS9, 1G66, and 2AXE.
References.
<templatestyles src="Reflist/styles.css" />
|
[
{
"math_id": 0,
"text": "\\ce{R-OC(O)CH3 + H2O} \\quad \\xrightarrow[\\text{acetylesterase}]{} \\quad \\ce{R-OH + HO-C(O)CH3}"
}
] |
https://en.wikipedia.org/wiki?curid=14453737
|
14453777
|
Acetylsalicylate deacetylase
|
Class of enzymes
The enzyme acetylsalicylate deacetylase (EC 3.1.1.55) catalyzes the reaction
acetylsalicylate + H2O formula_0 salicylate + acetate
This enzyme belongs to the family of hydrolases, specifically those acting on carboxylic ester bonds. The systematic name is acetylsalicylate "O"-acetylhydrolase. Other names in common use include aspirin esterase, acetylsalicylic acid esterase, and aspirin hydrolase.
References.
<templatestyles src="Reflist/styles.css" />
|
[
{
"math_id": 0,
"text": "\\rightleftharpoons"
}
] |
https://en.wikipedia.org/wiki?curid=14453777
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14453838
|
Actinomycin lactonase
|
Class of enzymes
The enzyme actinomycin lactonase (EC 3.1.1.39) catalyzes the reaction
actinomycin + H2O formula_0 actinomycinic monolactone
This enzyme belongs to the family of hydrolases, specifically those acting on carboxylic ester bonds. The systematic name is actinomycin lactonohydrolase.
References.
<templatestyles src="Reflist/styles.css" />
|
[
{
"math_id": 0,
"text": "\\rightleftharpoons"
}
] |
https://en.wikipedia.org/wiki?curid=14453838
|
14453863
|
Acylcarnitine hydrolase
|
Class of enzymes
The enzyme acylcarnitine hydrolase (EC 3.1.1.28) catalyzes the reaction
"O"-acylcarnitine + H2O formula_0 a fatty acid + -carnitine
This enzyme belongs to the family of hydrolases, specifically those acting on carboxylic ester bonds. The systematic name is "O"-acylcarnitine acylhydrolase. Other names in common use include high activity acylcarnitine hydrolase, HACH, carnitine ester hydrolase, palmitoylcarnitine hydrolase, palmitoyl--carnitine hydrolase, long-chain acyl--carnitine hydrolase, and palmitoyl carnitine hydrolase.
References.
<templatestyles src="Reflist/styles.css" />
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[
{
"math_id": 0,
"text": "\\rightleftharpoons"
}
] |
https://en.wikipedia.org/wiki?curid=14453863
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14453889
|
(acyl-carrier-protein) phosphodiesterase
|
Enzyme
The enzyme [acyl-carrier-protein] phosphodiesterase (EC 3.1.4.14) catalyzes the reaction
holo-[acyl-carrier-protein] + H2O formula_0 4′-phosphopantetheine + apo-[acyl-carrier-protein]
This enzyme belongs to the family of hydrolases, specifically those acting on phosphoric diester bonds. The systematic name is holo-[acyl-carrier-protein] 4′-pantetheine-phosphohydrolase. Other names in common use include ACP hydrolyase, ACP phosphodiesterase, AcpH, and [acyl-carrier-protein] 4′-pantetheine-phosphohydrolase. This enzyme participates in pantothenate and CoA biosynthesis.
Structural studies.
As of late 2007, two structures have been solved for this class of enzymes, with PDB accession codes 1T5B and 1TIK.
References.
<templatestyles src="Reflist/styles.css" />
|
[
{
"math_id": 0,
"text": "\\rightleftharpoons"
}
] |
https://en.wikipedia.org/wiki?curid=14453889
|
14453911
|
Acyl-CoA hydrolase
|
InterPro Family
The enzyme acyl-CoA hydrolase (EC 3.1.2.20) catalyzes the reaction
acyl-CoA + H2O formula_0 CoA + a carboxylate
This enzyme belongs to the family of hydrolases, specifically those acting on thioester bonds. The systematic name of this enzyme class is acyl-CoA hydrolase. Other names in common use include acyl coenzyme A thioesterase, acyl-CoA thioesterase, acyl coenzyme A hydrolase, thioesterase B, thioesterase II, and acyl-CoA thioesterase.
Structural studies.
As of late 2007, two structures have been solved for this class of enzymes, with PDB accession codes 1Y7U and 2GVH.
References.
<templatestyles src="Reflist/styles.css" />
|
[
{
"math_id": 0,
"text": "\\rightleftharpoons"
}
] |
https://en.wikipedia.org/wiki?curid=14453911
|
14453959
|
Adenylyl-(glutamate—ammonia ligase) hydrolase
|
In enzymology, an adenylyl-[glutamate---ammonia ligase] hydrolase (EC 3.1.4.15) is an enzyme that catalyzes the chemical reaction
adenylyl-[L-glutamate:ammonia ligase (ADP-forming)] + H2O formula_0 adenylate + [L-glutamate:ammonia ligase (ADP-forming)]
Thus, the two substrates of this enzyme are ] and H2O, whereas its two products are adenylate and .
This enzyme belongs to the family of hydrolases, specifically those acting on phosphoric diester bonds. The systematic name of this enzyme class is adenylyl-[L-glutamate:ammonia ligase (ADP-forming)] adenylylhydrolase. Other names in common use include adenylyl-[glutamine-synthetase]hydrolase, and adenylyl(glutamine synthetase) hydrolase.
References.
<templatestyles src="Reflist/styles.css" />
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[
{
"math_id": 0,
"text": "\\rightleftharpoons"
}
] |
https://en.wikipedia.org/wiki?curid=14453959
|
14453977
|
ADP-dependent medium-chain-acyl-CoA hydrolase
|
The enzyme ADP-dependent medium-chain-acyl-CoA hydrolase (EC 3.1.2.19) catalyzes the reaction
acyl-CoA + H2O formula_0 CoA + a carboxylate
This enzyme belongs to the family of hydrolases, specifically those acting on thioester bonds. The systematic name is ADP-dependent-medium-chain-acyl-CoA hydrolase. Other names in common use include medium-chain acyl coenzyme A hydrolase, medium-chain acyl-CoA hydrolase, medium-chain acyl-thioester hydrolase, medium-chain hydrolase, and myristoyl-CoA thioesterase. It employs one cofactor, ADP. At least one compound, NADH is known to inhibit this enzyme.
References.
<templatestyles src="Reflist/styles.css" />
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[
{
"math_id": 0,
"text": "\\rightleftharpoons"
}
] |
https://en.wikipedia.org/wiki?curid=14453977
|
14453999
|
ADP-dependent short-chain-acyl-CoA hydrolase
|
The enzyme ADP-dependent short-chain-acyl-CoA hydrolase (EC 3.1.2.18) catalyzes the reaction
acyl-CoA + H2O formula_0 CoA + a carboxylate
This enzyme belongs to the family of hydrolases, specifically those acting on thioester bonds. The systematic name of this enzyme class is ADP-dependent-short-chain-acyl-CoA hydrolase. Other names in common use include short-chain acyl coenzyme A hydrolase, propionyl coenzyme A hydrolase, propionyl-CoA hydrolase, propionyl-CoA thioesterase, short-chain acyl-CoA hydrolase, and short-chain acyl-CoA thioesterase. It employs one cofactor, ADP. At least one compound, NADH is known to inhibit this enzyme.
References.
<templatestyles src="Reflist/styles.css" />
|
[
{
"math_id": 0,
"text": "\\rightleftharpoons"
}
] |
https://en.wikipedia.org/wiki?curid=14453999
|
14454026
|
ADP-phosphoglycerate phosphatase
|
The enzyme ADP-phosphoglycerate phosphatase (EC 3.1.3.28) catalyzes the reaction
3-(ADP)-2-phosphoglycerate + H2O formula_0 3-(ADP)-glycerate + phosphate
This enzyme belongs to the family of hydrolases, specifically those acting on phosphoric monoester bonds. The systematic name is 3-(ADP)-2-phosphoglycerate phosphohydrolase. This enzyme is also called adenosine diphosphate phosphoglycerate phosphatase.
References.
<templatestyles src="Reflist/styles.css" />
|
[
{
"math_id": 0,
"text": "\\rightleftharpoons"
}
] |
https://en.wikipedia.org/wiki?curid=14454026
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14454065
|
Alkylacetylglycerophosphatase
|
The enzyme alkylacetylglycerophosphatase (EC 3.1.3.59) catalyzes the reaction
1-alkyl-2-acetyl-"sn"-glycero-3-phosphate + H2O formula_0 1-alkyl-2-acetyl-"sn"-glycerol + phosphate
This enzyme belongs to the family of hydrolases, specifically those acting on phosphoric monoester bonds. The systematic name is 1-alkyl-2-acetyl-"sn"-glycero-3-phosphate phosphohydrolase. Other names in common use include 1-alkyl-2-lyso-"sn"-glycero-3-"P":acetyl-CoA acetyltransferase, and alkylacetylglycerophosphate phosphatase. This enzyme participates in ether lipid metabolism.
References.
<templatestyles src="Reflist/styles.css" />
|
[
{
"math_id": 0,
"text": "\\rightleftharpoons"
}
] |
https://en.wikipedia.org/wiki?curid=14454065
|
14454101
|
Alkylglycerophosphoethanolamine phosphodiesterase
|
The enzyme alkylglycerophosphoethanolamine phosphodiesterase (EC 3.1.4.39) catalyzes the reaction
1-alkyl-"sn"-glycero-3-phosphoethanolamine + H2O formula_0 1-alkyl-"sn"-glycerol 3-phosphate + ethanolamine
This enzyme belongs to the family of hydrolases, specifically those acting on phosphoric diester bonds. The systematic name is 1-alkyl-"sn"-glycero-3-phosphoethanolamine ethanolaminehydrolase. This enzyme is also called lysophospholipase D. This enzyme participates in ether lipid metabolism.
Structural studies.
As of late 2007, only one structure has been solved for this class of enzymes, with the PDB accession code 1FJ2.
References.
<templatestyles src="Reflist/styles.css" />
|
[
{
"math_id": 0,
"text": "\\rightleftharpoons"
}
] |
https://en.wikipedia.org/wiki?curid=14454101
|
14454163
|
Alpha-amino-acid esterase
|
The enzyme α-amino-acid esterase (EC 3.1.1.43) catalyzes the reaction
an α-amino acid ester + H2O formula_0 an α-amino acid + an alcohol
This enzyme belongs to the family of hydrolases, specifically those acting on carboxylic ester bonds. The systematic name is α-amino-acid-ester aminoacylhydrolase. This enzyme is also called α-amino acid ester hydrolase.
Structural studies.
As of late 2007, 5 structures have been solved for this class of enzymes, with PDB accession codes 1MPX, 1NX9, 1RYY, 2B4K, and 2B9V.
References.
<templatestyles src="Reflist/styles.css" />
|
[
{
"math_id": 0,
"text": "\\rightleftharpoons"
}
] |
https://en.wikipedia.org/wiki?curid=14454163
|
14454184
|
Alpha-ribazole phosphatase
|
The primary biochemical reaction catalyzed by the enzyme adenosylcobalamin/α-ribazole phosphatase (formerly α-ribazole phosphatase) (EC 3.1.3.73) is
adenosylcobalamin 5′-phosphate + H2O = coenzyme B12 + phosphate
This enzyme can also catalyze the following reaction in vitro, however it is not the biologically relevant reaction
α-ribazole 5′-phosphate + H2O formula_0 α-ribazole + phosphate
This enzyme belongs to the family of hydrolases, specifically those acting on phosphoric monoester bonds. The systematic name is adenosylcobalamin/α-ribazole-5′-phosphate phosphohydrolase. This enzyme is also called CobC. It is part of the biosynthetic pathway to cobalamin (vitamin B12) in bacteria.
Structural studies.
As of late 2007, 16 structures have been solved for this class of enzymes, with PDB accession codes 2ENU, 2ENW, 2EOA, 2OWE, 2P2Y, 2P2Z, 2P30, 2P6M, 2P6O, 2P75, 2P77, 2P78, 2P79, 2P9Y, 2P9Z, and 2PA0.
References.
<templatestyles src="Reflist/styles.css" />
|
[
{
"math_id": 0,
"text": "\\rightleftharpoons"
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https://en.wikipedia.org/wiki?curid=14454184
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14454224
|
Aryldialkylphosphatase
|
Aryldialkylphosphatase (EC 3.1.8.1, also known as phosphotriesterase, organophosphate hydrolase, parathion hydrolase, paraoxonase, and parathion aryl esterase; systematic name aryltriphosphate dialkylphosphohydrolase) is a metalloenzyme that hydrolyzes the triester linkage found in organophosphate insecticides:
an aryl dialkyl phosphate + H2O formula_0 dialkyl phosphate + an aryl alcohol
The gene ("opd", for organophosphate-degrading) that codes for the enzyme is found in a large plasmid (pSC1, 51Kb) endogenous to "Pseudomonas" "diminuta", although the gene has also been found in many other bacterial species such as "Flavobacterium" sp. (ATCC27551), where it is also encoded in an extrachromosomal element (pSM55, 43Kb).
Organophosphate is the general name for esters of phosphoric acid and is one of the organophosphorus compounds. They can be found as part of insecticides, herbicides, and nerve gases, amongst others. Some less-toxic organophosphates can be used as solvents, plasticizers, and EP additives. The use of organophosphates accounts for approximately 38% of all pesticide use globally.
Gene.
