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14502395
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Creatinine deaminase
|
In enzymology, a creatinine deaminase (EC 3.5.4.21) is an enzyme that catalyzes the chemical reaction
creatinine + H2O formula_0 N-methylhydantoin + NH3
Thus, the two substrates of this enzyme are creatinine and H2O, whereas its two products are N-methylhydantoin and NH3.
This enzyme belongs to the family of hydrolases, those acting on carbon-nitrogen bonds other than peptide bonds, specifically in cyclic amidines. The systematic name of this enzyme class is creatinine iminohydrolase. Other names in common use include creatinine hydrolase, and creatinine desiminase. This enzyme participates in arginine and proline metabolism.
References.
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[
{
"math_id": 0,
"text": "\\rightleftharpoons"
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https://en.wikipedia.org/wiki?curid=14502395
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14502412
|
Cyanoalanine nitrilase
|
In enzymology, a cyanoalanine nitrilase (EC 3.5.5.4) is an enzyme that catalyzes the chemical reaction
3-cyano-L-alanine + 2 H2O formula_0 L-aspartate + NH3
Thus, the two substrates of this enzyme are 3-cyano-L-alanine and H2O, whereas its two products are L-aspartate and NH3.
This enzyme belongs to the family of hydrolases, those acting on carbon-nitrogen bonds other than peptide bonds, specifically in nitriles. The systematic name of this enzyme class is 3-cyano-L-alanine aminohydrolase. This enzyme is also called beta-cyanoalanine nitrilase. This enzyme participates in cyanoamino acid metabolism.
References.
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[
{
"math_id": 0,
"text": "\\rightleftharpoons"
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https://en.wikipedia.org/wiki?curid=14502412
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14502427
|
Cyanuric acid amidohydrolase
|
In enzymology, a cyanuric acid amidohydrolase (EC 3.5.2.15) is an enzyme that catalyzes the chemical reaction
cyanuric acid + H2O formula_0 biuret + CO2
Thus, the two substrates of this enzyme are cyanuric acid and H2O, whereas its two products are biuret and CO2.
This enzyme belongs to the family of hydrolases, those acting on carbon-nitrogen bonds other than peptide bonds, specifically in cyclic amides. The systematic name of this enzyme class is cyanuric acid amidohydrolase. This enzyme participates in atrazine degradation.
References.
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[
{
"math_id": 0,
"text": "\\rightleftharpoons"
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https://en.wikipedia.org/wiki?curid=14502427
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14502442
|
Cytosine deaminase
|
In enzymology, a cytosine deaminase (EC 3.5.4.1) is an enzyme that catalyzes the chemical reaction
cytosine + H2O formula_0 uracil + NH3
Thus, the two substrates of this enzyme are cytosine and H2O, whereas its two products are uracil and NH3.
This enzyme belongs to the family of hydrolases, those acting on carbon-nitrogen bonds other than peptide bonds, specifically in cyclic amidines. The systematic name of this enzyme class is cytosine aminohydrolase. This enzyme is also called isocytosine deaminase. This enzyme participates in pyrimidine metabolism.
Structural studies.
As of late 2007, 13 structures have been solved for this class of enzymes, with PDB accession codes 1K6W, 1K70, 1OX7, 1P6O, 1R9X, 1R9Y, 1RA0, 1RA5, 1RAK, 1RB7, 1UAQ, 1YSB, and 1YSD.
References.
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[
{
"math_id": 0,
"text": "\\rightleftharpoons"
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https://en.wikipedia.org/wiki?curid=14502442
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14502486
|
D-benzoylarginine-4-nitroanilide amidase
|
In enzymology, a D-benzoylarginine-4-nitroanilide amidase (EC 3.5.1.72) is an enzyme that catalyzes the chemical reaction
N-benzoyl-D-arginine-4-nitroanilide + H2O formula_0 N-benzoyl-D-arginine + 4-nitroaniline
Thus, the two substrates of this enzyme are N-benzoyl-D-arginine-4-nitroanilide and H2O, whereas its two products are N-benzoyl-D-arginine and 4-nitroaniline.
This enzyme belongs to the family of hydrolases, those acting on carbon-nitrogen bonds other than peptide bonds, specifically in linear amides. The systematic name of this enzyme class is N-benzoyl-D-arginine-4-nitroanilide amidohydrolase. Other names in common use include benzoyl-D-arginine arylamidase, and D-BAPA-ase.
References.
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{
"math_id": 0,
"text": "\\rightleftharpoons"
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https://en.wikipedia.org/wiki?curid=14502486
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14502495
|
DCTP deaminase
|
In enzymology, a dCTP deaminase (EC 3.5.4.13) is an enzyme that catalyzes the chemical reaction
dCTP + H2O formula_0 dUTP + NH3
Thus, the two substrates of this enzyme are dCTP and H2O, whereas its two products are dUTP and NH3.
This enzyme belongs to the family of hydrolases, those acting on carbon-nitrogen bonds other than peptide bonds, specifically in cyclic amidines. The systematic name of this enzyme class is dCTP aminohydrolase. Other names in common use include deoxycytidine triphosphate deaminase, and 5-methyl-dCTP deaminase. This enzyme participates in pyrimidine metabolism.
Structural studies.
As of late 2007, 9 structures have been solved for this class of enzymes, with PDB accession codes 1OGH, 1PKH, 1PKJ, 1PKK, 1XS1, 1XS4, 1XS6, 2J4H, and 2J4Q.
References.
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[
{
"math_id": 0,
"text": "\\rightleftharpoons"
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https://en.wikipedia.org/wiki?curid=14502495
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14502505
|
DCTP deaminase (dUMP-forming)
|
In enzymology, a dCTP deaminase (dUMP-forming) (EC 3.5.4.30) is an enzyme that catalyzes the chemical reaction
dCTP + 2 H2O formula_0 dUMP + diphosphate + NH3
Thus, the two substrates of this enzyme are dCTP and H2O, whereas its 3 products are dUMP, diphosphate, and NH3.
This enzyme belongs to the family of hydrolases, those acting on carbon-nitrogen bonds other than peptide bonds, specifically in cyclic amidines. The systematic name of this enzyme class is dCTP aminohydrolase (dUMP-forming). This enzyme participates in pyrimidine metabolism.
Structural studies.
As of late 2007, 3 structures have been solved for this class of enzymes, with PDB accession codes 2HXB, 2HXD, and 2HXE.
References.
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[
{
"math_id": 0,
"text": "\\rightleftharpoons"
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https://en.wikipedia.org/wiki?curid=14502505
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14502511
|
Deoxycytidine deaminase
|
In enzymology, a deoxycytidine deaminase (EC 3.5.4.5) is an enzyme that catalyzes the chemical reaction
deoxycytidine + H2O formula_0 deoxyuridine + NH3
Thus, the two substrates of this enzyme are deoxycytidine and H2O, whereas its two products are deoxyuridine and NH3.
This enzyme belongs to the family of hydrolases, those acting on carbon-nitrogen bonds other than peptide bonds, specifically in cyclic amidines. The systematic name of this enzyme class is cytidine/2'-deoxycytidine aminohydrolase. This enzyme participates in pyrimidine metabolism. As every deoxycytidine deaminase is also a cytidine deaminase, they share the same EC number. The recommended name assigned by the IUBMB is cytidine deaminase.
References.
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{
"math_id": 0,
"text": "\\rightleftharpoons"
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https://en.wikipedia.org/wiki?curid=14502511
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14502522
|
D-glutaminase
|
In enzymology, a D-glutaminase (EC 3.5.1.35) is an enzyme that catalyzes the chemical reaction
D-glutamine + H2O formula_0 D-glutamate + NH3
Thus, the two substrates of this enzyme are D-glutamine and H2O, whereas its two products are D-glutamate and NH3.
This enzyme belongs to the family of hydrolases, those acting on carbon-nitrogen bonds other than peptide bonds, specifically in linear amides. The systematic name of this enzyme class is D-glutamine amidohydrolase. This enzyme participates in d-glutamine and d-glutamate metabolism and nitrogen metabolism.
References.
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{
"math_id": 0,
"text": "\\rightleftharpoons"
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https://en.wikipedia.org/wiki?curid=14502522
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14502536
|
Diaminohydroxyphosphoribosylaminopyrimidine deaminase
|
In enzymology, a diaminohydroxyphosphoribosylaminopyrimidine deaminase (EC 3.5.4.26) is an enzyme that catalyzes the chemical reaction
2,5-diamino-6-hydroxy-4-(5-phosphoribosylamino)pyrimidine + H2O formula_0 5-amino-6-(5-phosphoribosylamino)uracil + NH3
Thus, the two substrates of this enzyme are 2,5-diamino-6-hydroxy-4-(5-phosphoribosylamino)pyrimidine and H2O, whereas its two products are 5-amino-6-(5-phosphoribosylamino)uracil and NH3.
This enzyme belongs to the family of hydrolases, those acting on carbon-nitrogen bonds other than peptide bonds (specifically in cyclic amidines). The systematic name of this enzyme class is 2,5-diamino-6-hydroxy-4-(5-phosphoribosylamino)pyrimidine 2-aminohydrolase. This enzyme participates in riboflavin metabolism.
Structural studies.
As of late 2007, 6 structures have been solved for this class of enzymes, with PDB accession codes 2B3Z, 2D5N, 2G6V, 2HXV, 2O7P, and 2OBC.
References.
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{
"math_id": 0,
"text": "\\rightleftharpoons"
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https://en.wikipedia.org/wiki?curid=14502536
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14502547
|
Diguanidinobutanase
|
In enzymology, a diguanidinobutanase (EC 3.5.3.20) is an enzyme that catalyzes the chemical reaction
1,4-diguanidinobutane + H2O formula_0 agmatine + urea
Thus, the two substrates of this enzyme are 1,4-diguanidinobutane and H2O, whereas its two products are agmatine and urea.
This enzyme belongs to the family of hydrolases, those acting on carbon-nitrogen bonds other than peptide bonds, specifically in linear amidines. The systematic name of this enzyme class is 1,4-diguanidinobutane amidinohydrolase.
References.
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{
"math_id": 0,
"text": "\\rightleftharpoons"
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https://en.wikipedia.org/wiki?curid=14502547
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14502562
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Dihydropyrimidinase
|
In enzymology, a dihydropyrimidinase (EC 3.5.2.2) is an enzyme that catalyzes the chemical reaction
5,6-dihydrouracil + H2O formula_0 3-ureidopropanoate
Thus, the two substrates of this enzyme are 5,6-dihydrouracil and H2O, whereas its product is 3-ureidopropanoate.
This enzyme belongs to the family of hydrolases, those acting on carbon-nitrogen bonds other than peptide bonds, specifically in cyclic amides. The systematic name of this enzyme class is 5,6-dihydropyrimidine amidohydrolase. Other names in common use include hydantoinase, hydropyrimidine hydrase, hydantoin peptidase, pyrimidine hydrase, and D-hydantoinase. This enzyme participates in 3 metabolic pathways: pyrimidine metabolism, beta-alanine metabolism, and pantothenate and coa biosynthesis.
Structural studies.
As of late 2007, 10 structures have been solved for this class of enzymes, with PDB accession codes 1GKP, 1GKQ, 1GKR, 1NFG, 1YNY, 2FTW, 2FTY, 2FVK, 2FVM, and 2GSE.
References.
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{
"math_id": 0,
"text": "\\rightleftharpoons"
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https://en.wikipedia.org/wiki?curid=14502562
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14502577
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Dimethylargininase
|
Class of enzymes
In the field of enzymology, a dimethylargininase, also known as a dimethylarginine dimethylaminohydrolase (DDAH), is an enzyme that catalyzes the chemical reaction:
N-omega,N-omega'-methyl-L-arginine + H2O formula_0 dimethylamine + L-citrulline
Thus, the two substrates of this enzyme are N-omega,N-omega'-methyl-L-arginine and H2O, whereas its two products are dimethylamine and L-citrulline.
Isozymes.
Dimethylarginine dimethylaminohydrolase is an enzyme found in all mammalian cells. Two isoforms exist, DDAH I and DDAH II, with some differences in tissue distribution of the two isoforms). The enzyme degrades methylarginines, specifically asymmetric dimethylarginine (ADMA) and NG-monomethyl-L-arginine (MMA).
Function.
The methylarginines ADMA and MMA inhibit the enzyme nitric oxide synthase. As such, DDAH is important in removing methylarginines, generated by protein degradation, from accumulating and inhibiting the generation of nitric oxide.
Clinical significance.