Bacterial isolates capable of degrading organophosphate (OP) pesticides have been identified from soil samples from different parts of the world. The first organophosphate-degrading bacterial species was isolated from a soil sample from the Philippines in 1973, which identified as "Flavobacterium" sp. ATCC27551. Since then, other species have demonstrated to have OP-degrading abilities, such as "Pseudomonas diminuta" (isolated from US soil sample), "Agrobacterium radiobacter" (isolated from Australian soil sample), "Alteromonas haloplanktis" (isolated from US soil sample), and "Pseudomonas" sp. WBC-3 (isolated from Chinese soil sample).
The capacity to hydrolyze organophosphates is not unique to bacteria. A few fungi and cyanobacteria species have been found to also hydrolyze them. Moreover, through sequence homology searches of whole genomes, several other bacterial species were identified that also contain sequences from the same gene family as "opd", including pathogenic bacteria such as "Escherichia coli" ("yhfV") and "Mycobacterium tuberculosis".
The gene sequence encoding the enzyme ("opd") in "Flavobacterium" sp. ATCC27551 and "Pseudomonas diminuta" is highly conserved (100% sequence homology), although the plasmids where the genes are found have very different sequences apart from a 5.1Kb conserved region where the gene is found.
A closer look on the organization of the "opd" gene from "Flavobacterium" suggests a potential transposon-like architecture, which accounts for the widespread distribution of the gene among other microbial species that might have occurred through lateral DNA transfer. The "opd" gene is flanked by transposition insertion sequences, characteristic of Tn3 family of transposons. Moreover, a transposase-like sequence (homologous to "TnpA") and a resolvase-like sequence (homologous to "TnpR") were also identified in regions upstream of the "opd" gene, which are characteristics of class II transposons such as Tn3.
Furthermore, another open reading frame was identified downstream of "opd" and encodes a protein that further degrades "p"-nitrophenol, one of the byproducts of OP degradation. This protein is believed to work as a complex with PTE, since a dramatic increase in activity is observed when PTE is present.
Therefore, the characteristic architectural organization of the "opd" gene region suggests that different species acquired the gene through horizontal transfer through transposition and plasmid transfer.
Protein.
Structure.
Phosphotriesterase (PTE) belongs to a family metalloenzymes that has two catalytic Zn2+ metal atoms, bridged via a common ligand and coordinated by imidazole side chains of histidine residues that are clustered around the metal atoms. The protein forms a homodimer. The overall structure consists of an α/β-barrel motif, also present in other 20 catalytic proteins. The active sites of these proteins is located at the C-terminal portion of the β-barrel, which is where the active site of PTE is also located.
Catalysis.
Catalysis of organophosphates occurs via a nucleophilic substitution with inversion of configuration (SN2 mechanism) about the phosphorus centre of the substrate. In the active site, the metal cations aid in catalysis by further polarizing the P–O bond of the substrate, which makes it more susceptible to a nucleophilic attack. Furthermore, a basic residue abstracts a proton from a water molecule, and the hydroxide ion produced bridges the two divalent cations and acts as the nucleophile. The OH− then attacks the phosphorus centre of the substrate, followed by a proton transfer event. The P–O bond is broken, and the products are released from the active site. The turnover rate ("k"cat) of phosphotriesterase is nearly 104 s−1 for the hydrolysis of paraoxon, and the products are p-nitrophenol and diethyl phosphoric acid.
Species.
Phosphotriesterase is present in two species, "Pseudomonas diminuta" and "Flavobacterium" sp. ATCC27551. Other gene variants that also encode organophosphate-degrading enzymes are present in other species. The list includes bacterial species such as the radioresistant "Deinococcus radiodurans", pathogens "Mycobacterium tuberculosis" and "Mycobacterium bovis", the anaerobic bacterium "Desulfatibacillum alkenivorans", the thermophilic bacteria "Geobacillus" sp. and "Thermoanaerobacter" sp. X514, "Escherichia coli" ("yhfV") and many other groups of bacteria, and also some Archaea such as "Sulfolobus acidocaldarius".
Subcellular localization.
Phosphotriesterase is a membrane-associated protein that is translated with a 29 amino acid-long target peptide (Tat motif), which is then cleaved from the mature protein after insertion in the plasma membrane. The protein is anchored to the inner membrane of the cell, facing the periplasm.
Function.
The enzyme phosphotriesterase hydrolyzes organophosphate compounds by cleaving the triester linkage in the substrate.
The enzyme has a very broad substrate specificity, and is very efficient in catalyzing the reaction: PTE hydrolyzes paraoxon at a rate approaching the diffusion limit, which indicates that the enzyme is optimally evolved for using this substrate. It acts specifically on synthetic organophosphate triesters and phosphorofluoridates. It does not seem to have a natural occurring substrate and may thus have optimally evolved for utilizing paraoxon and other common agricultural pesticides.
The products of the reaction are diethyl phosphoric acid and "p"-nitrophenol. The latter product is further degraded by an enzyme encoded 750bp downstream of the "opd" gene, and encodes a 29kDa putative hydrolase that may be involved in degrading aromatic compounds, and works in concert with PTE. This enzyme is homologous to hydrolases in "Pseudomonas putida", "Pseudomonas azelaica", "Rhodococcus" sp., and "P. fluorescens".
Organophosphates are not toxic to bacteria, but they act as acetylcholinesterase inhibitors in animals. Some species of bacteria are also able to utilize organophosphates as a nutrient and carbon source.
Environmental significance.
Phosphotriesterases are considered a strong candidate biocatalyst for bioremediation purposes. Its wide substrate specificity and catalytic efficiency makes it an attractive target for the potential use of microbes containing the opd gene in detoxifying soils that are toxic due to pesticide overuse. Moreover, organophosphates act as acetylcholinesterase (AChE) inhibitors. The AChE neurotransmitter is a vital component of the central nervous system (CNS) in insects in animals, and the inhibition of the proper turnover of this neurochemical results in overstimulation of the CNS, which ultimately results in death of insects and mammals. As a result, the use of organophosphate-degrading microorganisms is a potentially effective, low-cost, and environmentally friendly method of removing these toxic compounds from the environment.
History.
Bacterial species that had the ability to degrade organophosphate pesticides have been isolated from soil samples from different parts of the world. The first bacterial strain identified to be able to hydrolyze organophosphates was "Flavobacterium" sp. ATCC 27551, found by Sethunathan and Yoshida in 1973 from a soil sample originally from the Philippines. Since then, other species were found to also have organophosphate-degrading enzymes similar to that found in "Flavobacterium""."
References.
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Further reading.
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[
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https://en.wikipedia.org/wiki?curid=14454224
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14454452
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Aminoacyl-tRNA hydrolase
|
The enzyme aminoacyl-tRNA hydrolase (EC 3.1.1.29) catalyzes the reaction
"N"-substituted aminoacyl-tRNA + H2O formula_0 "N"-substituted amino acid + tRNA
This enzyme belongs to the family of hydrolases, specifically those acting on carboxylic ester bonds. The systematic name is aminoacyl-tRNA aminoacylhydrolase. Other names in common use include aminoacyl-transfer ribonucleate hydrolase, "N"-substituted aminoacyl transfer RNA hydrolase, and peptidyl-tRNA hydrolase.
Structural studies.
As of late 2007, 9 structures have been solved for this class of enzymes, with PDB accession codes 1RYB, 1WN2, 1XTY, 2D3K, 2E1B, 2PTH, 2Z2I, 2Z2J, and 2Z2K.
References.
<templatestyles src="Reflist/styles.css" />
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[
{
"math_id": 0,
"text": "\\rightleftharpoons"
}
] |
https://en.wikipedia.org/wiki?curid=14454452
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14454545
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Bicycle tire
|
Tire that fits on the wheel of a bicycle
A bicycle tire is a tire that fits on the wheel of a bicycle or similar vehicle. These tires may also be used on tricycles, wheelchairs, and handcycles, frequently for racing. Bicycle tires provide an important source of suspension, generate the lateral forces necessary for balancing and turning, and generate the longitudinal forces necessary for propulsion and braking. Although the use of a pneumatic tire greatly reduces rolling resistance compared to the use of a rigid wheel or solid tire, the tires are still typically the second largest source, after wind resistance (air drag), of power consumption on a level road. The modern detachable pneumatic bicycle tire contributed to the popularity and eventual dominance of the safety bicycle.
Bicycle tires are also used on unicycles, tricycles, quadracycles, tandem bicycles, hand cycles, bicycle trailers, and trailer bikes.
History.
The first bicycle "tires" were iron bands on the wooden wheels of velocipedes. These were followed by solid rubber tires on penny-farthings. The first patent for "rubberized wheels" was granted to Clément Ader in 1868. In an attempt to soften the ride, rubber tires with a hollow core were also tried.
The first practical pneumatic tire was made by John Boyd Dunlop in 1887 for his son's bicycle, in an effort to prevent the headaches his son had while riding on rough roads. (Dunlop's patent was later declared invalid because of prior art by fellow Scot Robert William Thomson.) Dunlop is credited with "realizing rubber could withstand the wear and tear of being a tire while retaining its resilience". This led to the founding of Dunlop Pneumatic Tyre Co. Ltd in 1889. By 1890, it began adding a tough canvas layer to the rubber to reduce punctures. Racers quickly adopted the pneumatic tire for the increase in speed and ride quality it enabled.
Finally, the detachable tire was introduced in 1891 by Édouard Michelin. It was held on the rim with clamps, instead of glue, and could be removed to replace or patch the separate inner tube.
Attaching to the rim.
Three main techniques for attaching a bicycle tire to a bicycle rim have been developed: "clincher", "wired" and "tubular". Clinchers originally did not have wire in the beads and the shape of the bead interlocked with a flange on the rim, relying on air pressure to hold the tire bead in place. However, this type of tire is no longer in general use and the term "clincher" has transferred to the modern wired-on tire. For the remainder of this article, the modern use of the word "clincher" will be assumed.
In an attempt to provide the best attributes of both wired and tubular methods, tubular clinchers have also been offered.
Clincher.
Most bicycle tires are clincher types for use with "clincher" rims. These tires have a steel wire or Kevlar fiber bead that interlocks with flanges inside of the rim. A separate airtight inner tube enclosed by the tire supports the tire carcass and maintains the bead lock. An advantage of this system is that the inner tube can be easily accessed for a patch repair or replacement of the tube.
The ISO 5775-2 standard defines designations for bicycle rims. It distinguishes between
Traditional wired-on rims were straight-sided. Various "hook" (also called "crochet") designs re-emerged in the 1970s to seat the tire bead on the wheel rim and hold the tire in place, resulting in the modern clincher design. This allows higher () air pressures than was possible older wired-on tires. In these designs, it is the interlocking of the bead with the rim flanges, not the tight fit or resistance to stretching of the bead, that keeps the tire on the rim and retains the air pressure.
Some clincher tires can be used without tubes in a system which is referred to as tubeless. Typical tubeless tires have airtight sidewalls and beads which are designed to maximize the seal between the tyre and the wheel rim.
Tubular or sew-up.
Some tires are torus-shaped and attached to tubular rims with adhesive. Tubular rims are designed with shallow circular cross-section beds in which the tires seat instead of being attached to rim flanges by tire beads as in clincher types.
Providing suspension.
Adequate tire casing stiffness is necessary to support the rider, while softness and flexibility in the casing is desirable for cushioning. Most bicycle tires are pneumatic, the stiffness of the tires is easily controlled by controlling the air pressure inside of the tire. Airless tires utilize a semi solid sponge type elastomer material which eliminates air loss through punctures and air seepage.
Pneumatic tires.
In a pneumatic tire, pressurized air is held inside either with a separate, relatively impermeable inner tube, or by the tire and rim, in a tubeless system. Pneumatic tires are superior in providing effective cushioning while keeping rolling resistance very low.
Tubed.
A tubed tire has a separate inner tube, made of butyl rubber or latex, that provides a relatively airtight barrier inside the tire. A vast majority of the tire systems in use are clinchers, due to the relative simplicity of repairs and wide availability of replacement inner tubes.
Most of bicycle inner tubes are torus-shaped balloons while some are not. For example, inner tubes in bicycles of the Moscow bike-sharing service are simply rubber tubes long enough to be coiled and inserted into a tire.
Tubeless.
Tubeless tires are primarily used on mountain bikes due to their ability to use low air pressure for better traction without getting pinch flats. Tubeless tires work similarly to clinchers in that the bead of the tire is specifically designed to interlock into a corresponding tubeless rim, but without an inner tube. Air is inflated directly into the tire, and once "locked" into the rim, the system is airtight. Liquid sealants are often injected into tubeless tires to improve sealing and to stop leaks caused by punctures. An advantage is that pinch flats are less common in a tubeless setup because they require a hole through the tire carcass, not just the inner tube. A disadvantage is that air can escape if the bead lock is compromised from too much lateral force on the tire or deformation of the rim/tire due to hard impact with an object.
Tubeless tires require tubeless-compatible rims, which do not allow air to escape where the spokes connect and have a different shape groove for the tire bead to seat.
Road tubeless.
In 2006, Shimano and Hutchinson introduced a tubeless system for road bicycles. Tubeless tires have not yet gained popular acceptance in road racing due to lack of sponsorship, the tradition of using tubular tires and the fact that, even without the inner tube, the combined weight of tubeless rims and tires is more than top-of-the-line tubular tire wheelsets. Road tubeless is gaining popularity among riders for whom the benefits are worth the costs. Road tubeless tires tend to be a much tighter fit than traditional clincher tires, which makes mounting and removing the tire more difficult.
Airless tires.
Airless were used before pneumatic tires were developed, appearing on velocipedes by 1869. They continue to be developed in an effort to solve the problem of losing air pressure, either from a puncture or from permeability. Modern examples of airless tires for bicycles include BriTek's Energy Return Wheel, an airless bicycle tire from Bridgestone,
the tire pictured to the right on a Mobike, and solid tires discussed below.
Although modern airless tires are better than early ones, most give a rough ride and may damage the wheel or bicycle.
Solid.
The most common form of airless tire is simply the solid tire. Besides solid rubber, solid tires made of polyurethane or microcellular foam are also offered for 100% flat prevention. Much of the desirable suspension quality of the pneumatic tire is lost, however, and ride quality suffers.
Many bicycle-sharing systems use these tires to reduce maintenance, and examples of solid tires include those available from Greentyre, Puncture Proof Tyres Ltd, KIK-Reifen, Tannus, Hutchinson, and Specialized.
Construction.
Bicycle tires consist of a rubber-impregnated cloth casing, also called the carcass, with additional rubber, called the tread, on the surface that contacts the road. In the case of clinchers, the casing wraps around two beads, one on each edge.
Casing.
Bicycle tire casing is made of cloth, usually nylon, though cotton and silk have also been used. The casing provides the resistance against stretching necessary to contain the internal air pressure while remaining flexible enough to conform to the ground surface. The thread count of the cloth affects the weight and performance of the tire, and high thread counts improve ride quality and reduce rolling resistance at the expense of durability and puncture resistance.
Bias ply.
The fibers of the cloth in most bicycle tires are not woven together, but kept in separate plies so that they can move more freely to reduce wear and rolling resistance. They are also usually oriented diagonally, forming bias plies.
Radial ply.
Radial ply has been attempted, and examples include Panasonic in the 1980s and the Maxxis in the 2010s, but often found to provide undesirable handling characteristics.
Tread.
<templatestyles src="Stack/styles.css"/>
The tread is the part of the tire that contacts the ground to provide grip and protect the casing from wear.
The tread is made of natural and synthetic rubber that often includes fillers such as carbon black, which gives it its characteristic color, and silica. The type and amount of filler is selected based on characteristics such as wear, traction (wet and dry), rolling resistance, and cost. Oils and lubricants may be added as softeners. Sulphur and zinc oxide facilitate vulcanization. Some tires have a dual-compound tread that is tougher in the middle and grippier on the edges. Many modern tires are available with treads in a variety or combination of colors. Road racing tires with different tread compounds for the front and rear have been developed, thereby attempting to provide more traction in front and less rolling resistance in the rear.
Treads fall somewhere along the spectrum from smooth or slick to knobby. Smooth treads are intended for on-road use, where a tread pattern offers little to no improvement in traction. However, many otherwise slick tires have a light tread pattern, due to the common misbelief that a slick tire will be slippery in wet conditions. Knobby treads are intended for off-road use, where the tread texture can help improve traction on soft surfaces. Many treads are omnidirectional—the tire can be installed in either orientation—but some are unidirectional and designed to be oriented in a specific direction. Some tires, especially for mountain bikes, have a tread which is intended either for the front wheel or the rear wheel. A special tread pattern, with small dimples, has been developed to reduce air drag.
The profile of the tread is usually circular, matching the shape of the casing inside it and allowing the tire to roll to the side as the bicycle leans for turning or balancing. More-squared profiles are sometimes used on mountain bike tires and novelty tires designed to look like automotive racing slicks, as on wheelie bikes.
Bead.
The bead of clincher tires must be made of a material that will stretch very little to prevent the tire from expanding off of the rim under internal air pressure.
Steel wire beads are used on inexpensive tires. Though they cannot be folded, they can often be twisted into three smaller hoops.
Kevlar beads are used on expensive tires, and these are also called "foldable". They should not be used on straight sidewall rims as they may blow off the rim.
Sidewall.
The sidewall of the casing, the part not intended to contact the ground, may receive one of several treatments.
Tires with sidewalls made of natural rubber are called "gum wall". The tan colored, natural rubber lacks carbon black to decrease rolling resistance, as its added wear resistance isn't needed in the sidewall.
Tires with very little rubber, if any, covering the sidewall are called "skin wall". This reduces rolling resistance by reducing sidewall stiffness at the cost of reducing damage protection.
Variations.
Puncture resistance.
Some tires include an extra layer between the tread and the casing (as shown in the cross section pictured above) to help prevent punctures either by being tough or simply by being thick. These extra layers are usually associated with higher rolling resistance.
Studs.
Metal studs may be embedded in the tread of knobby tires to improve traction on ice. Inexpensive studded tires use steel studs, while pricier tires use more durable carbide studs. A studded, knobby tread that zips onto a smoother, non-studded tire has been developed to ease the transition between the two types of tires.
Reflective.
Some tires have a reflective strip on their sidewalls to improve visibility at night. Others have reflective material embedded in the tread.
Aerodynamics.
In addition to the dimple tread pattern mentioned above, at least one tire has an extra "wing" to cover the gap between the tire sidewall and the wheel rim and reduce drag.
Indoor use.
At least one modern bicycle tire has been designed specifically for indoor use on rollers or trainers. It minimizes excessive wear that traditional tires experience in this environment and is not suitable for use on pavement.
Different front and rear.
Besides the different tread patterns available on some mountain bike tires mentioned above, front and rear tire sets are available for road bikes with different tread patterns, tread compounds, and sizes for the front and rear wheels. Other scenarios involve replacing a damaged tire, and leaving the other one unchanged.
Self inflating.
Bicycle tires have been developed that pump themselves up as they roll forward.
Modular.
Bicycle tires have been developed so that different treads can be zipped on and off. This allows having the additional traction of studded tires only when necessary and avoiding the additional rolling resistance otherwise.
Parameters.
Sizes.
The modern tire-size designations (e.g. "37-622", also known as ETRTO) are defined by international standard ISO 5775, along with corresponding rim size designations (e.g., "622×19C"). Older English (inch, e.g. "28 × <templatestyles src="Fraction/styles.css" />1+5⁄8 × <templatestyles src="Fraction/styles.css" />1+3⁄8") and French (metric, e.g. "700×35C") designations are also still used, but can be ambiguous. The diameter of the tire must match the diameter of the rim, but the width of the tire only has to be in the range of widths appropriate for the width of the rim, while also not exceeding the clearances allowed by the frame, brakes, and any accessories such as fenders. Diameters vary from a large 910 mm, for touring unicycles, to a small 125 mm, for roller skiing. Widths vary from a narrow 18 mm to a wide 119 mm for the Surly Big Fat Larry.
Lightweight tires.
Lightweight tires range in size from wide.
Middleweight or Demi-balloon tires.
Middleweight or Demi-balloon tires range in size from wide.
Balloon tires.
A balloon tire is a type of wide, large-volume, low-pressure tire that first appeared on cruiser bicycles in the US in the 1930s. They are typically wide.
In the 1960s Raleigh made its small-wheeled RSW 16 with balloon tires so it would have a soft ride like the fully suspended Moulton Bicycle. Other manufacturers then used the same idea for their own small wheelers. Examples include the Stanningley (UK)-made Bootie Folding Bicycle, the Co-operative Wholesale Society (CWS) Commuter, and the Trusty Spacemaster.
Plus-size tires.
A plus-size tire has a width of typically . Three bead seat diameters are available: 559 mm for 26+, 584 mm for 27.5+ (650B+), and 622 mm for 29+. They fill the gap between balloon and fat tires.
Fat tires.
A fat tire is a type of wide oversized bicycle tire, typically or larger and rims or wider, designed for low ground pressure to allow riding on soft unstable terrain, such as snow, sand, bogs, and mud.
Since the 1980s, fat tires of width , and diameters similar to conventional bicycle wheels, have been used on "fatbikes" and all-terrain bikes designed for riding in snow and sand.
Inflation pressure.
The inflation pressure of bicycle tires ranges from for fat bike tires in snow to for tubular track racing tires.
The maximum pressure rating of tires is usually stamped on the sidewall, indicated as "Maximum Pressure", or "Inflate to ..." or sometimes expressed as a range like "". Decreasing pressure tends to increase traction and make the ride more comfortable while increasing pressure tends to make the ride more efficient and decreases the chances of getting pinch flats.
One published guideline for clincher inflation pressure is to pick the value for each wheel that produces a 15% reduction in the distance between the wheel rim and the ground when loaded (i.e. with the rider and cargo) compared to when unloaded. Pressures below this leads to increased rolling resistance and likelihood of pinch-flats. Pressures above this leads to less rolling resistance in the tire itself but to larger total energy dissipation caused by passing vibrations to the bike and especially the rider, which experience elastic hysterisis.
Inner tubes are not completely impermeable to air and slowly lose pressure over time. Butyl inner tubes hold pressure better than latex. Tires inflated from carbon dioxide canisters (often used for roadside repairs) or helium (occasionally used for elite track racing) lose pressure more quickly, because carbon dioxide, despite being a relatively large molecule, is slightly soluble in rubber, and helium is a very small atom which passes quickly through any porous material. At least one public bicycle sharing system, London's Santander Cycles, is inflating tires with nitrogen, instead of simple air, which is already 78% nitrogen, in an attempt to keep the tires at the proper inflation pressure longer, though the effectiveness of this is debatable.
Effect of temperature.
Since the volume of gas and the gas itself inside a tire is not altered significantly by a change of temperature, the ideal gas law states that the pressure of the gas should be directly proportional to the absolute temperature. Thus, if a tire is inflated to at room temperature, , the pressure will increase to (+10%)
at and decrease to (-10%) at .
In the example above, a 7% difference in absolute temperature resulted in a 10% difference in tire pressure. This is a result of the difference between gauge pressure and absolute pressure. For low inflation pressures, this distinction is more important, as the ideal gas law applies to absolute pressure, including atmospheric pressure. For example, if a fat-bike tire is inflated to gauge pressure at room temperature and then the temperature is decreased to (a 9% decrease in absolute temperature), the absolute pressure of will be decreased by 9% to , which translates to a 30% decrease in gauge pressure, to .
Effect of atmospheric pressure.
The net air pressure on the tire is the difference between the internal inflation pressure and the external atmospheric pressure, , and most tire pressure gauges report this difference. If a tire is inflated to at sea level, the absolute internal pressure would be (+25%), and this is the pressure that the tire would need to contain if it were moved to a location with no atmospheric pressure, such as the vacuum of free space. At the highest elevation of commercial air travel, , the atmospheric pressure is reduced to , and that same tire would have to contain (+20%).
Effect on carcass stress.
Bicycle tires are essentially toroidal thin-walled pressure vessels and if the carcass is treated as a homogeneous and isotropic material then stress in the "toroidal" direction ("longitudinal" or "axial" stress if the tire is considered a long cylinder) can be calculated as:
formula_0,
where:
Stress in the "poloidal" direction ("hoop" or "circumferential" stress if the tire is considered a long cylinder) is more complicated, varying around the minor circumference and depending on the ratio between the major and minor radii, but if the major radius is much larger than the minor radius, as on most bicycle tires where the major radius is measure in hundreds of mm and the minor radius is measured in tens of mm, then stress in the Poloidal direction is close to the hoop stress of cylindrical thin-walled pressure vessels:
formula_1.
In reality, of course, the tire carcass is not homogeneous nor isotropic, but instead is a composite material with fibers imbedded in a rubber matrix, which complicates things further.
Rim width.
While not strictly a tire parameter, the width of the rim on which any given tire is mounted has an influence on the size and shape of the contact patch, and possibly the rolling resistance and handling characteristics. The European Tyre and Rim Technical Organisation (ETRTO) publishes a guideline of recommended rim widths for different tire widths:
In 2006, it was expanded for allowing wide tires up to 50mm on 17C rims and 62mm on 19C rims.
Ideally, the tire width should be 1.8 to 2 times the rim width, but a ratio from 1.4 to 2.2 should fit, and even 3 for hooked rims.
Tire pressure versus width.
Mavic recommends maximum pressures in addition to rim width, and Schwalbe recommends specific pressures:
Fatbike tires of width are typically mounted on 65 to 100 mm rims.
Forces and moments generated.
Bicycle tires generate forces and moments between the wheel rim and the pavement that can affect bicycle performance, stability, and handling.
Vertical force.
The vertical force generated by a bicycle tire is approximately equal to the product of inflation pressure and contact patch area. In reality, it is usually slightly more than this because of the small but finite rigidity of the sidewalls.
The vertical stiffness, or spring rate, of a bicycle tire, as with motorcycle and automobile tires, increases with inflation pressure.
Rolling resistance.
Rolling resistance is a complex function of vertical load, inflation pressure, tire width, wheel diameter, the materials and methods used to construct the tire, roughness of the surface on which it rolls, and the speed at which it rolls. Rolling resistance coefficients may vary from 0.002 to 0.010, and have been found to increase with vertical load, surface roughness, and speed. Conversely, increased inflation pressure (up to a limit), wider tires (compared to narrower tires at the same pressure and of the same material and construction), larger-diameter wheels, thinner casing layers, and more-elastic tread material all tend to decrease rolling resistance.
For example, a study at the University of Oldenburg found that Schwalbe Standard GW HS 159 tires, all with a width of 47 mm and an inflation pressure of , but made for various diameter rims, had the following rolling resistances:
The author of the cited paper concludes, based on the data presented therein, that Crr is inversely proportional to inflation pressure and to wheel diameter.
Although increasing inflation pressure tends to decrease rolling resistance because it reduces tire deformation, on rough surfaces increasing inflation pressure tends to increase the vibration experienced by the bicycle and rider, where that energy is dissipated in their less-than-perfectly-inelastic deformation. Thus, depending on the myriad of factors involved, increasing inflation pressure can lead to increasing total energy dissipation and either slower speed or higher energy consumption.
Cornering force and camber thrust.
As with other pneumatic tires, bicycle tires generate cornering force that varies with slip angle and camber thrust that varies with camber angle. These forces have been measured by several researchers since the 1970s, and have been shown to influence bicycle stability.
Moments.