Inhibition of DDAH activity causes methylarginines to accumulate, blocking nitric oxide(NO) synthesis and causing vasoconstriction. An impairment of DDAH activity appears to be involved in the elevation of plasma ADMA, and impairment of vascular relaxation observed in humans with cardiovascular disease or risk factors (such as hypercholesterolemia, diabetes mellitus, and insulin resistance). The activity of DDAH is impaired by oxidative stress, permitting ADMA to accumulate. A wide range of pathologic stimuli induce endothelial oxidative stress such as oxidized LDL-cholesterol, inflammatory cytokines, hyperhomocysteinemia, hyperglycemia and infectious agents. Each of these insults attenuates DDAH activity "in vitro" and "in vivo". The attenuation of DDAH allows ADMA to accumulate, and to block NO synthesis. The adverse effect of these stimuli can be reversed in vitro by antioxidants, which preserve the activity of DDAH.
The sensitivity of DDAH to oxidative stress is conferred by a critical sulfhydryl in the active site of the enzyme that is required for the metabolism of ADMA. This sulfhydryl can also be reversibly inhibited by NO in an elegant form of negative feedback. Homocysteine (a putative cardiovascular risk factor) mounts an oxidative attack on DDAH to form a mixed disulfide, inactivating the enzyme. By oxidizing a sulfhydryl moiety critical for DDAH activity, homocysteine and other risk factors cause ADMA to accumulate and to suppress nitric oxide synthase (NOS) activity.
The critical role of DDAH activity in regulating NO synthesis "in vivo" was demonstrated using a transgenic DDAH mouse. In this animal, the activity of DDAH is increased, and plasma ADMA levels are reduced by 50%. The reduction in plasma ADMA is associated with a significant increase in NOS activity, as plasma and urinary nitrate levels are doubled. The increase in NOS activity translates into a 15mmHg reduction in systolic blood pressure in the transgenic mouse. This study provides evidence for the importance of DDAH activity and plasma ADMA levels in the regulation of NO synthesis. Subsequent studies have shown that DDAH transgenic animals also manifest improvements in endothelial regeneration and angiogenesis, and reduced vascular obstructive disease, in association with the reduced plasma levels of ADMA. These findings are consistent with evidence from a number of groups that nitric oxide plays a critical role in vascular regeneration. By contrast, elevations in ADMA impair angiogenesis. These insights into the role of DDAH in degrading endogenous inhibitors of NOS, and thereby maintaining vascular NO production, may have important implications in vascular health and therapy for cardiovascular disease.
References.
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Further reading.
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https://en.wikipedia.org/wiki?curid=14502577
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14502597
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Enamidase
|
In enzymology, an enamidase (EC 3.5.2.18) is an enzyme that catalyzes the chemical reaction
6-oxo-1,4,5,6-tetrahydronicotinate + 2 H2O formula_0 2-formylglutarate + NH3
Thus, the two substrates of this enzyme are 6-oxo-1,4,5,6-tetrahydronicotinate and H2O, whereas its two products are 2-formylglutarate and NH3.
This enzyme belongs to the family of hydrolases, those acting on carbon-nitrogen bonds other than peptide bonds, specifically in cyclic amides. The systematic name of this enzyme class is 6-oxo-1,4,5,6-tetrahydronicotinate amidohydrolase.
References.
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{
"math_id": 0,
"text": "\\rightleftharpoons"
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https://en.wikipedia.org/wiki?curid=14502597
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14502605
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Formamidase
|
In enzymology, a formamidase (EC 3.5.1.49) is an enzyme that catalyzes the chemical reaction
formamide + H2O formula_0 formate + NH3
Thus, the two substrates of this enzyme are formamide and H2O, whereas its two products are formate and NH3.
This enzyme belongs to the family of hydrolases, those acting on carbon-nitrogen bonds other than peptide bonds, specifically in linear amides. The systematic name of this enzyme class is formamide amidohydrolase. This enzyme participates in glyoxylate and dicarboxylate metabolism and nitrogen metabolism.
Structural studies.
As of late 2007, four structures have been solved for this class of enzymes, with PDB accession codes 2DYU, 2DYV, 2E2K, and 2E2L.
References.
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{
"math_id": 0,
"text": "\\rightleftharpoons"
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https://en.wikipedia.org/wiki?curid=14502605
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14502625
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Formimidoylaspartate deiminase
|
In enzymology, a formimidoylaspartate deiminase (EC 3.5.3.5) is an enzyme that catalyzes the chemical reaction
N-formimidoyl-L-aspartate + H2O formula_0 N-formyl-L-aspartate + NH3
Thus, the two substrates of this enzyme are N-formimidoyl-L-aspartate and H2O, whereas its two products are N-formyl-L-aspartate and NH3.
This enzyme belongs to the family of hydrolases, those acting on carbon-nitrogen bonds other than peptide bonds, specifically in linear amidines. The systematic name of this enzyme class is N-formimidoyl-L-aspartate iminohydrolase. This enzyme is also called formiminoaspartate deiminase. This enzyme participates in histidine metabolism.
References.
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{
"math_id": 0,
"text": "\\rightleftharpoons"
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https://en.wikipedia.org/wiki?curid=14502625
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14502702
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Formimidoylglutamase
|
In enzymology, a formimidoylglutamase (EC 3.5.3.8) is an enzyme that catalyzes the chemical reaction
N-formimidoyl-L-glutamate + H2O formula_0 L-glutamate + formamide
Thus, the two substrates of this enzyme are N-formimidoyl-L-glutamate and H2O, whereas its two products are L-glutamate and formamide.
This enzyme belongs to the family of hydrolases, those acting on carbon-nitrogen bonds other than peptide bonds, specifically in linear amidines. The systematic name of this enzyme class is N-formimidoyl-L-glutamate formimidoylhydrolase. Other names in common use include formiminoglutamase, N-formiminoglutamate hydrolase, and N-formimino-L-glutamate formiminohydrolase. This enzyme participates in histidine metabolism.
Structural studies.
As of late 2007, two structures have been solved for this class of enzymes, with PDB accession codes 1XFK and 2A0M.
References.
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https://en.wikipedia.org/wiki?curid=14502702
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14502716
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Formimidoylglutamate deiminase
|
In enzymology, a formimidoylglutamate deiminase (EC 3.5.3.13) is an enzyme that catalyzes the chemical reaction
N-formimidoyl-L-glutamate + H2O formula_0 N-formyl-L-glutamate + NH3
Thus, the two substrates of this enzyme are N-formimidoyl-L-glutamate and H2O, whereas its two products are N-formyl-L-glutamate and NH3.
This enzyme belongs to the family of hydrolases, those acting on carbon-nitrogen bonds other than peptide bonds, specifically in linear amidines. The systematic name of this enzyme class is N-formimidoyl-L-glutamate iminohydrolase. Other names in common use include formiminoglutamate deiminase, and formiminoglutamic iminohydrolase. This enzyme participates in histidine metabolism.
References.
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{
"math_id": 0,
"text": "\\rightleftharpoons"
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https://en.wikipedia.org/wiki?curid=14502716
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14502729
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Formylaspartate deformylase
|
Class of enzyme
In enzymology, a formylaspartate deformylase (EC 3.5.1.8) is an enzyme that catalyzes the chemical reaction
N-formyl-L-aspartate + H2O formula_0 formate + L-aspartate
Thus, the two substrates of this enzyme are N-formyl-L-aspartate and H2O, whereas its two products are formate and L-aspartate.
This enzyme belongs to the family of hydrolases, those acting on carbon-nitrogen bonds other than peptide bonds, specifically in linear amides. The systematic name of this enzyme class is N-formyl-L-aspartate amidohydrolase. This enzyme is also called formylaspartic formylase (formylase I, formylase II). This enzyme participates in histidine metabolism and glyoxylate and dicarboxylate metabolism.
References.
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"math_id": 0,
"text": "\\rightleftharpoons"
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https://en.wikipedia.org/wiki?curid=14502729
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14502746
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Formylmethionine deformylase
|
In enzymology, a formylmethionine deformylase (EC 3.5.1.31) is an enzyme that catalyzes the chemical reaction
N-formyl-L-methionine + H2O formula_0 formate + L-methionine
Thus, the two substrates of this enzyme are N-formyl-L-methionine and H2O, whereas its two products are formate and L-methionine.
This enzyme belongs to the family of hydrolases, those acting on carbon-nitrogen bonds other than peptide bonds, specifically in linear amides. The systematic name of this enzyme class is N-formyl-L-methionine amidohydrolase. This enzyme participates in methionine metabolism and glyoxylate and dicarboxylate metabolism.
Structural studies.
As of late 2007, 14 structures have been solved for this class of enzymes, with PDB accession codes 1BS4, 1BS5, 1BS6, 1BS7, 1BS8, 1BSZ, 1DEF, 1DFF, 1G27, 1G2A, 1ICJ, 1JYM, 1RL4, and 2DEF.
References.
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{
"math_id": 0,
"text": "\\rightleftharpoons"
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https://en.wikipedia.org/wiki?curid=14502746
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14502759
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Formyltetrahydrofolate deformylase
|
In enzymology, a formyltetrahydrofolate deformylase (EC 3.5.1.10) is an enzyme that catalyzes the chemical reaction
10-formyltetrahydrofolate + H2O formula_0 formate + tetrahydrofolate
Thus, the two substrates of this enzyme are 10-formyltetrahydrofolate and H2O, whereas its two products are formate and tetrahydrofolate.
This enzyme belongs to the family of hydrolases, those acting on carbon-nitrogen bonds other than peptide bonds, specifically in linear amides. The systematic name of this enzyme class is 10-formyltetrahydrofolate amidohydrolase. This enzyme participates in glyoxylate and dicarboxylate metabolism and one carbon pool by folate.
References.
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{
"math_id": 0,
"text": "\\rightleftharpoons"
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https://en.wikipedia.org/wiki?curid=14502759
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14502768
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Gamma-glutamyl-gamma-aminobutyrate hydrolase
|
In enzymology, a gamma-glutamyl-gamma-aminobutyrate hydrolase (EC 3.5.1.94) is an enzyme that catalyzes the chemical reaction
4-(gamma-glutamylamino)butanoate + H2O formula_0 4-aminobutanoate + L-glutamate
Thus, the two substrates of this enzyme are 4-(gamma-glutamylamino)butanoate and H2O, whereas its two products are 4-aminobutanoate and L-glutamate.
This enzyme belongs to the family of hydrolases, those acting on carbon-nitrogen bonds other than peptide bonds, specifically in linear amides. The systematic name of this enzyme class is 4-(gamma-glutamylamino)butanoate amidohydrolase. Other names in common use include gamma-glutamyl-GABA hydrolase, PuuD, and YcjL. This enzyme participates in urea cycle and metabolism of amino groups.
References.
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{
"math_id": 0,
"text": "\\rightleftharpoons"
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https://en.wikipedia.org/wiki?curid=14502768
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14502786
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Glucosamine-6-phosphate deaminase
|
In enzymology, a glucosamine-6-phosphate deaminase (EC 3.5.99.6) is an enzyme that catalyzes the chemical reaction
D-glucosamine 6-phosphate + H2O formula_0 D-fructose 6-phosphate + NH3
Thus, the two substrates of this enzyme are glucosamine 6-phosphate and H2O, whereas its two products are fructose 6-phosphate and NH3.
This enzyme belongs to the family of hydrolases, those acting on carbon-nitrogen bonds other than peptide bonds, specifically in compounds that have not been otherwise categorized within EC number 3.5. The systematic name of this enzyme class is 2-amino-2-deoxy-D-glucose-6-phosphate aminohydrolase (ketol isomerizing). Other names in common use include glucosaminephosphate isomerase, glucosamine-6-phosphate isomerase, phosphoglucosaminisomerase, glucosamine phosphate deaminase, aminodeoxyglucosephosphate isomerase, and phosphoglucosamine isomerase. This enzyme participates in aminosugars metabolism. This enzyme has at least one effector, N-Acetyl-D-glucosamine 6-phosphate.
Structural studies.
As of late 2007, 5 structures have been solved for this class of enzymes, with PDB accession codes 1J5X, 1JT9, 1NE7, 2BKV, and 2BKX.
References.
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{
"math_id": 0,
"text": "\\rightleftharpoons"
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https://en.wikipedia.org/wiki?curid=14502786
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14502805
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Glutamin-(asparagin-)ase
|
In enzymology, a glutamin-(asparagin-)ase (EC 3.5.1.38) is an enzyme that catalyzes the chemical reaction
L-glutamine + H2O formula_0 L-glutamate + NH3
Thus, the two substrates of this enzyme are L-glutamine and H2O, whereas its two products are L-glutamate and NH3.