Moments generated in the contact patch by a pneumatic tire include the self aligning torque associated with cornering force, twisting torque associated with camber thrust, both about a vertical axis, and an overturning moment about the roll axis of the bike.
References.
<templatestyles src="Reflist/styles.css" />
|
[
{
"math_id": 0,
"text": "\\sigma_{toroidal} = \\frac{pr}{2t}"
},
{
"math_id": 1,
"text": "\\sigma_{poloidal} = \\frac{pr}{t}"
}
] |
https://en.wikipedia.org/wiki?curid=14454545
|
14454675
|
Arylesterase
|
The enzyme arylesterase (EC 3.1.1.2) catalyzes the reaction
a phenyl acetate + H2O formula_0 a phenol + acetate
This enzyme belongs to the family of hydrolases, specifically those acting on carboxylic ester bonds. The systematic name of this enzyme class is aryl-ester hydrolase. Other names in common use include A-esterase, paraoxonase, and aromatic esterase. This enzyme participates in bisphenol a degradation.
Structural studies.
As of late 2007, two structures have been solved for this class of enzymes, with PDB accession codes 1V04 and 1VA4.
References.
<templatestyles src="Reflist/styles.css" />
|
[
{
"math_id": 0,
"text": "\\rightleftharpoons"
}
] |
https://en.wikipedia.org/wiki?curid=14454675
|
14454687
|
Bile-acid-CoA hydrolase
|
In enzymology, a bile-acid-CoA hydrolase (EC 3.1.2.26) is an enzyme that catalyzes the chemical reaction
deoxycholoyl-CoA + H2O formula_0 CoA + deoxycholate
Thus, the two substrates of this enzyme are deoxycholoyl-CoA and H2O, whereas its two products are CoA and deoxycholate.
This enzyme belongs to the family of hydrolases, specifically those acting on thioester bonds. The systematic name of this enzyme class is deoxycholoyl-CoA hydrolase.
References.
<templatestyles src="Reflist/styles.css" />
|
[
{
"math_id": 0,
"text": "\\rightleftharpoons"
}
] |
https://en.wikipedia.org/wiki?curid=14454687
|
14454695
|
Delta-v (physics)
|
In general physics, delta-"v" is a change in velocity. The Greek uppercase letter Δ (delta) is the standard mathematical symbol to represent change in some quantity.
Depending on the situation, delta-"v" can be either a spatial vector (Δv) or a scalar (Δ"v"). In either case it is equal to the acceleration (vector or scalar) integrated over time:
If acceleration is constant, the change in velocity can thus be expressed as:
formula_2
where:
Change in velocity is useful in many cases, such as determining the change in momentum (impulse), where: formula_3, where formula_4 is momentum and m is mass.
|
[
{
"math_id": 0,
"text": "\\Delta \\mathbf{v} = \\mathbf{v}_1 - \\mathbf{v}_0 = \\int^{t_1}_{t_0} \\mathbf {a} \\, dt"
},
{
"math_id": 1,
"text": "\\Delta v = {v}_1 - {v}_0 = \\int^{t_1}_{t_0} a \\, dt"
},
{
"math_id": 2,
"text": "\\Delta \\mathbf{v} = \\mathbf{v}_1 - \\mathbf{v}_0 = \\mathbf{a} \\times \\Delta t = \\mathbf{a} \\times (t_1-t_0)"
},
{
"math_id": 3,
"text": "\\Delta \\mathbf{p} = m \\Delta \\mathbf{v}"
},
{
"math_id": 4,
"text": "\\mathbf{p}"
}
] |
https://en.wikipedia.org/wiki?curid=14454695
|
14454706
|
Bis(2-ethylhexyl)phthalate esterase
|
The enzyme bis(2-ethylhexyl)phthalate esterase (EC 3.1.1.60) catalyzes the reaction
bis(2-ethylhexyl)phthalate + H2O formula_0 2-ethylhexyl phthalate + 2-ethylhexan-1-ol
This enzyme belongs to the family of hydrolases, specifically those acting on carboxylic ester bonds. The systematic name is bis(2-ethylhexyl)phthalate acylhydrolase. This enzyme is also called DEHP esterase.
References.
<templatestyles src="Reflist/styles.css" />
|
[
{
"math_id": 0,
"text": "\\rightleftharpoons"
}
] |
https://en.wikipedia.org/wiki?curid=14454706
|
14454720
|
Bisphosphoglycerate phosphatase
|
In enzymology, a bisphosphoglycerate phosphatase (EC 3.1.3.13) is an enzyme that catalyzes the chemical reaction
2,3-bisphospho-D-glycerate + H2O formula_0 3-phospho-D-glycerate + phosphate
Thus, the two substrates of this enzyme are 2,3-bisphospho-D-glycerate and H2O, whereas its two products are 3-phospho-D-glycerate and phosphate.
This enzyme belongs to the family of hydrolases, specifically those acting on phosphoric monoester bonds. The systematic name of this enzyme class is 2,3-bisphospho-D-glycerate 2-phosphohydrolase. Other names in common use include 2,3-diphosphoglycerate phosphatase, diphosphoglycerate phosphatase, 2,3-diphosphoglyceric acid phosphatase, 2,3-bisphosphoglycerate phosphatase, and glycerate-2,3-diphosphate phosphatase. This enzyme participates in glycolysis/gluconeogenesis.
Structural studies.
As of late 2007, 7 structures have been solved for this class of enzymes, with PDB accession codes 1YFK, 1YJX, 2F90, 2H4X, 2H4Z, 2H52, and 2HHJ.
References.
<templatestyles src="Reflist/styles.css" />
|
[
{
"math_id": 0,
"text": "\\rightleftharpoons"
}
] |
https://en.wikipedia.org/wiki?curid=14454720
|
14454743
|
Caldesmon-phosphatase
|
The enzyme caldesmon-phosphatase (EC 3.1.3.55) catalyzes the reaction
caldesmon phosphate + H2O formula_0 caldesmon + phosphate
This enzyme belongs to the family of hydrolases, specifically those acting on phosphoric monoester bonds. The systematic name is caldesmon-phosphate phosphohydrolase. Other names in common use include SMP-I, and smooth muscle caldesmon phosphatase.
References.
<templatestyles src="Reflist/styles.css" />
|
[
{
"math_id": 0,
"text": "\\rightleftharpoons"
}
] |
https://en.wikipedia.org/wiki?curid=14454743
|
14454999
|
Carboxylesterase
|
The enzyme carboxylesterase (or carboxylic-ester hydrolase, EC 3.1.1.1; systematic name carboxylic-ester hydrolase) catalyzes reactions of the following form:
a carboxylic ester + H2O formula_0 an alcohol + a carboxylate
Most enzymes from this group are serine hydrolases belonging to the superfamily of proteins with α/β hydrolase fold. Some exceptions include an esterase with β-lactamase-like structure (PDB: 1ci8).
Carboxylesterases are widely distributed in nature, and are common in mammalian liver. Many participate in phase I metabolism of xenobiotics such as toxins or drugs; the resulting carboxylates are then conjugated by other enzymes to increase solubility and eventually excreted. The essential polyunsaturated fatty acid arachidonic acid (AA C20H32O2; 20:4, n-6), formed by the synthesis from dietary linoleic acid (LA: C18H32O2 18:2, n-6), has a role as a human carboxylesterase inhibitor.
The carboxylesterase family of evolutionarily related proteins (those with clear sequence homology to each other) includes a number of proteins with different substrate specificities, such as acetylcholinesterases.
Examples.
<templatestyles src="Div col/styles.css"/>
The last enzyme also participates in alkaloid biosynthesis.
Genes.
Humans genes that encode carboxylesterase enzymes include:
An approved nomenclature has been established for the five mammalian carboxylesterase gene families.
References.
<templatestyles src="Reflist/styles.css" />
Further reading.
<templatestyles src="Refbegin/styles.css" />
|
[
{
"math_id": 0,
"text": "\\rightleftharpoons"
}
] |
https://en.wikipedia.org/wiki?curid=14454999
|
14455080
|
Carboxymethylenebutenolidase
|
Class of enzymes
In enzymology, a carboxymethylenebutenolidase (EC 3.1.1.45, also known as CMBL and dienelactone hydrolase) is an enzyme that catalyzes the chemical reaction
4-carboxymethylenebut-2-en-4-olide + H2O formula_0 4-oxohex-2-enedioate
Thus, the two substrates of this enzyme are 4-carboxymethylenebut-2-en-4-olide and H2O, whereas its product is 4-oxohex-2-enedioate.
This enzyme belongs to the family of hydrolases, specifically those acting on carboxylic ester bonds. The systematic name of this enzyme class is 4-carboxymethylenebut-2-en-4-olide lactonohydrolase. Other names in common use include maleylacetate enol-lactonase, dienelactone hydrolase, and carboxymethylene butenolide hydrolase. This enzyme participates in gamma-hexachlorocyclohexane degradation and 1,4-dichlorobenzene degradation.
Structural studies.
As of late 2007, 10 structures have been solved for this class of enzymes, with PDB accession codes 1DIN, 1GGV, 1ZI6, 1ZI8, 1ZI9, 1ZIC, 1ZIX, 1ZIY, 1ZJ4, and 1ZJ5.
References.
<templatestyles src="Reflist/styles.css" />
|
[
{
"math_id": 0,
"text": "\\rightleftharpoons"
}
] |
https://en.wikipedia.org/wiki?curid=14455080
|
14455102
|
Cephalosporin-C deacetylase
|
The enzyme cephalosporin-C deacetylase (EC 3.1.1.41) catalyzes the reaction
cephalosporin C + H2O formula_0 deacetylcephalosporin C + acetate
This enzyme belongs to the family of hydrolases, specifically those acting on carboxylic ester bonds. The systematic name is cephalosporin-C acetylhydrolase. Other names in common use include cephalosporin C acetyl-hydrolase, cephalosporin C acetylase, cephalosporin acetylesterase, cephalosporin C acetylesterase, cephalosporin C acetyl-esterase, and cephalosporin C deacetylase. This enzyme participates in penicillin and cephalosporin biosynthesis.
Structural studies.
As of late 2007, 4 structures have been solved for this class of enzymes, with PDB accession codes 1L7A, 1ODS, 1ODT, and 1VLQ.
References.
<templatestyles src="Reflist/styles.css" />
|
[
{
"math_id": 0,
"text": "\\rightleftharpoons"
}
] |
https://en.wikipedia.org/wiki?curid=14455102
|
14455129
|
Cetraxate benzylesterase
|
The enzyme cetraxate benzylesterase (EC 3.1.1.70) catalyzes the reaction
cetraxate benzyl ester + H2O formula_0 cetraxate + benzyl alcohol
This enzyme belongs to the family of hydrolases, specifically those acting on carboxylic ester bonds. The systematic name is cetraxate-benzyl-ester benzylhydrolase.
References.
<templatestyles src="Reflist/styles.css" />
|
[
{
"math_id": 0,
"text": "\\rightleftharpoons"
}
] |
https://en.wikipedia.org/wiki?curid=14455129
|
14455153
|
Chlorogenate hydrolase
|
The enzyme chlorogenate hydrolase (EC 3.1.1.42) catalyzes the reaction
chlorogenate + H2O formula_0 caffeate + quinate
This enzyme belongs to the family of hydrolases, specifically those acting on carboxylic ester bonds. The systematic name is chlorogenate hydrolase. Other names in common use include chlorogenase, and chlorogenic acid esterase.
References.
<templatestyles src="Reflist/styles.css" />
|
[
{
"math_id": 0,
"text": "\\rightleftharpoons"
}
] |
https://en.wikipedia.org/wiki?curid=14455153
|
14455181
|
Choline-sulfatase
|
The enzyme choline-sulfatase (EC 3.1.6.6) catalyzes the reaction
choline sulfate + H2O formula_0 choline + sulfate
This enzyme belongs to the family of hydrolases, specifically those acting on sulfuric ester bonds. The systematic name is choline-sulfate sulfohydrolase.
References.
<templatestyles src="Reflist/styles.css" />
|
[
{
"math_id": 0,
"text": "\\rightleftharpoons"
}
] |
https://en.wikipedia.org/wiki?curid=14455181
|
14455205
|
Choloyl-CoA hydrolase
|
The enzyme choloyl-CoA hydrolase (EC 3.1.2.27) catalyzes the reaction
choloyl-CoA + H2O formula_0 cholate + CoA
This enzyme belongs to the family of hydrolases, specifically those acting on thioester bonds. The systematic name is choloyl-CoA hydrolase. Other names in common use include PTE-2 (ambiguous), choloyl-coenzyme A thioesterase, chenodeoxycholoyl-coenzyme A thioesterase, and peroxisomal acyl-CoA thioesterase 2.
References.
<templatestyles src="Reflist/styles.css" />
|
[
{
"math_id": 0,
"text": "\\rightleftharpoons"
}
] |
https://en.wikipedia.org/wiki?curid=14455205
|
14455231
|
Chondro-4-sulfatase
|
The enzyme chondro-4-sulfatase (EC 3.1.6.9) catalyzes the reaction
4-deoxy-β--gluc-4-enuronosyl-(1→3)-"N"-acetyl--galactosamine 4-sulfate + H2O formula_0 4-deoxy-β--gluc-4-enuronosyl-(1→3)-"N"-acetyl--galactosamine + sulfate
This enzyme belongs to the family of hydrolases, specifically those acting on sulfuric ester bonds. The systematic name is 4-deoxy-β--gluc-4-enuronosyl-(1→3)-"N"-acetyl--galactosamine-4-sulfate 4-sulfohydrolase. This enzyme is also called chondroitin-4-sulfatase.
References.
<templatestyles src="Reflist/styles.css" />
|
[
{
"math_id": 0,
"text": "\\rightleftharpoons"
}
] |
https://en.wikipedia.org/wiki?curid=14455231
|
14455242
|
Chondro-6-sulfatase
|
The enzyme chondro-6-sulfatase (EC 3.1.6.10) catalyzes the reaction
4-deoxy-β--gluc-4-enuronosyl-(1→3)-"N"-acetyl--galactosamine 6-sulfate + H2O formula_0 4-deoxy-β--gluc-4-enuronosyl-(1→3)-"N"-acetyl--galactosamine + sulfate
This enzyme belongs to the family of hydrolases, specifically those acting on sulfuric ester bonds. The systematic name is 4-deoxy-β--gluc-4-enuronosyl-(1→3)-"N"-acetyl--galactosamine-6-sulfate 6-sulfohydrolase.
References.
<templatestyles src="Reflist/styles.css" />
|
[
{
"math_id": 0,
"text": "\\rightleftharpoons"
}
] |
https://en.wikipedia.org/wiki?curid=14455242
|
14455290
|
CMP-N-acylneuraminate phosphodiesterase
|
Enzyme
The enzyme CMP-"N"-acylneuraminate phosphodiesterase (EC 3.1.4.40) catalyzes the reaction
CMP-"N"-acylneuraminate + H2O formula_0 CMP + "N"-acylneuraminate
This enzyme belongs to the family of hydrolases, specifically those acting on phosphoric diester bonds. The systematic name of this enzyme class is CMP-"N"-acylneuraminate "N"-acylneuraminohydrolase. Other names in common use include CMP-sialate hydrolase, CMP-sialic acid hydrolase, CMP-"N"-acylneuraminic acid hydrolase, cytidine monophosphosialic hydrolase, cytidine monophosphosialate hydrolase, cytidine monophosphate-"N"-acetylneuraminic acid hydrolase, and CMP-"N"-acetylneuraminate hydrolase.
References.
<templatestyles src="Reflist/styles.css" />
|
[
{
"math_id": 0,
"text": "\\rightleftharpoons"
}
] |
https://en.wikipedia.org/wiki?curid=14455290
|
144553
|
Projectile
|
Object propelled through the air
A projectile is an object that is propelled by the application of an external force and then moves freely under the influence of gravity and air resistance. Although any objects in motion through space are projectiles, they are commonly found in warfare and sports (for example, a thrown baseball, kicked football, fired bullet, shot arrow, stone released from catapult).
In ballistics mathematical equations of motion are used to analyze projectile trajectories through launch, flight, and impact.
Motive force.
Blowguns and pneumatic rifles use compressed gases, while most other guns and cannons utilize expanding gases liberated by sudden chemical reactions by propellants like smokeless powder. Light-gas guns use a combination of these mechanisms.
Railguns utilize electromagnetic fields to provide a constant acceleration along the entire length of the device, greatly increasing the muzzle velocity.
Some projectiles provide propulsion during flight by means of a rocket engine or jet engine. In military terminology, a rocket is unguided, while a missile is guided. Note the two meanings of "rocket" (weapon and engine): an ICBM is a guided missile with a rocket engine.
An explosion, whether or not by a weapon, causes the debris to act as multiple high velocity projectiles. An explosive weapon or device may also be designed to produce many high velocity projectiles by the break-up of its casing; these are correctly termed "fragments".
In sports.
In projectile motion the most important force applied to the ‘projectile’ is the propelling force, in this case the propelling forces are the muscles that act upon the ball to make it move, and the stronger the force applied, the more propelling force, which means the projectile (the ball) will travel farther. See pitching, bowling.
As a weapon.
Delivery projectiles.
Many projectiles, e.g. shells, may carry an explosive charge or another chemical or biological substance. Aside from explosive payload, a projectile can be designed to cause special damage, e.g. fire (see also early thermal weapons), or poisoning (see also arrow poison).
Wired projectiles.
Some projectiles stay connected by a cable to the launch equipment after launching it:
Equations of motion.
An object projected at an angle to the horizontal has both the vertical and horizontal components of velocity. The vertical component of the velocity on the y-axis is given as formula_0 while the horizontal component of the velocity is formula_1. There are various calculations for projectiles at a specific angle formula_2:
1. Time to reach maximum height. It is symbolized as (formula_3), which is the time taken for the projectile to reach the maximum height from the plane of projection. Mathematically, it is given as formula_4 where formula_5 = acceleration due to gravity (app 9.81 m/s²), formula_6 = initial velocity (m/s) and formula_2 = angle made by the projectile with the horizontal axis.
2. Time of flight (formula_7): this is the total time taken for the projectile to fall back to the same plane from which it was projected. Mathematically it is given as formula_8.
3. Maximum Height (formula_9): this is the maximum height attained by the projectile OR the maximum displacement on the vertical axis (y-axis) covered by the projectile. It is given as formula_10.
4. Range (formula_11): The Range of a projectile is the horizontal distance covered (on the x-axis) by the projectile. Mathematically, formula_12. The Range is maximum when angle formula_2 = 45°, i.e. formula_13.
Notes.
<templatestyles src="Reflist/styles.css" />
References.
<templatestyles src="Reflist/styles.css" />
|
[
{
"math_id": 0,
"text": "V_y=U\\sin\\theta"
},
{
"math_id": 1,
"text": "V_x=U\\cos\\theta"
},
{
"math_id": 2,
"text": "\\theta"
},
{
"math_id": 3,
"text": "t"
},
{
"math_id": 4,
"text": "t=U \\sin\\theta/g"
},
{
"math_id": 5,
"text": "g"
},
{
"math_id": 6,
"text": "U"
},
{
"math_id": 7,
"text": "T"
},
{
"math_id": 8,
"text": "T=2U\\sin\\theta/g"
},
{
"math_id": 9,
"text": "H"
},
{
"math_id": 10,
"text": "H = U^2 \\sin^2\\theta/2g"
},
{
"math_id": 11,
"text": "R"
},
{
"math_id": 12,
"text": "R = U^2 \\sin 2\\theta/g"
},
{
"math_id": 13,
"text": "\\sin 2\\theta=1"
}
] |
https://en.wikipedia.org/wiki?curid=144553
|
14455337
|
D-arabinonolactonase
|
The enzyme -arabinonolactonase (EC 3.1.1.30) the reaction
-arabinono-1,4-lactone + H2O formula_0 -arabinonate
This enzyme belongs to the family of hydrolases, specifically those acting on carboxylic ester bonds. The systematic name is -arabinono-1,4-lactone lactonohydrolase.
References.
<templatestyles src="Reflist/styles.css" />
|
[
{
"math_id": 0,
"text": "\\rightleftharpoons"
}
] |
https://en.wikipedia.org/wiki?curid=14455337
|
14455352
|
Deoxylimonate A-ring-lactonase
|
The enzyme deoxylimonate A-ring-lactonase (EC 3.1.1.46) catalyzes the reaction
deoxylimonate + H2O formula_0 deoxylimononic acid -ring-lactone
The reaction opens the A-ring-lactone of the triterpenoid deoxylimonic acid, leaving the -ring-lactone intact.
This enzyme belongs to the family of hydrolases, specifically those acting on carboxylic ester bonds. The systematic name is deoxylimonate A-ring-lactonohydrolase.
References.
<templatestyles src="Reflist/styles.css" />
|
[
{
"math_id": 0,
"text": "\\rightleftharpoons"
}
] |
https://en.wikipedia.org/wiki?curid=14455352
|
14455393
|
DGTPase
|
Enzyme
The enzyme dGTPase (EC 3.1.5.1) catalyzes the reaction
dGTP + H2O formula_0 deoxyguanosine + triphosphate
This enzyme belongs to the family of hydrolases, specifically those acting on triphosphoric monoester bonds. The systematic name is dGTP triphosphohydrolase. Other names in common use include deoxy-GTPase, deoxyguanosine 5-triphosphate triphosphohydrolase, deoxyguanosine triphosphatase, and deoxyguanosine triphosphate triphosphohydrolase. 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 1HA3, 2C77, 2C78, and 2DQB.
References.
<templatestyles src="Reflist/styles.css" />
|
[
{
"math_id": 0,
"text": "\\rightleftharpoons"
}
] |
https://en.wikipedia.org/wiki?curid=14455393
|
14455419
|
Dihydrocoumarin hydrolase
|
The enzyme dihydrocoumarin hydrolase (EC 3.1.1.35) catalyzes the reaction
dihydrocoumarin + H2O formula_0 melilotate
This enzyme belongs to the family of hydrolases, specifically those acting on carboxylic ester bonds. The systematic name is dihydrocoumarin lactonohydrolase. This enzyme participates in fluorene degradation.
References.
<templatestyles src="Reflist/styles.css" />
|
[
{
"math_id": 0,
"text": "\\rightleftharpoons"
}
] |
https://en.wikipedia.org/wiki?curid=14455419
|
14455429
|
Diisopropyl-fluorophosphatase
|
The enzyme diisopropyl-fluorophosphatase (EC 3.1.8.2) catalyzes the reaction
diisopropyl fluorophosphate + H2O formula_0 diisopropyl phosphate + fluoride
This enzyme belongs to the family of hydrolases, specifically those acting on ester bonds phosphoric-triester hydrolases. The systematic name is diisopropyl-fluorophosphate fluorohydrolase. Other names in common use include DFPase, tabunase, somanase, organophosphorus acid anhydrolase, organophosphate acid anhydrase, OPA anhydrase, diisopropylphosphofluoridase, dialkylfluorophosphatase, diisopropyl phosphorofluoridate hydrolase, isopropylphosphorofluoridase, and diisopropylfluorophosphonate dehalogenase. It employs one cofactor, divalent cation. At least one compound, chelating agent is known to inhibit this enzyme.
Structural studies.
As of late 2007, 16 structures have been solved for this class of enzymes, with PDB accession codes 1E1A, 1PJX, 2GVU, 2GVV, 2GVW, 2GVX, 2IAO, 2IAP, 2IAQ, 2IAR, 2IAS, 2IAT, 2IAU, 2IAV, 2IAW, and 2IAX.
References.
<templatestyles src="Reflist/styles.css" />
|
[
{
"math_id": 0,
"text": "\\rightleftharpoons"
}
] |
https://en.wikipedia.org/wiki?curid=14455429
|
14455448
|
Disulfoglucosamine-6-sulfatase
|
The enzyme disulfoglucosamine-6-sulfatase (EC 3.1.6.1) catalyzes the reaction
2-"N",6-"O"-disulfo--glucosamine + H2O formula_0 2-"N"-sulfo--glucosamine + sulfate
This enzyme belongs to the family of hydrolases, specifically those acting on sulfuric ester bonds. The systematic name is 2-"N",6-"O"-disulfo--glucosamine 6-sulfohydrolase. Other names in common use include "N"-sulfoglucosamine-6-sulfatase, and 6,"N"-disulfoglucosamine 6-"O"-sulfohydrolase.
References.
<templatestyles src="Reflist/styles.css" />
|
[
{
"math_id": 0,
"text": "\\rightleftharpoons"
}
] |
https://en.wikipedia.org/wiki?curid=14455448
|
14455465
|
D-lactate-2-sulfatase
|
The enzyme -lactate-2-sulfatase (EC 3.1.6.17) catalyzes the reaction
("R")-2-"O"-sulfolactate + H2O formula_0 ("R")-lactate + sulfate
This enzyme belongs to the family of hydrolases, specifically those acting on sulfuric ester bonds. The systematic name is ("R")-2-"O"-sulfolactate 2-sulfohydrolase.
The other name ("S")-2-"O"-sulfolactate 2-sulfohydrolase specifies the stereochemistry incorrectly.
References.
<templatestyles src="Reflist/styles.css" />
|
[
{
"math_id": 0,
"text": "\\rightleftharpoons"
}
] |
https://en.wikipedia.org/wiki?curid=14455465
|
14455486
|
Dodecanoyl-(acyl-carrier-protein) hydrolase
|
The enzyme dodecanoyl-[acyl-carrier-protein] hydrolase (EC 3.1.2.21) catalyzes the reaction
a dodecanoyl-[acyl-carrier-protein] + H2O formula_0 an [acyl-carrier-protein] + dodecanoate
This enzyme belongs to the family of hydrolases, specifically those acting on thioester bonds. The systematic name is dodecanoyl-[acyl-carrier-protein] hydrolase. Other names in common use include lauryl-acyl-carrier-protein hydrolase, dodecanoyl-acyl-carrier-protein hydrolase, dodecyl-acyl-carrier protein hydrolase, and dodecanoyl-[acyl-carrier protein] hydrolase.
References.
<templatestyles src="Reflist/styles.css" />
|
[
{
"math_id": 0,
"text": "\\rightleftharpoons"
}
] |
https://en.wikipedia.org/wiki?curid=14455486
|
14455502
|
Dolichyl-phosphatase
|
The enzyme dolichyl-phosphatase (EC 3.1.3.51) catalyzes the reaction
dolichyl phosphate + H2O formula_0 dolichol + phosphate
This enzyme belongs to the family of hydrolases, to be specific, those acting on phosphoric monoester bonds. The systematic name is dolichyl-phosphate phosphohydrolase. Other names in common use include dolichol phosphate phosphatase, dolichol phosphatase, dolichol monophosphatase, dolichyl monophosphate phosphatase, dolichyl phosphate phosphatase, polyisoprenyl phosphate phosphatase, polyprenylphosphate phosphatase, and Dol-"P" phosphatase. This enzyme participates in "N"-linked-glycan biosynthesis.
References.