This enzyme belongs to the family of hydrolases, those acting on carbon-nitrogen bonds other than peptide bonds, specifically in linear amides. The systematic name of this enzyme class is L-glutamine(L-asparagine) amidohydrolase. This enzyme participates in 4 metabolic pathways: glutamate metabolism, alanine and aspartate metabolism, d-glutamine and d-glutamate metabolism, and nitrogen metabolism.
Structural studies.
As of late 2007, 3 structures have been solved for this class of enzymes, with PDB accession codes 1DJO, 1DJP, and 4PGA.
References.
<templatestyles src="Reflist/styles.css" />
|
[
{
"math_id": 0,
"text": "\\rightleftharpoons"
}
] |
https://en.wikipedia.org/wiki?curid=14502805
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14502826
|
Glutaryl-7-aminocephalosporanic-acid acylase
|
In enzymology, a glutaryl-7-aminocephalosporanic-acid acylase (EC 3.5.1.93) is an enzyme that catalyzes the chemical reaction
(7R)-7-(4-carboxybutanamido)cephalosporanate + H2O formula_0 (7R)-7-aminocephalosporanate + glutarate
Thus, the two substrates of this enzyme are (7R)-7-(4-carboxybutanamido)cephalosporanate and H2O, whereas its two products are (7R)-7-aminocephalosporanate and glutarate.
This enzyme belongs to the family of hydrolases, those acting on carbon-nitrogen bonds other than peptide bonds, specifically in linear amides. The systematic name of this enzyme class is (7R)-7-(4-carboxybutanamido)cephalosporanate amidohydrolase. Other names in common use include 7beta-(4-carboxybutanamido)cephalosporanic acid acylase, cephalosporin C acylase, glutaryl-7-ACA acylase, CA, GCA, GA, cephalosporin acylase, glutaryl-7-aminocephalosporanic acid acylase, and GL-7-ACA acylase. This enzyme participates in penicillin and cephalosporin biosynthesis.
References.
<templatestyles src="Reflist/styles.css" />
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[
{
"math_id": 0,
"text": "\\rightleftharpoons"
}
] |
https://en.wikipedia.org/wiki?curid=14502826
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14502836
|
Glutathionylspermidine amidase
|
In enzymology, a glutathionylspermidine amidase (EC 3.5.1.78) is an enzyme that catalyzes the chemical reaction
glutathionylspermidine + H2O formula_0 glutathione + spermidine
Thus, the two substrates of this enzyme are glutathionylspermidine and H2O, whereas its two products are glutathione and spermidine.
This enzyme belongs to the family of hydrolases, those acting on carbon-nitrogen bonds other than peptide bonds, specifically in linear amides. The systematic name of this enzyme class is gamma-L-glutamyl-L-cysteinyl-glycine:spermidine amidase. This enzyme is also called glutathionylspermidine amidohydrolase (spermidine-forming). This enzyme participates in glutathione metabolism.
Structural studies.
As of late 2007, 5 structures have been solved for this class of enzymes, with PDB accession codes 2IO7, 2IO8, 2IO9, 2IOA, and 2IOB.
References.
<templatestyles src="Reflist/styles.css" />
|
[
{
"math_id": 0,
"text": "\\rightleftharpoons"
}
] |
https://en.wikipedia.org/wiki?curid=14502836
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14502852
|
GTP cyclohydrolase II
|
In enzymology, a GTP cyclohydrolase II (EC 3.5.4.25) is an enzyme that catalyzes the chemical reaction
GTP + 3 H2O formula_0 formate + 2,5-diamino-6-hydroxy-4-(5-phosphoribosylamino)pyrimidine + diphosphate
Thus, the two substrates of this enzyme are GTP and H2O, whereas its 3 products are formate, 2,5-diamino-6-hydroxy-4-(5-phosphoribosylamino)pyrimidine, and diphosphate.
This enzyme belongs to the family of hydrolases, those acting on carbon-nitrogen bonds other than peptide bonds, specifically in cyclic amidines. The systematic name of this enzyme class is GTP 7,8-8,9-dihydrolase (diphosphate-forming). Other names in common use include guanosine triphosphate cyclohydrolase II, and GTP-8-formylhydrolase. This enzyme participates in riboflavin metabolism.
Structural studies.
As of late 2007, two structures have been solved for this class of enzymes, with PDB accession codes 2BZ0 and 2BZ1.
References.
<templatestyles src="Reflist/styles.css" />
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[
{
"math_id": 0,
"text": "\\rightleftharpoons"
}
] |
https://en.wikipedia.org/wiki?curid=14502852
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14502867
|
GTP cyclohydrolase IIa
|
In enzymology, a GTP cyclohydrolase IIa (EC 3.5.4.29) is an enzyme that catalyzes the chemical reaction
GTP + 3 H2O formula_0 2-amino-5-formylamino-6-(5-phosphoribosylamino)pyrimidin-4(3H)-one + 2 phosphate
Thus, the two substrates of this enzyme are GTP and H2O, whereas its two products are 2-amino-5-formylamino-6-(5-phosphoribosylamino)pyrimidin-4(3H)-one and phosphate.
This enzyme belongs to the family of hydrolases, those acting on carbon-nitrogen bonds other than peptide bonds, specifically in cyclic amidines. The systematic name of this enzyme class is GTP 8,9-hydrolase (phosphate-forming).
References.
<templatestyles src="Reflist/styles.css" />
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[
{
"math_id": 0,
"text": "\\rightleftharpoons"
}
] |
https://en.wikipedia.org/wiki?curid=14502867
|
14502879
|
Guanidinoacetase
|
In enzymology, a guanidinoacetase (EC 3.5.3.2) is an enzyme that catalyzes the chemical reaction
guanidinoacetate + H2O formula_0 glycine + urea
Thus, the two substrates of this enzyme are guanidinoacetate and H2O, whereas its two products are glycine and urea.
This enzyme belongs to the family of hydrolases, those acting on carbon-nitrogen bonds other than peptide bonds, specifically in linear amidines. The systematic name of this enzyme class is guanidinoacetate amidinohydrolase. This enzyme is also called glycocyaminase. It employs one cofactor, manganese.
References.
<templatestyles src="Reflist/styles.css" />
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[
{
"math_id": 0,
"text": "\\rightleftharpoons"
}
] |
https://en.wikipedia.org/wiki?curid=14502879
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14502890
|
Guanidinobutyrase
|
In enzymology, a guanidinobutyrase (EC 3.5.3.7) is an enzyme that catalyzes the chemical reaction
4-guanidinobutanoate + H2O formula_0 4-aminobutanoate + urea
Thus, the two substrates of this enzyme are 4-guanidinobutanoate and H2O, whereas its two products are 4-aminobutanoate and urea.
This enzyme belongs to the family of hydrolases, those acting on carbon-nitrogen bonds other than peptide bonds, specifically in linear amidines. The systematic name of this enzyme class is 4-guanidinobutanoate amidinohydrolase. Other names in common use include gamma-guanidobutyrase, 4-guanidinobutyrate amidinobutyrase, gamma-guanidinobutyrate amidinohydrolase, G-Base, GBH, and guanidinobutyrate ureahydrolase. This enzyme participates in urea cycle and metabolism of amino groups. It employs one cofactor, manganese.
References.
<templatestyles src="Reflist/styles.css" />
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[
{
"math_id": 0,
"text": "\\rightleftharpoons"
}
] |
https://en.wikipedia.org/wiki?curid=14502890
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14502907
|
Guanidinopropionase
|
In enzymology, a guanidinopropionase (EC 3.5.3.17) is an enzyme that catalyzes the chemical reaction
3-guanidinopropanoate + H2O formula_0 beta-alanine + urea
Thus, the two substrates of this enzyme are 3-guanidinopropanoate and H2O, whereas its two products are beta-alanine and urea.
This enzyme belongs to the family of hydrolases, those acting on carbon-nitrogen bonds other than peptide bonds, specifically in linear amidines. The systematic name of this enzyme class is 3-guanidinopropanoate amidinopropionase. Other names in common use include GPase and GPH. It employs one cofactor, manganese.
References.
<templatestyles src="Reflist/styles.css" />
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[
{
"math_id": 0,
"text": "\\rightleftharpoons"
}
] |
https://en.wikipedia.org/wiki?curid=14502907
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14502921
|
Guanosine deaminase
|
In enzymology, a guanosine deaminase (EC 3.5.4.15) is an enzyme that catalyzes the chemical reaction
guanosine + H2O formula_0 xanthosine + NH3
Thus, the two substrates of this enzyme are guanosine and H2O, whereas its two products are xanthosine and NH3.
This enzyme belongs to the family of hydrolases, those acting on carbon-nitrogen bonds other than peptide bonds, specifically in cyclic amidines. The systematic name of this enzyme class is guanosine aminohydrolase. This enzyme is also called guanosine aminase.
References.
<templatestyles src="Reflist/styles.css" />
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[
{
"math_id": 0,
"text": "\\rightleftharpoons"
}
] |
https://en.wikipedia.org/wiki?curid=14502921
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14502972
|
Hippurate hydrolase
|
In enzymology, a hippurate hydrolase (EC 3.5.1.32) is an enzyme that catalyzes the chemical reaction
hippurate + H2O formula_0 benzoate + glycine
Thus, the two substrates of this enzyme are hippurate and H2O, whereas its two products are benzoate and glycine.
This enzyme belongs to the family of hydrolases, those acting on carbon-nitrogen bonds other than peptide bonds, specifically in linear amides. The systematic name of this enzyme class is N-benzoylamino-acid amidohydrolase. This enzyme participates in phenylalanine metabolism.
Hippurate hydrolysis test is used in the presumptive identification of Gardnerella vaginalis, Campylobacter jejuni, Listeria monocytogenes and group B streptococci by detecting the ability of the organism to hydrolyze hippurate.
References.
<templatestyles src="Reflist/styles.css" />
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[
{
"math_id": 0,
"text": "\\rightleftharpoons"
}
] |
https://en.wikipedia.org/wiki?curid=14502972
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14502986
|
Hydroxydechloroatrazine ethylaminohydrolase
|
In enzymology, a hydroxydechloroatrazine ethylaminohydrolase (EC 3.5.99.3) is an enzyme that catalyzes the chemical reaction
4-(ethylamino)-2-hydroxy-6-(isopropylamino)-1,3,5-triazine + H2O formula_0 N-isopropylammelide + ethylamine
Thus, the two substrates of this enzyme are 4-(ethylamino)-2-hydroxy-6-(isopropylamino)-1,3,5-triazine and H2O, whereas its two products are N-isopropylammelide and ethylamine.
This enzyme belongs to the family of hydrolases, those acting on carbon-nitrogen bonds other than peptide bonds, specifically in compounds that have not been otherwise categorized within EC number 3.5. The systematic name of this enzyme class is 4-(ethylamino)-2-hydroxy-6-(isopropylamino)-1,3,5-triazine ethylaminohydrolase. Other names in common use include AtzB, and hydroxyatrazine ethylaminohydrolase. This enzyme participates in atrazine degradation.
References.
<templatestyles src="Reflist/styles.css" />
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[
{
"math_id": 0,
"text": "\\rightleftharpoons"
}
] |
https://en.wikipedia.org/wiki?curid=14502986
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14502999
|
Hydroxyisourate hydrolase
|
In enzymology, a hydroxyisourate hydrolase (EC 3.5.2.17) is an enzyme that catalyzes the chemical reaction
5-hydroxyisourate + H2O formula_0 5-hydroxy-2-oxo-4-ureido-2,5-dihydro-1H-imidazole-5-carboxylate
Thus, the two substrates of this enzyme are 5-hydroxyisourate and H2O, whereas its product is 5-hydroxy-2-oxo-4-ureido-2,5-dihydro-1H-imidazole-5-carboxylate.
This enzyme belongs to the family of hydrolases, those acting on carbon-nitrogen bonds other than peptide bonds, specifically in cyclic amides. The systematic name of this enzyme class is 5-hydroxyisourate amidohydrolase. Other names in common use include HIUHase, and 5-hydroxyisourate hydrolase. This enzyme participates in purine metabolism.
Structural studies.
As of late 2007, two structures have been solved for this class of enzymes, with PDB accession codes 2H1X and 2H6U.
References.
<templatestyles src="Reflist/styles.css" />
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[
{
"math_id": 0,
"text": "\\rightleftharpoons"
}
] |
https://en.wikipedia.org/wiki?curid=14502999
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14503011
|
Imidazolonepropionase
|
In enzymology, an imidazolonepropionase (EC 3.5.2.7) is an enzyme that catalyzes the chemical reaction
(S)-3-(5-oxo-4,5-dihydro-3H-imidazol-4-yl)propanoate + H2O formula_0 N-formimidoyl-L-glutamate + H+
Thus, the two substrates of this enzyme are (S)-3-(5-oxo-4,5-dihydro-3H-imidazol-4-yl)propanoate and H2O, whereas its two products are N-formimidoyl-L-glutamate and H+.
This enzyme belongs to the family of hydrolases, those acting on carbon-nitrogen bonds other than peptide bonds, specifically in cyclic amides. The systematic name of this enzyme class is 3-(5-oxo-4,5-dihydro-3H-imidazol-4-yl)propanoate amidohydrolase. Other names in common use include 4(5)-imidazolone-5(4)-propionic acid hydrolase, and imidazolone propionic acid hydrolase. This enzyme participates in histidine metabolism.
Structural studies.
As of late 2007, 6 structures have been solved for this class of enzymes, with PDB accession codes 2BB0, 2G3F, 2GOK, 2OOF, 2PUZ, and 2Q09.
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=14503011
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14503028
|
IMP cyclohydrolase
|
In enzymology, an IMP cyclohydrolase (EC 3.5.4.10) is an enzyme that catalyzes the chemical reaction
IMP + H2O formula_0 5-formamido-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide
Thus, the two substrates of this enzyme are IMP and H2O, whereas its product is 5-formamido-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide.
This enzyme belongs to the family of hydrolases, those acting on carbon-nitrogen bonds other than peptide bonds, specifically in cyclic amidines. The systematic name of this enzyme class is IMP 1,2-hydrolase (decyclizing). Other names in common use include inosinicase, and inosinate cyclohydrolase. This enzyme
catalyses the cyclisation of 5-formylamidoimidazole-4-carboxamide ribonucleotide to IMP, a reaction which is important in "de novo" purine biosynthesis in archaeal species.
Structural studies.
In most cases this single-domain protein is arranged to form an overall fold that consists of a four-layered alpha-beta-beta-alpha core structure. The two antiparallel beta-sheets pack against each other and are covered by alpha-helices on one face of the molecule. The protein is structurally similar to members of the N-terminal nucleophile (NTN) hydrolase superfamily. A deep pocket was in fact found on the surface of IMP cyclohydrolase in a position equivalent to that of active sites of NTN-hydrolases, but an N-terminal nucleophile could not be found. Therefore, it is thought that this enzyme is structurally but not functionally similar to members of the NTN-hydrolase family.
As of late 2007, 14 structures have been solved for this class of enzymes, with PDB accession codes 1G8M, 1M9N, 1OZ0, 1P4R, 1PKX, 1PL0, 1THZ, 2B1G, 2B1I, 2IU0, 2IU3, 2NTK, 2NTL, and 2NTM.
References.
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[
{
"math_id": 0,
"text": "\\rightleftharpoons"
}
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https://en.wikipedia.org/wiki?curid=14503028
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14503041
|
L-lysine-lactamase
|
In enzymology, a L-lysine-lactamase (EC 3.5.2.11) is an enzyme that catalyzes the chemical reaction
L-lysine 1,6-lactam + H2O formula_0 L-lysine
Thus, the two substrates of this enzyme are L-lysine 1,6-lactam and H2O, whereas its product is L-lysine.
This enzyme belongs to the family of hydrolases, those acting on carbon-nitrogen bonds other than peptide bonds, specifically in cyclic amides. The systematic name of this enzyme class is L-lysine-1,6-lactam lactamhydrolase. Other names in common use include L-alpha-aminocaprolactam hydrolase, and L-lysinamidase.
References.
<templatestyles src="Reflist/styles.css" />
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[
{
"math_id": 0,
"text": "\\rightleftharpoons"
}
] |
https://en.wikipedia.org/wiki?curid=14503041
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14503058
|
Long-chain-fatty-acyl-glutamate deacylase
|
In enzymology, a long-chain-fatty-acyl-glutamate deacylase (EC 3.5.1.55) is an enzyme that catalyzes the chemical reaction
N-long-chain-fatty-acyl-L-glutamate + H2O formula_0 a long-chain carboxylate + L-glutamate
Thus, the two substrates of this enzyme are N-long-chain-fatty-acyl-L-glutamate and H2O, whereas its two products are long-chain carboxylate and L-glutamate.
This enzyme belongs to the family of hydrolases, those acting on carbon-nitrogen bonds other than peptide bonds, specifically in linear amides. The systematic name of this enzyme class is N-long-chain-fatty-acyl-L-glutamate amidohydrolase. Other names in common use include long-chain aminoacylase, long-chain-fatty-acyl-glutamate deacylase, long-chain acylglutamate amidase, and N-acyl-D-glutamate deacylase.
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=14503058
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14503076
|
Maleimide hydrolase
|
In enzymology, a maleimide hydrolase (EC 3.5.2.16) is an enzyme that catalyzes the chemical reaction
maleimide + H2O formula_0 maleamic acid
Thus, the two substrates of this enzyme are maleimide and H2O, whereas its product is maleamic acid.
This enzyme belongs to the family of hydrolases, those acting on carbon-nitrogen bonds other than peptide bonds, specifically in cyclic amides. The systematic name of this enzyme class is cyclic-imide amidohydrolase (decyclizing). Other names in common use include imidase, cyclic imide hydrolase, and cyclic-imide amidohydrolase (decyclicizing) [misprint].
References.
<templatestyles src="Reflist/styles.css" />
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[
{
"math_id": 0,
"text": "\\rightleftharpoons"
}
] |
https://en.wikipedia.org/wiki?curid=14503076
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14503093
|
Mandelamide amidase
|
In enzymology, a mandelamide amidase (EC 3.5.1.86) is an enzyme that catalyzes the chemical reaction
(R)-mandelamide + H2O formula_0 (R)-mandelate + NH3
Thus, the two substrates of this enzyme are (R)-mandelamide and H2O, whereas its two products are (R)-mandelate and NH3.
This enzyme belongs to the family of hydrolases, those acting on carbon-nitrogen bonds other than peptide bonds, specifically in linear amides. The systematic name of this enzyme class is mandelamide hydrolase. This enzyme is also called Pseudomonas mandelamide hydrolase.
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=14503093
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14503105
|
Methenyltetrahydrofolate cyclohydrolase
|
In enzymology, a methenyltetrahydrofolate cyclohydrolase (EC 3.5.4.9) is an enzyme that catalyzes the chemical reaction
5,10-methenyltetrahydrofolate + H2O formula_0 10-formyltetrahydrofolate
Thus, the two substrates of this enzyme are 5,10-methenyltetrahydrofolate and H2O, whereas its product is 10-formyltetrahydrofolate.
This enzyme belongs to the family of hydrolases, those acting on carbon-nitrogen bonds other than peptide bonds, specifically in cyclic amidines.
This enzyme participates in glyoxylate and dicarboxylate metabolism and one carbon pool by folate.
Synonyms.
The systematic name of this enzyme class is 5,10-methenyltetrahydrofolate 5-hydrolase (decyclizing).
Other names in common use include:
Structural studies.
As of late 2007, 6 structures have been solved for this class of enzymes, with PDB accession codes 1A4I, 1DIA, 1DIB, 1DIG, 2C2X, and 2C2Y.
References.
<templatestyles src="Reflist/styles.css" />
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[
{
"math_id": 0,
"text": "\\rightleftharpoons"
}
] |
https://en.wikipedia.org/wiki?curid=14503105
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14503133
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Methenyltetrahydromethanopterin cyclohydrolase
|
In enzymology, a methenyltetrahydromethanopterin cyclohydrolase (EC 3.5.4.27) is an enzyme that catalyzes the chemical reaction
5,10-methenyl-5,6,7,8-tetrahydromethanopterin + H2O formula_0 5-formyl-5,6,7,8-tetrahydromethanopterin
Thus, the two substrates of this enzyme are 5,10-methenyl-5,6,7,8-tetrahydromethanopterin and H2O, whereas its product is 5-formyl-5,6,7,8-tetrahydromethanopterin.
This enzyme belongs to the family of hydrolases, those acting on carbon-nitrogen bonds other than peptide bonds, specifically in cyclic amidines. The systematic name of this enzyme class is 5,10-methenyltetrahydromethanopterin 10-hydrolase (decyclizing). Other names in common use include 5,10-methenyltetrahydromethanopterin cyclohydrolase, N5,N10-methenyltetrahydromethanopterin cyclohydrolase, and methenyl-H4MPT cyclohydrolase. This enzyme participates in folate biosynthesis.
References.
<templatestyles src="Reflist/styles.css" />
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[
{
"math_id": 0,
"text": "\\rightleftharpoons"
}
] |
https://en.wikipedia.org/wiki?curid=14503133
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14503147
|
Methylguanidinase
|
In enzymology, a methylguanidinase (EC 3.5.3.16) is an enzyme that catalyzes the chemical reaction
methylguanidine + H2O formula_0 methylamine + urea
Thus, the two substrates of this enzyme are methylguanidine and H2O, whereas its two products are methylamine and urea.
This enzyme belongs to the family of hydrolases, those acting on carbon-nitrogen bonds other than peptide bonds, specifically in linear amidines. The systematic name of this enzyme class is methylguanidine amidinohydrolase. This enzyme is also called methylguanidine hydrolase.
References.
<templatestyles src="Reflist/styles.css" />
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[
{
"math_id": 0,
"text": "\\rightleftharpoons"
}
] |
https://en.wikipedia.org/wiki?curid=14503147
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14503166
|
Mimosinase
|
In enzymology, a mimosinase (EC 3.5.1.61) is an enzyme that catalyzes the chemical reaction
(S)-2-amino-3-(3-hydroxy-4-oxo-4H-pyridin-1-yl)propanoate + H2O formula_0 3-hydroxy-4H-pyrid-4-one + L-serine
Thus, the two substrates of this enzyme are (S)-2-amino-3-(3-hydroxy-4-oxo-4H-pyridin-1-yl)propanoate and H2O, whereas its two products are 3-hydroxy-4H-pyrid-4-one and L-serine.
This enzyme belongs to the family of hydrolases, those acting on carbon-nitrogen bonds other than peptide bonds, specifically in linear amides. The systematic name of this enzyme class is mimosine amidohydrolase.
Occurrence.
Known to occur in all "Leucaena" and "Mimosa". Negi & Borthakur 2016 clone the synthase found in "L. leucocephala" .
Research methods.
Heterologous expression in "E. coli" can be used. Negi & Borthakur 2016 provide a protocol.
References.
<templatestyles src="Reflist/styles.css" />
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[
{
"math_id": 0,
"text": "\\rightleftharpoons"
}
] |
https://en.wikipedia.org/wiki?curid=14503166
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14503181
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N-acetyl-beta-alanine deacetylase
|
In enzymology, a N-acetyl-beta-alanine deacetylase (EC 3.5.1.21) is an enzyme that catalyzes the chemical reaction
N-acetyl-beta-alanine + H2O formula_0 acetate + beta-alanine
Thus, the two substrates of this enzyme are N-acetyl-beta-alanine and H2O, whereas its two products are acetate and beta-alanine.
This enzyme belongs to the family of hydrolases, those acting on carbon-nitrogen bonds other than peptide bonds, specifically in linear amides. The systematic name of this enzyme class is N-acetyl-beta-alanine amidohydrolase. This enzyme participates in beta-alanine metabolism.
References.
<templatestyles src="Reflist/styles.css" />
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[
{
"math_id": 0,
"text": "\\rightleftharpoons"
}
] |
https://en.wikipedia.org/wiki?curid=14503181
|
14503198
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N-acetyldiaminopimelate deacetylase
|
In enzymology, a N-acetyldiaminopimelate deacetylase (EC 3.5.1.47) is an enzyme that catalyzes the chemical reaction
N-acetyl-LL-2,6-diaminoheptanedioate + H2O formula_0 acetate + LL-2,6-diaminoheptanedioate
Thus, the two substrates of this enzyme are N-acetyl-LL-2,6-diaminoheptanedioate and H2O, whereas its two products are acetate and LL-2,6-diaminoheptanedioate.