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[
{
"math_id": 0,
"text": "\\rightleftharpoons"
}
] |
https://en.wikipedia.org/wiki?curid=14455502
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14455514
|
Dolichylphosphate-glucose phosphodiesterase
|
The enzyme dolichylphosphate-glucose phosphodiesterase (EC 3.1.4.48) catalyzes the reaction
dolichyl β--glucosyl phosphate + H2O formula_0 dolichyl phosphate + -glucose
This enzyme belongs to the family of hydrolases, specifically those acting on phosphoric diester bonds. The systematic name is dolichyl-β--glucosyl-phosphate dolichylphosphohydrolase. Other names in common use include dolichol phosphoglucose phosphodiesterase, and Dol-"P"-Glc phosphodiesterase. This enzyme participates in "n"-glycan biosynthesis.
References.
<templatestyles src="Reflist/styles.css" />
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[
{
"math_id": 0,
"text": "\\rightleftharpoons"
}
] |
https://en.wikipedia.org/wiki?curid=14455514
|
14455531
|
Dolichylphosphate-mannose phosphodiesterase
|
The enzyme dolichylphosphate-mannose phosphodiesterase (EC 3.1.4.49) catalyzes the reaction
dolichyl β--mannosyl phosphate + H2O formula_0 dolichyl phosphate + -mannose
This enzyme belongs to the family of hydrolases, specifically those acting on phosphoric diester bonds. The systematic name is dolichyl-β--mannosyl-phosphate dolichylphosphohydrolase. This enzyme is also called mannosylphosphodolichol phosphodiesterase.
References.
<templatestyles src="Reflist/styles.css" />
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[
{
"math_id": 0,
"text": "\\rightleftharpoons"
}
] |
https://en.wikipedia.org/wiki?curid=14455531
|
14455552
|
Fatty-acyl-ethyl-ester synthase
|
The enzyme fatty-acyl-ethyl-ester synthase (EC 3.1.1.67) catalyzes the reaction
a long-chain-fatty-acyl ethyl ester + H2O formula_0 a long-chain-fatty acid + ethanol
This enzyme belongs to the family of hydrolases, specifically those acting on carboxylic ester bonds. The systematic name is long-chain-fatty-acyl-ethyl-ester acylhydrolase. This enzyme is also called FAEES.
References.
<templatestyles src="Reflist/styles.css" />
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[
{
"math_id": 0,
"text": "\\rightleftharpoons"
}
] |
https://en.wikipedia.org/wiki?curid=14455552
|
14455574
|
Feruloyl esterase
|
The enzyme feruloyl esterase (EC 3.1.1.73) catalyzes the reaction
feruloyl-polysaccharide + H2O formula_0 ferulate + polysaccharide
This enzyme belongs to the family of hydrolases, specifically those acting on carboxylic ester bonds. The systematic name is 4-hydroxy-3-methoxycinnamoyl-sugar hydrolase. Other names in common use include ferulic acid esterase (FAE), hydroxycinnamoyl esterase, hemicellulase accessory enzyme, cinnamoyl ester hydrolase (cinnAE).
Structural studies.
As of late 2007, 6 structures have been solved for this class of enzymes, with PDB accession codes 1USW, 1UWC, 1UZA, 2BJH, 2HL6, and 2IX9.
References.
<templatestyles src="Reflist/styles.css" />
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[
{
"math_id": 0,
"text": "\\rightleftharpoons"
}
] |
https://en.wikipedia.org/wiki?curid=14455574
|
14455593
|
Formyl-CoA hydrolase
|
The enzyme formyl-CoA hydrolase (EC 3.1.2.10) catalyzes the reaction
formyl-CoA + H2O formula_0 CoA + formate
This enzyme belongs to the family of hydrolases, specifically those acting on thioester bonds. The systematic name is formyl-CoA hydrolase. This enzyme is also called formyl coenzyme A hydrolase. 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=14455593
|
14455607
|
Fructose-2,6-bisphosphate 2-phosphatase
|
The enzyme fructose-2,6-bisphosphate 2-phosphatase ({EC 3.1.3.46) catalyzes the reaction
β--fructose 2,6-bisphosphate + H2O formula_0 -fructose 6-phosphate + phosphate
This enzyme belongs to the family of hydrolases, specifically those acting on phosphoric monoester bonds. The systematic name is β--fructose-2,6-bisphosphate 2-phosphohydrolase. Other names in common use include fructose-2,6-bisphosphatase, and -fructose-2,6-bisphosphate 2-phosphohydrolase. This enzyme participates in fructose and mannose metabolism.
Structural studies.
As of late 2007, 13 structures have been solved for this class of enzymes, with PDB accession codes 1BIF, 1C7Z, 1C80, 1C81, 1FBT, 1K6M, 1TIP, 2AXN, 2BIF, 2DWO, 2DWP, 2I1V, and 3BIF.
References.
<templatestyles src="Reflist/styles.css" />
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[
{
"math_id": 0,
"text": "\\rightleftharpoons"
}
] |
https://en.wikipedia.org/wiki?curid=14455607
|
14455630
|
Fructose-2,6-bisphosphate 6-phosphatase
|
The enzyme fructose-2,6-bisphosphate 6-phosphatase (EC 3.1.3.54) catalyzes the reaction
β--fructose 2,6-bisphosphate + H2O formula_0 β--fructofuranose 2-phosphate + phosphate
This enzyme belongs to the family of hydrolases, specifically those acting on phosphoric monoester bonds. The systematic name of this enzyme class is β--fructose-2,6-bisphosphate 6-phosphohydrolase. Other names in common use include fructose 2,6-bisphosphate-6-phosphohydrolase, fructose-2,6-bisphosphate 6-phosphohydrolase, and -fructose-2,6-bisphosphate 6-phosphohydrolase. This enzyme participates in fructose and mannose metabolism.
References.
<templatestyles src="Reflist/styles.css" />
|
[
{
"math_id": 0,
"text": "\\rightleftharpoons"
}
] |
https://en.wikipedia.org/wiki?curid=14455630
|
14455654
|
Fusarinine-C ornithinesterase
|
The enzyme fusarinine-C ornithinesterase (EC 3.1.1.48) catalyzes the reaction
"N" 5-acyl--ornithine ester + H2O formula_0 "N" 5-acyl--ornithine + an alcohol
This enzyme belongs to the family of hydrolases, specifically those acting on carboxylic ester bonds. The systematic name of this enzyme class is "N" 5--ornithine-ester hydrolase. Other names in common use include ornithine esterase, and 5-"N" 5--ornithine-ester hydrolase.
References.
<templatestyles src="Reflist/styles.css" />
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[
{
"math_id": 0,
"text": "\\rightleftharpoons"
}
] |
https://en.wikipedia.org/wiki?curid=14455654
|
14455665
|
Galactolipase
|
The enzyme galactolipase (EC 3.1.1.26) catalyzes the reaction
1,2-diacyl-3-β--galactosyl-"sn"-glycerol + 2 H2O formula_0 3-β--galactosyl-"sn"-glycerol + 2 carboxylates
This enzyme belongs to the family of hydrolases, specifically those acting on carboxylic ester bonds. The systematic name of this enzyme class is 1,2-diacyl-3-β--galactosyl-"sn"-glycerol acylhydrolase. Other names in common use include galactolipid lipase, polygalactolipase, and galactolipid acylhydrolase. This enzyme participates in glycerolipid metabolism.
References.
<templatestyles src="Reflist/styles.css" />
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[
{
"math_id": 0,
"text": "\\rightleftharpoons"
}
] |
https://en.wikipedia.org/wiki?curid=14455665
|
14455689
|
Gluconolactonase
|
The enzyme gluconolactonase (EC 3.1.1.17) catalyzes the reaction
-glucono-1,5-lactone + H2O formula_0 -gluconate
This enzyme belongs to the family of hydrolases, specifically those acting on carboxylic ester bonds. The systematic name is -glucono-1,5-lactone lactonohydrolase. Other names in common use include lactonase, aldonolactonase, glucono-δ-lactonase, and gulonolactonase. This enzyme participates in three metabolic pathways: pentose phosphate pathway, ascorbate and aldarate metabolism, and caprolactam degradation.
References.
<templatestyles src="Reflist/styles.css" />
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[
{
"math_id": 0,
"text": "\\rightleftharpoons"
}
] |
https://en.wikipedia.org/wiki?curid=14455689
|
14455712
|
Glucose-1-phosphatase
|
The enzyme glucose-1-phosphatase (EC 3.1.3.10) catalyzes the reaction
α--glucose 1-phosphate + H2O formula_0 -glucose + phosphate
This enzyme belongs to the family of hydrolases, specifically those acting on phosphoric monoester bonds. The systematic name is α--glucose-1-phosphate phosphohydrolase. This enzyme participates in glycolysis and gluconeogenesis.
Structural studies.
As of late 2007, only one structure has been solved for this class of enzymes, with the PDB accession code 1NT4.
References.
<templatestyles src="Reflist/styles.css" />
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[
{
"math_id": 0,
"text": "\\rightleftharpoons"
}
] |
https://en.wikipedia.org/wiki?curid=14455712
|
14455727
|
Glucose-1-phospho-D-mannosylglycoprotein phosphodiesterase
|
The enzyme glucose-1-phospho--mannosylglycoprotein phosphodiesterase (EC 3.1.4.51) catalyzes the reaction
6-(-glucose-1-phospho)--mannosylglycoprotein + H2O formula_0 α--glucose 1-phosphate + -mannosylglycoprotein
This enzyme belongs to the family of hydrolases, specifically those acting on phosphoric diester bonds. The systematic name of this enzyme class is 6-(-glucose-1-phospho)--mannosylglycoprotein glucose-1-phosphohydrolase. This enzyme is also called α-glucose-1-phosphate phosphodiesterase.
References.
<templatestyles src="Reflist/styles.css" />
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[
{
"math_id": 0,
"text": "\\rightleftharpoons"
}
] |
https://en.wikipedia.org/wiki?curid=14455727
|
14455759
|
Glutathione thiolesterase
|
The enzyme glutathione thiolesterase (EC 3.1.2.7) catalyzes the reaction
"S"-acylglutathione + H2O formula_0 glutathione + a carboxylate
This enzyme belongs to the family of hydrolases, specifically those acting on thioester bonds. The systematic name is "S"-acylglutathione hydrolase. It is also called citryl-glutathione thioesterhydrolase.
References.
<templatestyles src="Reflist/styles.css" />
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[
{
"math_id": 0,
"text": "\\rightleftharpoons"
}
] |
https://en.wikipedia.org/wiki?curid=14455759
|
14455780
|
Glycerol-1,2-cyclic-phosphate 2-phosphodiesterase
|
The enzyme glycerol-1,2-cyclic-phosphate 2-phosphodiesterase (EC 3.1.4.42) catalyzes the reaction
glycerol 1,2-cyclic phosphate + H2O formula_0 glycerol 1-phosphate
This enzyme belongs to the family of hydrolases, specifically, those acting on phosphoric diester bonds. The systematic name is rac-glycerol-1,2-cyclic-phosphate 2-glycerophosphohydrolase. This enzyme is also called rac-glycerol 1:2-cyclic phosphate 2-phosphodiesterase.
References.
<templatestyles src="Reflist/styles.css" />
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[
{
"math_id": 0,
"text": "\\rightleftharpoons"
}
] |
https://en.wikipedia.org/wiki?curid=14455780
|
14455797
|
Glycerol-1-phosphatase
|
The enzyme glycerol-1-phosphatase (EC 3.1.3.21) catalyzes the reaction
glycerol 1-phosphate + H2O formula_0 glycerol + phosphate
This enzyme belongs to the family of hydrolases, specifically those acting on phosphoric monoester bonds. The systematic name is glycerol-1-phosphate phosphohydrolase. Other names in common use include α-glycerophosphatase, α-glycerol phosphatase, glycerol 3-phosphatase, glycerol-3-phosphate phosphatase, and glycerol 3-phosphate phosphohydrolase. This enzyme participates in glycerolipid metabolism.
Among the organisms that have been shown to express this enzymatic activity are "A. thaliana" (plant) via the "AtSgpp" and "AtGpp" gene products; "D. salina" (alga); "S. cerevisiae" (fungus) via the "GPP1/RHR2/YIL053W" and "GPP2/HOR2/YER062C" gene products; "C. albicans" (fungus) via the "GPP1" gene product; "M. tuberculosis" (bacteria) via the "rv1692" gene product; and C57BL/6N mice and Wistar rats (mammals) via the "PGP" gene product.
References.
<templatestyles src="Reflist/styles.css" />
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[
{
"math_id": 0,
"text": "\\rightleftharpoons"
}
] |
https://en.wikipedia.org/wiki?curid=14455797
|
14455811
|
Glycerol-2-phosphatase
|
The enzyme glycerol-2-phosphatase (EC 3.1.3.19) catalyzes the reaction
glycerol 2-phosphate + H2O formula_0 glycerol + phosphate
This enzyme belongs to the family of hydrolases, specifically those acting on phosphoric monoester bonds. The systematic name is glycerol-2-phosphate phosphohydrolase. Other names in common use include β-glycerophosphatase, β-glycerophosphate phosphatase, and 2-glycerophosphatase.
References.
<templatestyles src="Reflist/styles.css" />
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[
{
"math_id": 0,
"text": "\\rightleftharpoons"
}
] |
https://en.wikipedia.org/wiki?curid=14455811
|
14455841
|
Glycerophosphocholine phosphodiesterase
|
The enzyme glycerophosphocholine phosphodiesterase (EC 3.1.4.2) catalyzes the reaction
"sn"-glycero-3-phosphocholine + H2O formula_0 choline + "sn"-glycerol 3-phosphate
This enzyme belongs to the family of hydrolases, specifically those acting on phosphoric diester bonds. The systematic name is sn"-glycero-3-phosphocholine glycerophosphohydrolase. Other names in common use include glycerophosphinicocholine diesterase, glycerylphosphorylcholinediesterase, sn"-glycero-3-phosphorylcholine diesterase, glycerolphosphorylcholine phosphodiesterase, and glycerophosphohydrolase. This enzyme participates in glycerophospholipid metabolism.