This enzyme belongs to the family of hydrolases, those acting on carbon-nitrogen bonds other than peptide bonds, specifically in linear amides. The systematic name of this enzyme class is N6-acetyl-LL-2,6-diaminoheptanedioate amidohydrolase. Other names in common use include N-acetyl-L-diaminopimelic acid deacylase, N-acetyl-LL-diaminopimelate deacylase, and 6-N-acetyl-LL-2,6-diaminoheptanedioate amidohydrolase. This enzyme participates in lysine biosynthesis.
References.
<templatestyles src="Reflist/styles.css" />
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[
{
"math_id": 0,
"text": "\\rightleftharpoons"
}
] |
https://en.wikipedia.org/wiki?curid=14503198
|
14503218
|
N-acetylglucosamine-6-phosphate deacetylase
|
In enzymology, N-acetylglucosamine-6-phosphate deacetylase (EC 3.5.1.25), also known as GlcNAc-6-phosphate deacetylase or NagA, is an enzyme that catalyzes the deacetylation of N-acetylglucosamine-6-phosphate (GlcNAc-6-P) to glucosamine-6-phosphate (GlcN-6-P):
H2O + N-acetyl-D-glucosamine 6-phosphate formula_0 acetate + D-glucosamine 6-phosphate
GlcNAc-6-phosphate deacetylase is encoded by the gene NagA.
This enzyme belongs to the amidohydrolase superfamily. Amidohydrolases are a type of hydrolase that acts upon amide bonds. All members of the amidohydrolase family employ a TIM barrel structure, and a vast majority of members are metalloenzymes. The family of enzymes is important in amino acid and nucleotide metabolism as well as biodegradation of agricultural and industrial compounds. NagA participates in amino-sugar metabolism, specifically in the biosynthesis of amino-sugar-nucleotides.
Structure.
NagA is a homodimeric enzyme with two domains in each dimer of the structure. Each domain I comprises a (β/α)8 - barrel structural fold, also known as a TIM barrel, and contains an active site of the enzyme. Each active site consists of the catalytic site of the enzyme and the metal-binding site that are involved in substrate and metal co-factor recognition, respectively. Domain I also forms the dimeric interface with domain I of the neighboring subunit. The smaller second domain of NagA enzymes comprises a β-barrel, which potentially acts to stabilize the enzyme. While all members of the amidohydrolase superfamily employ a TIM-barrel structural fold, NagA in "Escherichia coli" (EcNagA) has a pseudo-TIM barrel enclosing the funnel-like catalytic site of the enzyme. The dimer structure of NagA is considered crucial for the activity and thermostability of the enzyme.
Metal-binding site.
Amidohydrolase enzymes can bind one, two, or three metal atoms in the active site. These metals can include Zn2+, Co2+, Fe2+, Cd2+, and others. EcNagA contains a mononuclear metal-binding site with a Zn2+ ion; in addition, EcNagA shows a phosphate ion bound at the metal-binding site. Unlike EcNagA, NagA of "Mycobacterium smegmatis" (MSNagA) and "Bacillus subtilis" (BsNagA) have binuclear metal-binding sites. MSNagA has two divalent metal ions located in each active site, which are both required for efficient catalysis and structural stability. While most other bacteria species use Zn as their metal co-factor, BsNagA utilizes iron as the predominant metal in the metal-binding site.
Catalytic-binding site.
Most of the active site residues of EcNagA and BsNagA are conserved and share similar structural positions. A notable difference between mycobacterial NagA enzymes and NagA enzymes from other bacterial species is the presence of a cysteine at position 131. Other bacterial species have a lysine residue at this position. This cysteine is located in the flexible loop, which prevents the physiological substrate from binding.
Mechanism.
The catalytic mechanism for NagA enzymes proposed utilizes nucleophilic attack via a metal-coordinated water molecule or hydroxide ion. The mechanism proceeds via a strictly conserved active-site aspartic acid residue (Asp-273) that acts initially as a base to activate the hydrolytic water molecule in order to attack the carbonyl group of the substrate. Asp-273 then acts as an acid to protonate the amine leaving group. One proposed mechanism using the BsNagA and its two iron co-factors in the metal-binding site demonstrates the nucleophilic attack by an Fe-bridged hydroxide and then the stabilization of the carbonyl oxygen by one of the two Fe atoms.
Biological Function.
NagA is located in the cytoplasm of the cell. N-acetylglucosamine (GlcNAc) enters the cell as part of the breakdown of the cell wall. GlcNAc, a monosaccharide and derivative of glucose, is part of a biopolymer in the bacterial cell wall. This biopolymer forms a layered structure called peptidoglycan (PG). GlcNAc is then converted into GlcNAc-6-P by the enzyme NagE. This substrate is then deacetylated into acetate and GlcN-6-P by NagA. NagA is important for the production of GlcN-6-P, which is then used in two main pathways: PG recycling pathway and the glycolysis pathway.
PG recycling pathway.
In the PG Recycling pathway, once GlcNAc-6-P is metabolized by NagA, its product, GlcN-6-P, can then be converted to GlcN-1-P by the enzyme GlmM, followed by reacetylation and reaction with UTP by GlmU to form UDP-GlcNAc. UDP-GlcNAc is the end product of this pathway, which is then used to make glycosaminoglycans, proteoglycans, and glycolipids, which are all necessary in order to replenish PG for the cell wall. PG recycling is necessary for bacterial cells in order to ensure bacteria growth and prevent cell lysis.
Glycolysis pathway.
Instead of entering the PG recycling pathway, GlcN-6-P can be converted into fructose-6-phosphate by NagB. This reaction is reversible by the enzyme GlmS, an amidotransferase. The produced fructose-6-phosphate then enters the glycolysis pathway. Glycolysis catalyzes the production of pyruvate, leading to the citric acid cycle and allowing for the production of amino acids. GlcN-6-P and fructose-6-phosphate act as allosteric regulators of NagA, inhibiting further deacetylation of GlcNAc-6-P.
Disease relevance.
NagA is a potential drug target of "Mycobacterium tuberculosis" (Mtb). Eliminating NagA produces high levels of the allosteric activator GlcNAc-6-P, which prevents the production of GlcN-6-P in order to proceed with the PG recycling pathway. NagA is, therefore, at a crucial metabolic chokepoint in Mtb, representing the key enzymatic step in the generation of essential amino-sugar precursors. These precursors are required for Mtb cell wall biosynthesis and influence the PG recycling pathway. Additionally, the presence of cysteine in MSNagA's active site may represent a unique exploitative target in Mtb therapeutics.
Structural studies.
As of early 2019, 11 structures have been solved for this class of enzymes, with PDB accession codes 1O12, 1UN7, 1YMY, 1YRR, 2P50, 2P53, 6FV3, 6FV4, 3EGJ, 3IV8, and 2VHL.
Nomenclature.
The systematic name of this enzyme class is N-acetyl-D-glucosamine-6-phosphate amidohydrolase. Other names in common use include acetylglucosamine phosphate deacetylase, acetylaminodeoxyglucosephosphate acetylhydrolase, and 2-acetamido-2-deoxy-D-glucose-6-phosphate amidohydrolase.
References.
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[
{
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"text": "\\rightleftharpoons"
}
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https://en.wikipedia.org/wiki?curid=14503218
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14503232
|
N-acetylglucosamine deacetylase
|
In enzymology, a N-acetylglucosamine deacetylase (EC 3.5.1.33) is an enzyme that catalyzes the chemical reaction
N-acetyl-D-glucosamine + H2O formula_0 D-glucosamine + acetate
Thus, the two substrates of this enzyme are N-acetyl-D-glucosamine and H2O, whereas its two products are D-glucosamine and acetate.
This enzyme belongs to the family of hydrolases, those acting on carbon-nitrogen bonds other than peptide bonds, specifically in linear amides. The systematic name of this enzyme class is N-acetyl-D-glucosamine amidohydrolase. Other names in common use include acetylaminodeoxyglucose acetylhydrolase, and N-acetyl-D-glucosaminyl N-deacetylase. This enzyme participates in aminosugars metabolism.
Structural studies.
As of late 2007, two structures have been solved for this class of enzymes, with PDB accession codes 2C1G and 2C1I.
References.
<templatestyles src="Reflist/styles.css" />
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[
{
"math_id": 0,
"text": "\\rightleftharpoons"
}
] |
https://en.wikipedia.org/wiki?curid=14503232
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14503248
|
N-acetylglucosaminylphosphatidylinositol deacetylase
|
In enzymology, a N-acetylglucosaminylphosphatidylinositol deacetylase (EC 3.5.1.89) is an enzyme that catalyzes the chemical reaction
6-(N-acetyl-alpha-D-glucosaminyl)-1-phosphatidyl-1D-myo-inositol + H2O formula_0 6-(alpha-D-glucosaminyl)-1-phosphatidyl-1D-myo-inositol + acetate
Thus, the two substrates of this enzyme are 6-(N-acetyl-alpha-D-glucosaminyl)-1-phosphatidyl-1D-myo-inositol and H2O, whereas its two products are 6-(alpha-D-glucosaminyl)-1-phosphatidyl-1D-myo-inositol and acetate.
This enzyme belongs to the family of hydrolases, those acting on carbon-nitrogen bonds other than peptide bonds, specifically in linear amides. The systematic name of this enzyme class is 6-(N-acetyl-alpha-D-glucosaminyl)-1-phosphatidyl-1D-myo-inositol acetylhydrolase. Other names in common use include N-acetyl-D-glucosaminylphosphatidylinositol acetylhydrolase, N-acetylglucosaminylphosphatidylinositol de-N-acetylase, GlcNAc-PI de-N-acetylase, GlcNAc-PI deacetylase, and acetylglucosaminylphosphatidylinositol deacetylase. This enzyme participates in 3 metabolic pathways: glycosylphosphatidylinositol(gpi)-anchor, and glycan structures - biosynthesis 2.
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=14503248
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14503271
|
N-acyl-D-amino-acid deacylase
|
In enzymology, a N-acyl-D-amino-acid deacylase (EC 3.5.1.81) is an enzyme that catalyzes the chemical reaction
N-acyl-D-amino acid + H2O formula_0 an acid + D-amino acid
Thus, the two substrates of this enzyme are N-acyl-D-amino acid and H2O, whereas its two products are acid and D-amino acid.
This enzyme belongs to the family of hydrolases, those acting on carbon-nitrogen bonds other than peptide bonds, specifically in linear amides. The systematic name of this enzyme class is N-acyl-D-amino acid amidohydrolase. It employs one cofactor, zinc.
Structural studies.
As of late 2007, 8 structures have been solved for this class of enzymes, with PDB accession codes 1M7J, 1RJP, 1RJQ, 1RJR, 1RK5, 1RK6, 1V4Y, and 1V51.
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=14503271
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14503288
|
N-acyl-D-aspartate deacylase
|
In enzymology, a N-acyl-D-aspartate deacylase (EC 3.5.1.83) is an enzyme that catalyzes the chemical reaction
N-acyl-D-aspartate + H2O formula_0 a carboxylate + D-aspartate
Thus, the two substrates of this enzyme are N-acyl-D-aspartate and H2O, whereas its two products are carboxylate and D-aspartate.
This enzyme belongs to the family of hydrolases, those acting on carbon-nitrogen bonds other than peptide bonds, specifically in linear amides. The systematic name of this enzyme class is N-acyl-D-aspartate amidohydrolase. It employs one cofactor, zinc.
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=14503288
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14503301
|
N-acyl-D-glutamate deacylase
|
In enzymology, a N-acyl-D-glutamate deacylase (EC 3.5.1.82) is an enzyme that catalyzes the chemical reaction
N-acyl-D-glutamate + H2O formula_0 a carboxylate + D-glutamate
Thus, the two substrates of this enzyme are N-acyl-D-glutamate and H2O, whereas its two products are carboxylate and D-glutamate.
This enzyme belongs to the family of hydrolases, those acting on carbon-nitrogen bonds other than peptide bonds, specifically in linear amides. The systematic name of this enzyme class is N-acyl-D-glutamate amidohydrolase. It employs one cofactor, zinc.
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=14503301
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14503317
|
Nα-benzyloxycarbonylleucine hydrolase
|
In enzymology, "Nα"-benzyloxycarbonylleucine hydrolase (EC 3.5.1.64) is an enzyme that catalyzes the chemical reaction
"Nα"-benzyloxycarbonyl--leucine + H2O formula_0 benzyl alcohol + CO2 + -leucine
Thus, the two substrates of this enzyme are "Nα"-benzyloxycarbonyl--leucine and H2O, whereas its three products are benzyl alcohol, CO2, and -leucine.
This enzyme belongs to the family of hydrolases, those acting on carbon-nitrogen bonds other than peptide bonds, specifically in linear amides. The systematic name of this enzyme class is Nalpha-benzyloxycarbonyl-L-leucine urethanehydrolase. Other names in common use include benzyloxycarbonylleucine hydrolase, Nalpha-benzyloxycarbonyl amino acid urethane hydrolase IV, and alpha-N-benzyloxycarbonyl-L-leucine urethanehydrolase.
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=14503317
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14503341
|
N-benzyloxycarbonylglycine hydrolase
|
In enzymology, a N-benzyloxycarbonylglycine hydrolase (EC 3.5.1.58) is an enzyme that catalyzes the chemical reaction
N-benzyloxycarbonylglycine + H2O formula_0 benzyl alcohol + CO2 + glycine
Thus, the two substrates of this enzyme are N-benzyloxycarbonylglycine and H2O, whereas its 3 products are benzyl alcohol, CO2, and glycine.
This enzyme belongs to the family of hydrolases, those acting on carbon-nitrogen bonds other than peptide bonds, specifically in linear amides. The systematic name of this enzyme class is N-benzyloxycarbonylglycine urethanehydrolase. Other names in common use include benzyloxycarbonylglycine hydrolase, Nalpha-carbobenzoxyamino acid amidohydrolase, Nalpha-benzyloxycarbonyl amino acid urethane hydrolase, and Nalpha-benzyloxycarbonyl amino acid urethane hydrolase I. It has 2 cofactors: zinc, and Cobalt.
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=14503341
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14503358
|
N-carbamoyl-D-amino acid hydrolase
|
In enzymology, a N-carbamoyl-D-amino acid hydrolase (EC 3.5.1.77) is an enzyme that catalyzes the chemical reaction
N-carbamoyl-D-amino acid + H2O formula_0 D-amino acid + NH3 + CO2
Thus, the two substrates of this enzyme are N-carbamoyl-D-amino acid and H2O, whereas its 3 products are D-amino acid, NH3, and CO2.
This enzyme belongs to the family of hydrolases, those acting on carbon-nitrogen bonds other than peptide bonds, specifically in linear amides.
Structural studies.
As of late 2007, 7 structures have been solved for this class of enzymes, with PDB accession codes 1ERZ, 1UF4, 1UF5, 1UF7, 1UF8, 2GGK, and 2GGL.
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=14503358
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14503373
|
N-carbamoyl-L-amino-acid hydrolase
|
In enzymology, a N-carbamoyl-L-amino-acid hydrolase (EC 3.5.1.87) is an enzyme that catalyzes the chemical reaction
N-carbamoyl-L-2-amino acid (a 2-ureido carboxylate) + H2O formula_0 L-2-amino acid + NH3 + CO2
Thus, the two substrates of this enzyme are N-carbamoyl-L-2-amino acid and H2O, whereas its 3 products are L-2-amino acid, NH3, and CO2.
This enzyme belongs to the family of hydrolases, those acting on carbon-nitrogen bonds other than peptide bonds, specifically in linear amides. The systematic name of this enzyme class is N-carbamoyl-L-amino acid amidohydrolase.
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=14503373
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14503385
|
N-carbamoylputrescine amidase
|
In enzymology, a N-carbamoylputrescine amidase (EC 3.5.1.53) is an enzyme that catalyzes the chemical reaction
N-carbamoylputrescine + H2O formula_0 putrescine + CO2 + NH3
Thus, the two substrates of this enzyme are N-carbamoylputrescine and H2O, whereas its 3 products are putrescine, CO2, and NH3.
This enzyme belongs to the family of hydrolases, those acting on carbon-nitrogen bonds other than peptide bonds, specifically in linear amides. The systematic name of this enzyme class is N-carbamoylputrescine amidohydrolase. Other names in common use include carbamoylputrescine hydrolase, and NCP. This enzyme participates in urea cycle and metabolism of amino groups.
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=14503385
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14503408
|
N-carbamoylsarcosine amidase
|
Class of enzymes
In enzymology, a N-carbamoylsarcosine amidase (EC 3.5.1.59) is an enzyme that catalyzes the chemical reaction
N-carbamoylsarcosine + H2O formula_0 sarcosine + CO2 + NH3
Thus, the two substrates of this enzyme are N-carbamoylsarcosine and H2O, whereas its 3 products are sarcosine, CO2, and NH3.
This enzyme belongs to the family of hydrolases, those acting on carbon-nitrogen bonds other than peptide bonds, specifically in linear amides. The systematic name of this enzyme class is N-carbamoylsarcosine amidohydrolase. This enzyme is also called carbamoylsarcosine amidase. This enzyme participates in arginine and proline metabolism.
Structural studies.
As of late 2007, only one structure has been solved for this class of enzymes, with the PDB accession code 1NBA.
References.
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[
{
"math_id": 0,
"text": "\\rightleftharpoons"
}
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https://en.wikipedia.org/wiki?curid=14503408
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14503427
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N-feruloylglycine deacylase
|
In enzymology, a N-feruloylglycine deacylase (EC 3.5.1.71) is an enzyme that catalyzes the chemical reaction
N-feruloylglycine + H2O formula_0 ferulate + glycine
Thus, the two substrates of this enzyme are N-feruloylglycine and H2O, whereas its two products are ferulate and glycine.
This enzyme belongs to the family of hydrolases, those acting on carbon-nitrogen bonds other than peptide bonds, specifically in linear amides. The systematic name of this enzyme class is N-feruloylglycine amidohydrolase. This enzyme is also called N-feruloylglycine hydrolase.
References.
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[
{
"math_id": 0,
"text": "\\rightleftharpoons"
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https://en.wikipedia.org/wiki?curid=14503427
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14503443
|
N-formylglutamate deformylase
|
In enzymology, a N-formylglutamate deformylase (EC 3.5.1.68) is an enzyme that catalyzes the chemical reaction
N-formyl-L-glutamate + H2O formula_0 formate + L-glutamate
Thus, the two substrates of this enzyme are N-formyl-L-glutamate and H2O, whereas its two products are formate and L-glutamate.
This enzyme belongs to the family of hydrolases, those acting on carbon-nitrogen bonds other than peptide bonds, specifically in linear amides. The systematic name of this enzyme class is N-formyl-L-glutamate amidohydrolase. Other names in common use include beta-citryl-L-glutamate hydrolase, formylglutamate deformylase, N-formylglutamate hydrolase, beta-citrylglutamate amidase, beta-citryl-L-glutamate amidohydrolase, beta-citryl-L-glutamate amidase, beta-citrylglutamate amidase, and beta-citryl-L-glutamate-hydrolyzing enzyme. This enzyme participates in histidine metabolism and glyoxylate and dicarboxylate metabolism.
References.
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[
{
"math_id": 0,
"text": "\\rightleftharpoons"
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https://en.wikipedia.org/wiki?curid=14503443
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14503458
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N-formylmethionylaminoacyl-tRNA deformylase
|
In enzymology, a N-formylmethionylaminoacyl-tRNA deformylase (EC 3.5.1.27) is an enzyme that catalyzes the chemical reaction
N-formyl-L-methionylaminoacyl-tRNA + H2O formula_0 formate + L-methionylaminoacyl-tRNA
Thus, the two substrates of this enzyme are N-formyl-L-methionylaminoacyl-tRNA and H2O, whereas its two products are formate and L-methionylaminoacyl-tRNA.
This enzyme belongs to the family of hydrolases, those acting on carbon-nitrogen bonds other than peptide bonds, specifically in linear amides. The systematic name of this enzyme class is N-formyl-L-methionylaminoacyl-tRNA amidohydrolase. This enzyme participates in glyoxylate and dicarboxylate metabolism.
Structural studies.
As of late 2007, 3 structures have been solved for this class of enzymes, with PDB accession codes 1BSJ, 1BSK, and 1LMH.
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=14503458
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14503474
|
Nicotinamidase
|
In enzymology, a nicotinamidase (EC 3.5.1.19) is an enzyme that catalyzes the chemical reaction
nicotinamide + H2O formula_0 nicotinate + NH3
Thus, the two substrates of this enzyme are nicotinamide and H2O, whereas its two products are nicotinate and NH3.
This enzyme belongs to the family of hydrolases, those acting on carbon-nitrogen bonds other than peptide bonds, specifically in linear amides. The systematic name of this enzyme class is nicotinamide amidohydrolase. Other names in common use include nicotinamide deaminase, nicotinamide amidase, and YNDase. This enzyme participates in nicotinate and nicotinamide metabolism.
Structural studies.
As of late 2007, 3 structures have been solved for this class of enzymes, with PDB accession codes 1ILW, 1IM5, and 2H0R.
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=14503474
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14503494
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Nicotinamide-nucleotide amidase
|
In enzymology, a nicotinamide-nucleotide amidase (EC 3.5.1.42) is an enzyme that catalyzes the chemical reaction
beta-nicotinamide D-ribonucleotide + H2O formula_0 beta-nicotinate D-ribonucleotide + NH3
Thus, the two substrates of this enzyme are beta-nicotinamide D-ribonucleotide and H2O, whereas its two products are beta-nicotinate D-ribonucleotide and NH3.
This enzyme belongs to the family of hydrolases, those acting on carbon-nitrogen bonds other than peptide bonds, specifically in linear amides. The systematic name of this enzyme class is nicotinamide-D-ribonucleotide amidohydrolase. Other names in common use include NMN deamidase, nicotinamide mononucleotide deamidase, and nicotinamide mononucleotide amidohydrolase. This enzyme participates in nicotinate and nicotinamide metabolism.
References.
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[
{
"math_id": 0,
"text": "\\rightleftharpoons"
}
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https://en.wikipedia.org/wiki?curid=14503494
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14503509
|
N-isopropylammelide isopropylaminohydrolase
|
In enzymology, a N-isopropylammelide isopropylaminohydrolase (EC 3.5.99.4) is an enzyme that catalyzes the chemical reaction
N-isopropylammelide + H2O formula_0 cyanuric acid + isopropylamine
Thus, the two substrates of this enzyme are N-isopropylammelide and H2O, whereas its two products are cyanuric acid and isopropylamine.
This enzyme belongs to the family of hydrolases, those acting on carbon-nitrogen bonds other than peptide bonds, specifically in compounds that have not been otherwise categorized within EC number 3.5. The systematic name of this enzyme class is N-isopropylammelide isopropylaminohydrolase. This enzyme is also called AtzC. This enzyme participates in atrazine degradation.
Structural studies.
As of late 2007, only one structure has been solved for this class of enzymes, with the PDB accession code 2QT3.
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=14503509
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14503525
|
N-(long-chain-acyl)ethanolamine deacylase
|
In enzymology, a N-(long-chain-acyl)ethanolamine deacylase (EC 3.5.1.60) is an enzyme that catalyzes the chemical reaction
N-(long-chain-acyl)ethanolamine + H2O formula_0 a long-chain carboxylate + ethanolamine
Thus, the two substrates of this enzyme are N-(long-chain-acyl)ethanolamine and H2O, whereas its two products are long-chain carboxylate and ethanolamine.
This enzyme belongs to the family of hydrolases, those acting on carbon-nitrogen bonds other than peptide bonds, specifically in linear amides. The systematic name of this enzyme class is N-(long-chain-acyl)ethanolamine amidohydrolase. Other names in common use include N-acylethanolamine amidohydrolase, and acylethanolamine amidase.
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=14503525
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14503535
|
N-malonylurea hydrolase
|
In enzymology, a N-malonylurea hydrolase (EC 3.5.1.95) is an enzyme that catalyzes the chemical reaction
3-oxo-3-ureidopropanoate + H2O formula_0 malonate + urea
Thus, the two substrates of this enzyme are 3-oxo-3-ureidopropanoate and H2O, whereas its two products are malonate and urea.
This enzyme belongs to the family of hydrolases, those acting on carbon-nitrogen bonds other than peptide bonds, specifically in linear amides. The systematic name of this enzyme class is 3-oxo-3-ureidopropanoate amidohydrolase (urea- and malonate-forming). This enzyme is also called ureidomalonase.
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=14503535
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14503546
|
N-methyl-2-oxoglutaramate hydrolase
|
In enzymology, a N-methyl-2-oxoglutaramate hydrolase (EC 3.5.1.36) is an enzyme that catalyzes the chemical reaction
N-methyl-2-oxoglutaramate + H2O formula_0 2-oxoglutarate + methylamine
Thus, the two substrates of this enzyme are N-methyl-2-oxoglutaramate and H2O, whereas its two products are 2-oxoglutarate and methylamine.