References.
<templatestyles src="Reflist/styles.css" />
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[
{
"math_id": 0,
"text": "\\rightleftharpoons"
}
] |
https://en.wikipedia.org/wiki?curid=14455841
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14455858
|
Glycerophosphodiester phosphodiesterase
|
The enzyme glycerophosphodiester phosphodiesterase ({EC 3.1.4.46) catalyzes the reaction
a glycerophosphodiester + H2O formula_0 an alcohol + "sn"-glycerol 3-phosphate
This enzyme belongs to the family of hydrolases, specifically those acting on phosphoric diester bonds. The systematic name is glycerophosphodiester glycerophosphohydrolase. Other names in common use include gene hpd protein, glycerophosphoryl diester phosphodiesterase, and IgD-binding protein D. This enzyme participates in glycerophospholipid metabolism.
References.
<templatestyles src="Reflist/styles.css" />
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[
{
"math_id": 0,
"text": "\\rightleftharpoons"
}
] |
https://en.wikipedia.org/wiki?curid=14455858
|
14455870
|
Glycerophosphoinositol glycerophosphodiesterase
|
The enzyme glycerophosphoinositol glycerophosphodiesterase (EC 3.1.4.44) catalyzes the reaction
1-("sn"-glycero-3-phospho)-1-"myo"inositol + H2O formula_0 "myo"-inositol + "sn"-glycerol 3-phosphate
This enzyme belongs to the family of hydrolases, specifically those acting on phosphoric diester bonds. The systematic name is 1-("sn"-glycero-3-phospho)-1-"myo"-inositol glycerophosphohydrolase. Other names in common use include sn"-glycero(3)phosphoinositol glycerophosphohydrolase, and sn"-glycero-3-phospho-1-inositol glycerophosphohydrolase.
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=14455870
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14456188
|
Glycerophosphoinositol inositolphosphodiesterase
|
The enzyme glycerophosphoinositol inositolphosphodiesterase (EC 3.1.4.43) is an enzyme that catalyzes the chemical reaction
1-("sn"-glycero-3-phospho)-1-"myo"-inositol + H2O formula_0 glycerol + 1-"myo"-inositol 1-phosphate
This enzyme belongs to the family of hydrolases, specifically those acting on phosphoric diester bonds. The systematic name is 1-("sn"-glycero-3-phospho)-1-"myo"-inositol inositolphosphohydrolase. Other names in common use include 1,2-cyclic-inositol-phosphate phosphodiesterase, -"myo"-inositol 1:2-cyclic phosphate 2-phosphohydrolase, -inositol 1,2-cyclic phosphate 2-phosphohydrolase, -"myo"-inositol 1,2-cyclic phosphate 2-phosphohydrolase, 1--"myo"-inositol-1,2-cyclic-phosphate 2-inositolphosphohydrolase, and inositol-1,2-cyclic-phosphate 2-inositolphosphohydrolase.
This enzyme 1--"myo"-inositol-1,2-cyclic-phosphate 2-inositolphosphohydrolase, was reported to be identical to annexin III. Sekar and co-workers clearly demonstrated the dissociation of 1--"myo"-inositol-1,2-cyclic-phosphate 2-inositolphosphohydrolase activity from annexin III. Perron and co-workers confirmed on the basis of structural studies that annexin III did not possess an enzymatic activity. While the physiological significance of this enzymatic activity is still not clear, Sekar et al. [Biochem. Mol. Med. 61:95-100, 1007] reported over 10-fold increased release of this enzymatic activity in several patients admitted to the hospital's intensive care unit.
References.
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[
{
"math_id": 0,
"text": "\\rightleftharpoons"
}
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https://en.wikipedia.org/wiki?curid=14456188
|
14456206
|
(glycogen-synthase-D) phosphatase
|
Class of enzymes
The enzyme [glycogen-synthase-D] phosphatase ({EC 3.1.3.42) catalyzes the reaction
[glycogen-synthase D] + H2O formula_0 [glycogen-synthase I] + phosphate
This enzyme belongs to the family of hydrolases, specifically those acting on phosphoric monoester bonds. The systematic name is [UDP-glucose:glycogen 4-α-D-glucosyltransferase-D] phosphohydrolase. Other names in common use include uridine diphosphoglucose-glycogen glucosyltransferase phosphatase, UDP-glycogen glucosyltransferase phosphatase, UDPglucose-glycogen glucosyltransferase phosphatase, glycogen glucosyltransferase phosphatase, glycogen synthetase phosphatase, glycogen synthase phosphatase, glycogen synthase D phosphatase, Mg2+ dependent glycogen synthase phosphatase, and phosphatase type 2 °C.
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=14456206
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14456226
|
Glycosulfatase
|
The enzyme glycosulfatase (EC 3.1.6.3) catalyzes the reaction
-glucose 6-sulfate + H2O formula_0 -glucose + sulfate
This enzyme belongs to the family of hydrolases, specifically those acting on sulfuric ester bonds. The systematic name of this enzyme class is sugar-sulfate sulfohydrolase. This enzyme is also called glucosulfatase. This enzyme participates in glycolysis and gluconeogenesis.
References.
<templatestyles src="Reflist/styles.css" />
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[
{
"math_id": 0,
"text": "\\rightleftharpoons"
}
] |
https://en.wikipedia.org/wiki?curid=14456226
|
14456238
|
Guanidinodeoxy-scyllo-inositol-4-phosphatase
|
The enzyme guanidinodeoxy-"scyllo"-inositol-4-phosphatase (EC 3.1.3.40) catalyzes the reaction
1-guanidino-1-deoxy-"scyllo"-inositol 4-phosphate + H2O formula_0 1-guanidino-1-deoxy-"scyllo"-inositol + phosphate
This enzyme belongs to the family of hydrolases, specifically those acting on phosphoric monoester bonds. The systematic name is 1-guanidino-1-deoxy-"scyllo"-inositol-4-phosphate 4-phosphohydrolase. Other names in common use include 1-guanidino-"scyllo"-inositol 4-phosphatase, and 1-guanidino-1-deoxy-"scyllo"-inositol-4-"P" phosphohydrolase.
References.
<templatestyles src="Reflist/styles.css" />
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[
{
"math_id": 0,
"text": "\\rightleftharpoons"
}
] |
https://en.wikipedia.org/wiki?curid=14456238
|
14456262
|
Guanosine-3',5'-bis(diphosphate) 3'-diphosphatase
|
The enzyme guanosine-3′,5′-bis(diphosphate) 3′-diphosphatase (EC 3.1.7.2) catalyzes the reaction
guanosine 3′,5′-bis(diphosphate) + H2O formula_0 GDP + diphosphate
This enzyme belongs to the family of hydrolases, specifically those acting on diphosphoric monoester bonds. The systematic name is guanosine-3′,5′-bis(diphosphate) 3′-diphosphohydrolase. Other names in common use include guanosine-3′,5′-bis(diphosphate) 3′-pyrophosphatase, PpGpp-3'-pyrophosphohydrolase, and PpGpp phosphohydrolase. 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 1VJ7.
References.
<templatestyles src="Reflist/styles.css" />
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[
{
"math_id": 0,
"text": "\\rightleftharpoons"
}
] |
https://en.wikipedia.org/wiki?curid=14456262
|
14456283
|
Histidinol-phosphatase
|
The enzyme histidinol-phosphatase (EC 3.1.3.15) catalyzes the reaction
-histidinol phosphate + H2O formula_0 -histidinol + phosphate
This enzyme participates in histidine metabolism.
Nomenclature.
This enzyme belongs to the family of hydrolases, to be specific, those acting on phosphoric monoester bonds. The systematic name is -histidinol-phosphate phosphohydrolase. Other names in common use include histidinol phosphate phosphatase, -histidinol phosphate phosphatase, histidinolphosphate phosphatase, HPpase, and histidinolphosphatase.
"E. coli".
In "E. coli" the enzyme encoded by the gene "hisB" is a fused imidazoleglycerol-phosphate dehydratase and histidinol-phosphatase.
References.
<templatestyles src="Reflist/styles.css" />
Further reading.
<templatestyles src="Refbegin/styles.css" />
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[
{
"math_id": 0,
"text": "\\rightleftharpoons"
}
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https://en.wikipedia.org/wiki?curid=14456283
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14456299
|
Hydroxybutyrate-dimer hydrolase
|
The enzyme hydroxybutyrate-dimer hydrolase (EC 3.1.1.22) catalyzes the reaction
("R")-3-(("R")-3-hydroxybutanoyloxy)butanoate + H2O formula_0 2 ("R")-3-hydroxybutanoate
This enzyme belongs to the family of hydrolases, specifically those acting on carboxylic ester bonds. The systematic name is ("R")-3-(("R")-3-hydroxybutanoyloxy)butanoate hydroxybutanoylhydrolase. The enzyme is also called -(–)-3-hydroxybutyrate-dimer hydrolase. It participates in butanoate 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=14456299
|
14456330
|
(hydroxymethylglutaryl-CoA reductase (NADPH))-phosphatase
|
Class of enzymes
The enzyme [hydroxymethylglutaryl-CoA reductase (NADPH)]-phosphatase (EC 3.1.3.47) catalyzes the reaction
[hydroxymethylglutaryl-CoA reductase (NADPH)] phosphate + H2O formula_0 [hydroxymethylglutaryl-CoA reductase (NADPH)] + phosphate
This enzyme belongs to the family of hydrolases, specifically those acting on phosphoric monoester bonds. The systematic name is [hydroxymethylglutaryl-CoA reductase (NADPH)]-phosphate phosphohydrolase. This enzyme is also called reductase phosphatase.
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=14456330
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14456342
|
Inositol-1,4-bisphosphate 1-phosphatase
|
The enzyme inositol-1,4-bisphosphate 1-phosphatase (EC 3.1.3.57) catalyzes the reaction
1-"myo"-inositol 1,4-bisphosphate + H2O formula_0 1-"myo"-inositol 4-phosphate + phosphate
This enzyme belongs to the family of hydrolases, specifically those acting on phosphoric monoester bonds. The systematic name is -"myo"-inositol-1,4-bisphosphate 1-phosphohydrolase. This enzyme is also called inositol-polyphosphate 1-phosphatase. This enzyme participates in inositol phosphate metabolism and phosphatidylinositol signaling system.
Structural studies.
As of late 2007, two structures have been solved for this class of enzymes, with PDB accession codes 1INP and 1JP4.
References.
<templatestyles src="Reflist/styles.css" />
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[
{
"math_id": 0,
"text": "\\rightleftharpoons"
}
] |
https://en.wikipedia.org/wiki?curid=14456342
|
14456354
|
Inositol-phosphate phosphatase
|
Class of enzymes
The enzyme Inositol phosphate-phosphatase (EC 3.1.3.25) is of the phosphodiesterase family of enzymes. It is involved in the phosphophatidylinositol signaling pathway, which affects a wide array of cell functions, including but not limited to, cell growth, apoptosis, secretion, and information processing. Inhibition of inositol monophosphatase may be key in the action of lithium in treating bipolar disorder, specifically manic depression.
The catalyzed reaction:
"myo"-inositol phosphate + H2O formula_0 "myo"-inositol + phosphate
Nomenclature.
This enzyme belongs to the family of hydrolases, specifically those acting on phosphoric monoester bonds. The systematic name is "myo"-inositol-phosphate phosphohydrolase. Other names in common use include:
Structure.
The enzyme is a dimer comprising 277 amino acid residues per subunit. Each dimer exists in 5 layers of alternating α-helices and β-sheets, totaling to 9 α-helices and β-sheets per subunit. IMPase has three hydrophilic hollow active sites, each of which bind water and magnesium molecules. These binding sites appear to be conserved in other phosphodiesterases such as fructose 1,6-bisphosphatase (FBPase) and inositol polyphosphate 1-phosphatase.
Catalytic mechanism.
It was previously reported that the hydrolysis of inositol monophosphate was catalyzed by IMPase through a 2-magnesium ion mechanism. However a recent 1.4 A resolution crystal structure shows 3 magnesium ions coordinating in each active binding site of the 2 dimers, supporting a 3-magnesium ion mechanism. The mechanism for hydrolysis is now thought to proceed as such: the enzyme is activated by a magnesium ion binding to binding site I, containing three water molecules, and stabilized by the negative charges on the carboxylates of Glu70 and Asp90, and the carbonyl of Ile92. Another magnesium ion then cooperatively binds to binding site 2, which has of carboxylates of Asp90, Asp93, Asp220, and three water molecules, one of which is shared by binding site 1. Then, a third magnesium weakly and non-cooperatively to the third binding site, which has 5 water molecules and residue Glu70. After all three magnesium ions have bound, the inositol monophosphatase can bind, the negatively charge phosphate group stabilized by the three positively charged magnesium ions. Finally an activated water molecule acts a nucleophile and hydrolyzes the substrate, giving inositol and inorganic phosphate.
Function.
Inositol monophosphatase plays an important role in maintaining intracellular levels of myo-inositol, a molecule that forms the structural basis of several secondary messengers in eukaryotic cells. IMPase dephosphorylates the isomers of inositol monophosphate to produce inositol, mostly in the form of the stereoisomer, myo-inositol. Inositol monophosphatase is able to regulate inositol homeostasis because it lies at the convergence of two pathways that generate inositol:
Inositol monophosphatase in the phosphatidylinositol signaling pathway.