This enzyme belongs to the family of hydrolases, those acting on carbon-nitrogen bonds other than peptide bonds, specifically in linear amides. The systematic name of this enzyme class is N-methyl-2-oxoglutaramate methylamidohydrolase. This enzyme is also called 5-hydroxy-N-methylpyroglutamate synthase.
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=14503546
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14503556
|
N-methylhydantoinase (ATP-hydrolysing)
|
In enzymology, an N-methylhydantoinase (ATP-hydrolysing) (EC 3.5.2.14) is an enzyme that catalyzes the chemical reaction
ATP + N-methylimidazolidine-2,4-dione + 2 H2O formula_0 ADP + phosphate + N-carbamoylsarcosine
The 3 substrates of this enzyme are ATP, N-methylimidazolidine-2,4-dione, and H2O, whereas its 3 products are ADP, phosphate, and N-carbamoylsarcosine.
This enzyme belongs to the family of hydrolases, those acting on carbon-nitrogen bonds other than peptide bonds, specifically in cyclic amides. The systematic name of this enzyme class is N-methylimidazolidine-2,4-dione amidohydrolase (ATP-hydrolysing). Other names in common use include N-methylhydantoin amidohydrolase, methylhydantoin amidase, N-methylhydantoin hydrolase, and N-methylhydantoinase. This enzyme participates in arginine, creatinine, and proline metabolism.
References.
<templatestyles src="Reflist/styles.css" />
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[
{
"math_id": 0,
"text": "\\rightleftharpoons"
}
] |
https://en.wikipedia.org/wiki?curid=14503556
|
14503573
|
N,N-dimethylformamidase
|
Class of enzymes
In enzymology, a N,N-dimethylformamidase (EC 3.5.1.56) is an enzyme that catalyzes the chemical reaction
N,N-dimethylformamide + H2O formula_0 dimethylamine + formate
Thus, the two substrates of this enzyme are N,N-dimethylformamide and H2O, whereas its two products are dimethylamine and formate.
This enzyme belongs to the family of hydrolases, those acting on carbon-nitrogen bonds other than peptide bonds, specifically in linear amides. The systematic name of this enzyme class is N,N-dimethylformamide amidohydrolase. Other names in common use include dimethylformamidase, and DMFase. This enzyme participates in glyoxylate and dicarboxylate metabolism. It employs one cofactor, iron.
References.
<templatestyles src="Reflist/styles.css" />
|
[
{
"math_id": 0,
"text": "\\rightleftharpoons"
}
] |
https://en.wikipedia.org/wiki?curid=14503573
|
14503588
|
N-substituted formamide deformylase
|
In enzymology, a "N"-substituted formamide deformylase (EC 3.5.1.91) is an enzyme that catalyzes the chemical reaction
"N"-benzylformamide + H2O formula_0 formate + benzylamine
Thus, the two substrates of this enzyme are "N"-benzylformamide and H2O, whereas its two products are formate and benzylamine.
This enzyme belongs to the family of hydrolases, those acting on carbon-nitrogen bonds other than peptide bonds, specifically in linear amides. The systematic name of this enzyme class is "N"-benzylformamide amidohydrolase and is also called NfdA. The enzyme is produced by "Arthrobacter pascens" bacteria.
References.
<templatestyles src="Reflist/styles.css" />
|
[
{
"math_id": 0,
"text": "\\rightleftharpoons"
}
] |
https://en.wikipedia.org/wiki?curid=14503588
|
14503603
|
N-succinylarginine dihydrolase
|
In enzymology, a N-succinylarginine dihydrolase (EC 3.5.3.23) is an enzyme that catalyzes the chemical reaction
N2-succinyl-L-arginine + 2 H2O formula_0 N2-succinyl-L-ornithine + 2 NH3 + CO2
Thus, the two substrates of this enzyme are N2-succinyl-L-arginine and H2O, whereas its 3 products are N2-succinyl-L-ornithine, NH3, and CO2.
This enzyme belongs to the family of hydrolases, those acting on carbon-nitrogen bonds other than peptide bonds, specifically in linear amidines. The systematic name of this enzyme class is N2-succinyl-L-arginine iminohydrolase (decarboxylating). Other names in common use include N2-succinylarginine dihydrolase, arginine succinylhydrolase, SADH, AruB, AstB, and 2-N-succinyl-L-arginine iminohydrolase (decarboxylating). This enzyme participates in arginine and proline metabolism.
References.
<templatestyles src="Reflist/styles.css" />
|
[
{
"math_id": 0,
"text": "\\rightleftharpoons"
}
] |
https://en.wikipedia.org/wiki?curid=14503603
|
14503621
|
Omega-amidase
|
In enzymology, an omega-amidase (EC 3.5.1.3) is an enzyme that catalyzes the chemical reaction
a monoamide of a dicarboxylic acid + H2O formula_0 a dicarboxylate + NH3
Thus, the two substrates of this enzyme are monoamide of a dicarboxylic acid and H2O, whereas its two products are dicarboxylate and NH3.
This enzyme belongs to the family of hydrolases, those acting on carbon-nitrogen bonds other than peptide bonds, specifically in linear amides. The systematic name of this enzyme class is omega-amidodicarboxylate amidohydrolase. This enzyme is also called alpha-keto acid-omega-amidase. This enzyme participates in glutamate metabolism and alanine and aspartate metabolism. This enzyme can be found in mammals, plants, and bacteria.
Structure and active site.
Omega-amidase has two independent monomers that have structure organizations similar to other nitrilase enzymes found in bacteria. Each monomer has a four layered alpha/beta/beta/alpha conformation. The enzyme is asymmetrical and contains a carbon-nitrogen hydrolase fold.
Just as omega-amidase shares a general structure organization as other nitrilases, omega-amidase also contains the same catalytic triad within the active site. This triad of residues includes a nucleophilic cysteine, a glutamate base, and a lysine, all of which are conserved within the structure. In addition to the catalytic triad, omega-amidase also contains a second glutamate that assists in substrate positioning. This second glutamate is why omega-amidase has no activity with glutamine or asparagine, even though they are sized similarly to typical substrates.
Mechanism.
Omega amidase catalyzes the deamidation of several different alpha-keto acids into ammonia and metabolically useful carboxylic acids The general mechanism is the same as for other nitrilases: binding of the substrate to the active site, followed by release of ammonia, formation of a thioester intermediate at the cysteine, binding of water and then release of the carboxylic acid product. Specifically, the active site cysteine acts as a nucleophile and binds to the substrate. The catalytic triad glutamate transfers a proton to the amide group to create and release ammonia. The remaining thioester intermediate is stabilized by the lysine and the backbone amino group following the cysteine. This intermediate is attacked by water to form a stable tetrahedral intermediate. This intermediate breaks down to release the carboxylic acid and restore the enzyme.
Biology.
Omega-amidase operates in coordination with glutamine transaminase to finish off the methionine salvage cycle in bacteria and plants. In the last step to obtain methionine from α-ketomethylthiobutyrate(KMTB), glutamine transaminase K(GTK) converts glutamine to α-ketoglutaramate(KGM). KGM is the main substrate for omega amidase, but KGM exists mainly in the ring form at physiological conditions. Omega-amidase has a higher affinity for the open linear form of KGM that forms more readily at pH 8.5. GTK catalyzes a reversible reaction, but coupling it with omega-amidase makes the transamination reaction irreversible at physiological conditions.
Due to omega-amidase's ability to convert toxic substrates like KGM into components that can be used by other processes, this enzyme can be considered a repair enzyme. Some such substrates are linked to diseases or conditions such as hyperammonemia. A list of some of the substrates that omega-amidase catalyzes may be found in Table 1.
Medical relevance.
The NIT2 gene in humans has been found to be identical to omega-amidase. The gene has the highest expression in the liver and kidney, but is also expressed in almost every human tissue. Overexpression of the NIT2 gene results in decreasing cell proliferation and growth in HeLa cells, which indicates that the gene may have a role in tumor suppression. However further studies are necessary to determine the effect on specific cancers, as a study done with colon cancer cells showed that downregulation of NIT2 induced cell cycle arrest. In addition to tumor suppression, NIT2/omega-amidase may be useful for detection and conversion of oncometabolites. Because omega-amidase is able to control concentration of toxic substrates such as KGM, it is likely that NIT2 can serve the same purpose.
References.
<templatestyles src="Reflist/styles.css" />
Further reading.
<templatestyles src="Refbegin/styles.css" />
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[
{
"math_id": 0,
"text": "\\rightleftharpoons"
}
] |
https://en.wikipedia.org/wiki?curid=14503621
|
14503638
|
Pantetheine hydrolase
|
Class of enzymes
In enzymology, a pantetheine hydrolase (EC 3.5.1.92) is an enzyme that catalyzes the chemical reaction
(R)-pantetheine + H2O formula_0 (R)-pantothenate + 2-aminoethanethiol
Thus, the two substrates of this enzyme are (R)-pantetheine and H2O, whereas its two products are (R)-pantothenate and 2-aminoethanethiol.
This enzyme belongs to the family of hydrolases, those acting on carbon-nitrogen bonds other than peptide bonds, specifically in linear amides. The systematic name of this enzyme class is (R)-pantetheine amidohydrolase. Other names in common use include pantetheinase, vanin, and vanin-1. This enzyme participates in pantothenate and CoA biosynthesis.
|
[
{
"math_id": 0,
"text": "\\rightleftharpoons"
}
] |
https://en.wikipedia.org/wiki?curid=14503638
|
14503654
|
Pantothenase
|
In enzymology, a pantothenase (EC 3.5.1.22) is an enzyme that catalyzes the chemical reaction
(R)-pantothenate + H2O formula_0 (R)-pantoate + beta-alanine
Thus, the two substrates of this enzyme are (R)-pantothenate and H2O, whereas its two products are (R)-pantoate and beta-alanine.
This enzyme belongs to the family of hydrolases, those acting on carbon-nitrogen bonds other than peptide bonds, specifically in linear amides. The systematic name of this enzyme class is (R)-pantothenate amidohydrolase. Other names in common use include pantothenate hydrolase, and pantothenate amidohydrolase. This enzyme participates in pantothenate and coa biosynthesis.
References.
<templatestyles src="Reflist/styles.css" />
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[
{
"math_id": 0,
"text": "\\rightleftharpoons"
}
] |
https://en.wikipedia.org/wiki?curid=14503654
|
14503668
|
Penicillin amidase
|
Class of enzymes
In enzymology, a penicillin amidase (EC 3.5.1.11) is an enzyme that catalyzes the chemical reaction
penicillin + H2O formula_0 a carboxylate + 6-aminopenicillanate
Thus, the two substrates of this enzyme are penicillin and H2O, whereas its two products are carboxylate and 6-aminopenicillanate.
This enzyme belongs to the family of hydrolases, those acting on carbon-nitrogen bonds other than peptide bonds, specifically in linear amides. The systematic name of this enzyme class is penicillin amidohydrolase. Other names in common use include penicillin acylase, benzylpenicillin acylase, novozym 217, semacylase, alpha-acylamino-beta-lactam acylhydrolase, and ampicillin acylase. This enzyme participates in penicillin and cephalosporin biosynthesis.
Structural studies.
As of late 2007, 34 structures have been solved for this class of enzymes, with PDB accession codes 1AI4, 1AI5, 1AI6, 1AI7, 1AJN, 1AJP, 1AJQ, 1CP9, 1E3A, 1FXH, 1FXV, 1GK0, 1GK1, 1GK9, 1GKF, 1GM7, 1GM8, 1GM9, 1H2G, 1JX9, 1K5Q, 1K5S, 1K7D, 1KEC, 1PNK, 1PNL, 1PNM, 2ADV, 2AE3, 2AE4, 2AE5, 2IWM, 2PVA, and 3PVA.
References.
<templatestyles src="Reflist/styles.css" />
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[
{
"math_id": 0,
"text": "\\rightleftharpoons"
}
] |
https://en.wikipedia.org/wiki?curid=14503668
|
14503680
|
Unger model
|
Crosstalk in communication systems
The Unger Model is an empirical standard model for near-end crosstalk (NEXT) power spectra as experienced by communication systems over unshielded twisted pair (UTP).