In this pathway, G-coupled protein receptors and tyrosine kinase receptors are activated, resulting in the activation of phospholipase C, which hydrolyzes phosphatidylinositol biphosphate (PIP2), resulting in a membrane associated product, diacylglycerol, and a water-soluble product, inositol triphosphate. Diacylglycerol acts as a second messenger, activating several protein kinases and produces extended downstream signaling. Inositol triphosphate is also a second messenger which activates receptors on the endoplasmic reticulum to release calcium ion stores into the cytoplasm, creating a complex signaling system that can be involved in modulating fertilization, proliferation, contraction, cell metabolism, vesicle and fluid secretion, and information processing in neuronal cells. Overall, diacylglycerol and inositol triphosphate signaling has implications for neuronal plasticity, impacting hippocampal long term potentiation, stress-induced cognitive impairment, and neuronal growth cone spreading. Furthermore, not only is PIP2 a precursor to several signaling molecules, it can be phosphorylated at the 3’ position to become PIP3, which is involved in cell proliferation, apoptosis and cell movement.
In this pathway, IMPase is the common, final step in recycling IP3 to produce PIP2. IMPase does this by dephosphorylating inositol monophosphate to produce inorganic phosphate and myo-inositol, the precursor to PIP2. Because of IMPase's crucial role in this signaling pathway, it is a potential drug target for inhibition and modulation.
Inositol monophosphatase in the "de novo" synthesis of "myo"-inositol.
There are at least 2 known steps in the "de novo" synthesis of "myo"-inositol from glucose 6-phosphate. In the first step, glucose 6-phosphate is converted to -inositol 1 monophosphate by the enzyme glucose 6 phosphate cyclase. Inositol monophosphatase catalyzes the final step in which D-inositol 1 monophosphate is dephosphorylated to form "myo"-inositol.
Clinical significance.
Inositol monophosphatase has historically been believed to be a direct target of lithium, the primary treatment for bipolar disorder. It is thought that lithium acts according to the inositol depletion hypothesis: lithium produces its therapeutic effect by inhibiting IMPase and therefore decreasing levels of myo-inositol. Scientific support for this hypothesis exists but is limited; the complete role of lithium and inositol monophosphatase in treating bipolar disorder or reducing "myo"-inositol levels is not well understood.
In support of the inositol depletion hypothesis, researchers have shown that lithium binds uncompetitively to purified bovine inositol monophosphatase at the site of one of the magnesium ions. Rodents administered lithium showed a decrease in inositol levels, in line with the hypothesis. Valproate, another mood-stabilizing drug given to bipolar disorder patients, has also been shown to mimic the effects of lithium on myo-inositol.
However, some clinical studies have found that bipolar disorder patients that had been administered lithium showed lower "myo"-inositol levels, while others found no effect on "myo"-inositol levels. Furthermore, lithium also binds to inositol polyphosphate 1-phosphatase (IPP), an enzyme also present in the phosphoinositide pathway, and could lower inositol levels through this mechanism More research is required to fully explain the role that lithium and IMPase play in bipolar disorder patients.
Despite the fact that lithium is effective in treating bipolar disorder, it is an extremely toxic metal and the toxic dose is only marginally greater than the therapeutic dose.
A novel inhibitor of inositol monophosphatase that is less toxic could be a more desirable treatment for bipolar disorder. Such an inhibitor would need to cross the blood–brain barrier in order to reach the inositol monophosphatase in neurons.
References.
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Further reading.
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14456381
|
L-arabinonolactonase
|
The enzyme -arabinonolactonase (EC 3.1.1.15) catalyzes the reaction
-arabinono-1,4-lactone + H2O formula_0 L-arabinonate
This enzyme belongs to the family of hydrolases, specifically those acting on carboxylic ester bonds. The systematic name is -arabinono-1,4-lactone lactonohydrolase. This enzyme participates in ascorbate and aldarate metabolism.
References.
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{
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"text": "\\rightleftharpoons"
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14456399
|
Limonin-D-ring-lactonase
|
The enzyme limonin--ring-lactonase (EC 3.1.1.36) catalyzes the reaction
limonoate -ring-lactone + H2O formula_0 limonoate
This enzyme belongs to the family of hydrolases, specifically those acting on carboxylic ester bonds. The systematic name of this enzyme class is limonoate--ring-lactone lactonohydrolase. Other names in common use include limonin--ring-lactone hydrolase, and limonin lactone hydrolase.
References.
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{
"math_id": 0,
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14456420
|
Lipid-phosphate phosphatase
|
The enzyme lipid-phosphate phosphatase (EC 3.1.3.76) catalyzes the reaction
(9"S",10"S")-10-hydroxy-9-(phosphonooxy)octadecanoate + H2O formula_0 (9"S",10"S")-9,10-dihydroxyoctadecanoate + phosphate
This enzyme belongs to the family of hydrolases, specifically those acting on phosphoric monoester bonds. The systematic name is (9"S",10"S")-10-hydroxy-9-(phosphonooxy)octadecanoate phosphohydrolase. Other names in common use include hydroxy fatty acid phosphatase, dihydroxy fatty acid phosphatase, hydroxy lipid phosphatase, sEH (ambiguous), and soluble epoxide hydrolase (ambiguous).
References.
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{
"math_id": 0,
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14456430
|
L-rhamnono-1,4-lactonase
|
The enzyme -rhamnono-1,4-lactonase (EC 3.1.1.65) catalyzes the reaction
-rhamnono-1,4-lactone + H2O formula_0 rhamnonate
This enzyme belongs to the family of hydrolases, specifically those acting on carboxylic ester bonds. The systematic name is -rhamnono-1,4-lactone lactonohydrolase. Other names in common use include rhamno-γ-lactonase, -rhamnono-γ-lactonase, and -rhamnonate dehydratase. This enzyme participates in fructose and mannose metabolism.
References.
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[
{
"math_id": 0,
"text": "\\rightleftharpoons"
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14456448
|
Lysophospholipase
|
The enzyme lysophospholipase (EC 3.1.1.5) catalyzes the reaction
2-lysophosphatidylcholine + H2O formula_0 glycerophosphocholine + a carboxylate
This enzyme belongs to the family of hydrolases, specifically those acting on carboxylic ester bonds. This family consists of lysophospholipase / phospholipase B (EC 3.1.1.5) and cytosolic phospholipase A2 which also has a C2 domain InterPro: "IPR000008". Phospholipase B enzymes catalyse the release of fatty acids from lysophospholipids and are capable "in vitro" of hydrolyzing all phospholipids extractable from yeast cells. Cytosolic phospholipase A2 associates with natural membranes in response to physiological increases in Ca2+ and selectively hydrolyses arachidonyl phospholipids, the aligned region corresponds the carboxy-terminal Ca2+-independent catalytic domain of the protein as discussed in.
The systematic name of this enzyme class is 2-lysophosphatidylcholine acylhydrolase. Other names in common use include lecithinase B, lysolecithinase, phospholipase B, lysophosphatidase, lecitholipase, phosphatidase B, lysophosphatidylcholine hydrolase, lysophospholipase A1, lysophopholipase L2, lysophospholipase transacylase, neuropathy target esterase, NTE, NTE-LysoPLA, and NTE-lysophospholipase. This enzyme participates in glycerophospholipid metabolism.
Examples.
Human genes encoding proteins that contain this domain include:
References.
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Further reading.
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14456466
|
Mannitol-1-phosphatase
|
The enzyme mannitol-1-phosphatase (EC 3.1.3.22) catalyzes the reaction
-mannitol 1-phosphate + H2O formula_0 -mannitol + phosphate
This enzyme belongs to the family of hydrolases, specifically those acting on phosphoric monoester bonds. The systematic name is -mannitol-1-phosphate phosphohydrolase. This enzyme is also called mannitol-1-phosphate phosphatase. This enzyme participates in fructose and mannose metabolism.
References.
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14456895
|
Methylphosphothioglycerate phosphatase
|
The enzyme methylphosphothioglycerate phosphatase (EC 3.1.3.14) catalyzes the reaction
"S"-methyl-3-phospho-1-thio--glycerate + H2O formula_0 "S"-methyl-1-thio--glycerate + phosphate
This enzyme belongs to the family of hydrolases, specifically those acting on phosphoric monoester bonds. The systematic name is "S"-methyl-3-phospho-1-thio--glycerate phosphohydrolase. This enzyme is also called methylthiophosphoglycerate phosphatase.
References.
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144569
|
Nilpotent group
|
Concept in group theory of mathematics
In mathematics, specifically group theory, a nilpotent group "G" is a group that has an upper central series that terminates with "G". Equivalently, it has a central series of finite length or its lower central series terminates with {1}.
Intuitively, a nilpotent group is a group that is "almost abelian". This idea is motivated by the fact that nilpotent groups are solvable, and for finite nilpotent groups, two elements having relatively prime orders must commute. It is also true that finite nilpotent groups are supersolvable. The concept is credited to work in the 1930s by Russian mathematician Sergei Chernikov.
Nilpotent groups arise in Galois theory, as well as in the classification of groups. They also appear prominently in the classification of Lie groups.
Analogous terms are used for Lie algebras (using the Lie bracket) including nilpotent, lower central series, and upper central series.
Definition.
The definition uses the idea of a central series for a group. The following are equivalent definitions for a nilpotent group G:
For a nilpotent group, the smallest n such that G has a central series of length n is called the nilpotency class of G; and G is said to be nilpotent of class n. (By definition, the length is n if there are formula_0 different subgroups in the series, including the trivial subgroup and the whole group.)
Equivalently, the nilpotency class of G equals the length of the lower central series or upper central series.
If a group has nilpotency class at most n, then it is sometimes called a nil-n group.
It follows immediately from any of the above forms of the definition of nilpotency, that the trivial group is the unique group of nilpotency class 0, and groups of nilpotency class 1 are exactly the non-trivial abelian groups.
Examples.
The natural numbers "k" for which any group of order "k" is nilpotent have been characterized (sequence in the OEIS).
Explanation of term.
Nilpotent groups are called so because the "adjoint action" of any element is nilpotent, meaning that for a nilpotent group formula_1 of nilpotence degree formula_2 and an element formula_3, the function formula_4 defined by formula_5 (where formula_6 is the commutator of formula_3 and formula_7) is nilpotent in the sense that the formula_2th iteration of the function is trivial: formula_8 for all formula_7 in formula_1.
This is not a defining characteristic of nilpotent groups: groups for which formula_9 is nilpotent of degree formula_2 (in the sense above) are called formula_2-Engel groups, and need not be nilpotent in general. They are proven to be nilpotent if they have finite order, and are conjectured to be nilpotent as long as they are finitely generated.
An abelian group is precisely one for which the adjoint action is not just nilpotent but trivial (a 1-Engel group).
Properties.
Since each successive factor group "Z""i"+1/"Z""i" in the upper central series is abelian, and the series is finite, every nilpotent group is a solvable group with a relatively simple structure.
Every subgroup of a nilpotent group of class "n" is nilpotent of class at most "n"; in addition, if "f" is a homomorphism of a nilpotent group of class "n", then the image of "f" is nilpotent of class at most "n".
The following statements are equivalent for finite groups, revealing some useful properties of nilpotency:
Proof:
Statement (d) can be extended to infinite groups: if "G" is a nilpotent group, then every Sylow subgroup "G""p" of "G" is normal, and the direct product of these Sylow subgroups is the subgroup of all elements of finite order in "G" (see torsion subgroup).
Many properties of nilpotent groups are shared by hypercentral groups.
Notes.
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[
{
"math_id": 0,
"text": "n + 1"
},
{
"math_id": 1,
"text": "G"
},
{
"math_id": 2,
"text": "n"
},
{
"math_id": 3,
"text": "g"
},
{
"math_id": 4,
"text": "\\operatorname{ad}_g \\colon G \\to G"
},
{
"math_id": 5,
"text": "\\operatorname{ad}_g(x) := [g,x]"
},
{
"math_id": 6,
"text": "[g,x]=g^{-1} x^{-1} g x"
},
{
"math_id": 7,
"text": "x"
},
{
"math_id": 8,
"text": "\\left(\\operatorname{ad}_g\\right)^n(x)=e"
},
{
"math_id": 9,
"text": "\\operatorname{ad}_g"
}
] |
https://en.wikipedia.org/wiki?curid=144569
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14456908
|
Methylumbelliferyl-acetate deacetylase
|
The enzyme methylumbelliferyl-acetate deacetylase (EC 3.1.1.56, esterase D) catalyzes the reaction
4-methylumbelliferyl acetate + H2O formula_0 4-methylumbelliferone + acetate
This enzyme belongs to the family of hydrolases, specifically those acting on carboxylic ester bonds. The systematic name is 4-methylumbelliferyl-acetate acylhydrolase. This enzyme is also called esterase D.
References.
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{
"math_id": 0,
"text": "\\rightleftharpoons"
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14456918
|
Monomethyl-sulfatase
|
The enzyme monomethyl-sulfatase (EC 3.1.6.16) catalyzes the reaction
monomethyl sulfate + H2O formula_0 methanol + sulfate
This enzyme belongs to the family of hydrolases, specifically those acting on sulfuric ester bonds. The systematic name is monomethyl-sulfate sulfohydrolase.
References.
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[
{
"math_id": 0,
"text": "\\rightleftharpoons"
}
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https://en.wikipedia.org/wiki?curid=14456918
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14456933
|
Monoterpenyl-diphosphatase
|
The enzyme monoterpenyl-diphosphatase (EC 3.1.7.3) catalyzes the reaction
a monoterpenyl diphosphate + H2O formula_0 a monoterpenol + diphosphate
This enzyme belongs to the family of hydrolases, specifically those acting on diphosphoric monoester bonds. The systematic name is monoterpenyl-diphosphate diphosphohydrolase. Other names in common use include bornyl pyrophosphate hydrolase and monoterpenyl-pyrophosphatase.
References.
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[
{
"math_id": 0,
"text": "\\rightleftharpoons"
}
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https://en.wikipedia.org/wiki?curid=14456933
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