Twisted pair cables are usually grouped together in a binder where they experience crosstalk. Based on empirical observations, Unger proposed that, at the 1% worst case, the NEXT power spectra formula_0, due to a single disturber, can be bounded by
<br>
formula_1
while the NEXT power spectra due to 49 disturbers (full binder) can be bounded by
<br>
formula_2
|
[
{
"math_id": 0,
"text": "|H_{NEXT}(f)|^2"
},
{
"math_id": 1,
"text": "10\\log(|H_{NEXT}(f)|^2)=\\begin{cases} -66 + 6\\log(f) dB & f < 20 kHz \\\\ -50.5 + 15\\log(f) dB & f \\geq 20 kHz \\end{cases}"
},
{
"math_id": 2,
"text": "10\\log(|H_{NEXT}(f)|^2)=\\begin{cases} -59.2 + 4\\log(f) dB & f < 20 kHz \\\\ -42.2 + 14\\log(f) dB & f \\geq 20 kHz \\end{cases}"
}
] |
https://en.wikipedia.org/wiki?curid=14503680
|
14503685
|
Pentanamidase
|
In enzymology, a pentanamidase (EC 3.5.1.50) is an enzyme that catalyzes the chemical reaction
pentanamide + H2O formula_0 pentanoate + NH3
Thus, the two substrates of this enzyme are pentanamide and H2O, whereas its two products are valerate and NH3.
This enzyme belongs to the family of hydrolases, those acting on carbon-nitrogen bonds other than peptide bonds, specifically in linear amides. The systematic name of this enzyme class is pentanamide amidohydrolase. This enzyme is also called valeramidase.
References.
<templatestyles src="Reflist/styles.css" />
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[
{
"math_id": 0,
"text": "\\rightleftharpoons"
}
] |
https://en.wikipedia.org/wiki?curid=14503685
|
14503696
|
Peptide deformylase
|
In enzymology, a peptide deformylase (EC 3.5.1.88) is an enzyme that removes the formyl group from the N terminus of nascent polypeptide chains in eubacteria, mitochondria and chloroplasts.
Peptide deformylases are metaloenzymes monomers and bind a metal cofactor, typically Fe(II) or Zn, in an active site. Cofactor identity impacts catalytic efficiency.
There are two types of peptide deformylases, types I and II, which differ in structure mainly in the outer surface of the protein.
Human gene PDF (gene) possesses this activity.
Function.
Peptide deformylase removes the formyl group from the N terminus of nascent polypeptides as they are synthesized by the ribosome.
The function of peptide deformylase can be described by the following equation, where formyl-L-methionyl peptide and water react under the formation of formate and methionyl peptide:
H2O + formyl-L-methionyl peptide formula_0 methionyl peptide + formate
This reaction takes place on the surface of the ribosome, where the C-terminal alpha-helix of the peptide deformylase interacts with a grove between ribosomal proteins uL22 and bL32, and rRNA.
For its function this enzyme belongs to the family of hydrolases, those acting on carbon-nitrogen bonds other than peptide bonds, specifically in linear amides. The systematic name of this enzyme class is formyl-L-methionyl peptide amidohydrolase.
Structural studies.
As of late 2007, 34 structures have been solved for this class of enzymes, with PDB accession codes 1IX1, 1LM4, 1LM6, 1LME, 1LQW, 1LQY, 1LRU, 1LRY, 1N5N, 1Q1Y, 1S17, 1SV2, 1SZZ, 1V3Y, 1VEV, 1VEY, 1VEZ, 1WS0, 1WS1, 1XEM, 1XEN, 1XEO, 1Y6H, 1ZXZ, 1ZY0, 1ZY1, 2AI7, 2AI8, 2AI9, 2AIA, 2AIE, 2EW5, 2EW6, and 2EW7.
References.
<templatestyles src="Reflist/styles.css" />
Further reading.
<templatestyles src="Refbegin/styles.css" />
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[
{
"math_id": 0,
"text": "\\rightleftharpoons"
}
] |
https://en.wikipedia.org/wiki?curid=14503696
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14503720
|
Peptidyl-glutaminase
|
In enzymology, a peptidyl-glutaminase (EC 3.5.1.43) is an enzyme that catalyzes the chemical reaction
alpha-N-peptidyl-L-glutamine + H2O formula_0 alpha-N-peptidyl-L-glutamate + NH3
Thus, the two substrates of this enzyme are alpha-N-peptidyl-L-glutamine and H2O, whereas its two products are alpha-N-peptidyl-L-glutamate and NH3.
This enzyme belongs to the family of hydrolases, those acting on carbon-nitrogen bonds other than peptide bonds, specifically in linear amides. The systematic name of this enzyme class is peptidyl-L-glutamine amidohydrolase. Other names in common use include peptidoglutaminase I, peptideglutaminase, and peptidoglutaminase.
References.
<templatestyles src="Reflist/styles.css" />
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[
{
"math_id": 0,
"text": "\\rightleftharpoons"
}
] |
https://en.wikipedia.org/wiki?curid=14503720
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14503737
|
Phosphoribosyl-AMP cyclohydrolase
|
In enzymology, a phosphoribosyl-AMP cyclohydrolase (EC 3.5.4.19) is an enzyme that catalyzes the chemical reaction
1-(5-phosphoribosyl)-AMP + H2O formula_0 1-(5-phosphoribosyl)-5-[(5- phosphoribosylamino)methylideneamino]imidazole-4-carboxamide
Thus, the two substrates of this enzyme are 1-(5-phosphoribosyl)-AMP and H2O, whereas its two products are 1-(5-phosphoribosyl)-5-[(5- and phosphoribosylamino)methylideneamino]imidazole-4-carboxamide.
This enzyme belongs to the family of hydrolases, those acting on carbon-nitrogen bonds other than peptide bonds, specifically in cyclic amidines. The systematic name of this enzyme class is 1-(5-phospho-D-ribosyl)-AMP 1,6-hydrolase. Other names in common use include PRAMP-cyclohydrolase, and phosphoribosyladenosine monophosphate cyclohydrolase. This enzyme participates in histidine metabolism.
Structural studies.
As of late 2007, only one structure has been solved for this class of enzymes, with the PDB accession code 1ZPS.
References.
<templatestyles src="Reflist/styles.css" />
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[
{
"math_id": 0,
"text": "\\rightleftharpoons"
}
] |
https://en.wikipedia.org/wiki?curid=14503737
|
14503751
|
Phthalyl amidase
|
In enzymology, a phthalyl amidase (EC 3.5.1.79) is an enzyme that catalyzes the chemical reaction
a phthalylamide + H2O formula_0 phthalic acid + a substituted amine
Thus, the two substrates of this enzyme are phthalylamide and H2O, whereas its two products are phthalic acid and substituted amine.
This enzyme belongs to the family of hydrolases, those acting on carbon-nitrogen bonds other than peptide bonds, specifically in linear amides. The systematic name of this enzyme class is phthalyl-amide amidohydrolase.
References.
<templatestyles src="Reflist/styles.css" />
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[
{
"math_id": 0,
"text": "\\rightleftharpoons"
}
] |
https://en.wikipedia.org/wiki?curid=14503751
|
14503770
|
Proclavaminate amidinohydrolase
|
In enzymology, a proclavaminate amidinohydrolase (EC 3.5.3.22) is an enzyme that catalyzes the chemical reaction
amidinoproclavaminate + H2O formula_0 proclavaminate + urea
Thus, the two substrates of this enzyme are amidinoproclavaminate and H2O, whereas its two products are proclavaminate and urea.
This enzyme belongs to the family of hydrolases, those acting on carbon-nitrogen bonds other than peptide bonds, specifically in linear amidines. The systematic name of this enzyme class is amidinoproclavaminate amidinohydrolase. Other names in common use include PAH, and proclavaminate amidino hydrolase. This enzyme participates in clavulanic acid biosynthesis.
References.
<templatestyles src="Reflist/styles.css" />
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[
{
"math_id": 0,
"text": "\\rightleftharpoons"
}
] |
https://en.wikipedia.org/wiki?curid=14503770
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14503782
|
Protein-arginine deiminase
|
In enzymology, a protein-arginine deiminase (EC 3.5.3.15) is an enzyme that catalyzes a form of post translational modification called arginine de-imination or citrullination:
protein -arginine + H2O formula_0 protein -citrulline + NH3
Thus, the two substrates of this enzyme are protein -arginine (arginine residue inside a protein) and H2O, whereas its two products are protein -citrulline and NH3:
This enzyme belongs to the family of hydrolases, those acting on carbon-nitrogen bonds other than peptide bonds, specifically in linear amidines. The systematic name of this enzyme class is protein-L-arginine iminohydrolase. This enzyme is also called peptidylarginine deiminase.
Structural studies.
As of late 2007, seven structures have been solved for this class of enzymes, with PDB accession codes 1WD8, 1WD9, 1WDA, 2DEW, 2DEX, 2DEY, and 2DW5.
Mammalian proteins.
Mammals have 5 protein-arginine deiminases, with symbols
except for rodents, there the letter case is different:
The different case is just a historical artifact. It doesn't indicate that the rodent proteins are special.
References.
<templatestyles src="Reflist/styles.css" />
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[
{
"math_id": 0,
"text": "\\rightleftharpoons"
}
] |
https://en.wikipedia.org/wiki?curid=14503782
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14503803
|
Protein-glutamine glutaminase
|
In enzymology, a protein-glutamine glutaminase (EC 3.5.1.44) is an enzyme that catalyzes the chemical reaction
protein L-glutamine + H2O formula_0 protein L-glutamate + NH3
Thus, the two substrates of this enzyme are protein L-glutamine and H2O, whereas its two products are protein L-glutamate and NH3.
This enzyme belongs to the family of hydrolases, those acting on carbon-nitrogen bonds other than peptide bonds, specifically in linear amides. The systematic name of this enzyme class is protein-L-glutamine amidohydrolase. Other names in common use include peptidoglutaminase II, glutaminyl-peptide glutaminase, destabilase, and peptidylglutaminase II.
References.
<templatestyles src="Reflist/styles.css" />
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[
{
"math_id": 0,
"text": "\\rightleftharpoons"
}
] |
https://en.wikipedia.org/wiki?curid=14503803
|
14503824
|
Pterin deaminase
|
In enzymology, a pterin deaminase (EC 3.5.4.11) is an enzyme that catalyzes the chemical reaction
2-amino-4-hydroxypteridine + H2O formula_0 2,4-dihydroxypteridine + NH3
Thus, the two substrates of this enzyme are 2-amino-4-hydroxypteridine and H2O, whereas its two products are 2,4-dihydroxypteridine and NH3.
This enzyme belongs to the family of hydrolases, those acting on carbon-nitrogen bonds other than peptide bonds, specifically in cyclic amidines. The systematic name of this enzyme class is 2-amino-4-hydroxypteridine aminohydrolase. This enzyme is also called acrasinase.
References.
<templatestyles src="Reflist/styles.css" />
|
[
{
"math_id": 0,
"text": "\\rightleftharpoons"
}
] |
https://en.wikipedia.org/wiki?curid=14503824
|
14503842
|
Pyrithiamine deaminase
|
In enzymology, a pyrithiamine deaminase (EC 3.5.4.20) is an enzyme that catalyzes the chemical reaction
1-(4-amino-2-methylpyrimid-5-ylmethyl)-3-(beta-hydroxyethyl)-2- methylpyridinium bromide + H2O formula_0 1-(4-hydroxy-2-methylpyrimid-5-ylmethyl)-3-(beta-hydroxyethyl)-2- methylpyridinium bromide + NH3
The 3 substrates of this enzyme are 1-(4-amino-2-methylpyrimid-5-ylmethyl)-3-(beta-hydroxyethyl)-2-, methylpyridinium bromide, and H2O, whereas its 3 products are 1-(4-hydroxy-2-methylpyrimid-5-ylmethyl)-3-(beta-hydroxyethyl)-2-, methylpyridinium bromide, and NH3.
This enzyme belongs to the family of hydrolases, those acting on carbon-nitrogen bonds other than peptide bonds, specifically in cyclic amidines. The systematic name of this enzyme class is 1-(4-amino-2-methylpyrimid-5-ylmethyl)-3-(beta-hydroxyethyl)-2-methylpyridinium-bromide aminohydrolase.
References.
<templatestyles src="Reflist/styles.css" />
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[
{
"math_id": 0,
"text": "\\rightleftharpoons"
}
] |
https://en.wikipedia.org/wiki?curid=14503842
|
14503855
|
Riboflavinase
|
In enzymology, a riboflavinase (EC 3.5.99.1) is an enzyme that catalyzes the chemical reaction
riboflavin + H2O formula_0 ribitol + lumichrome
Thus, the two substrates of this enzyme are riboflavin and H2O, whereas its two products are ribitol and lumichrome.
This enzyme belongs to the family of hydrolases, those acting on carbon-nitrogen bonds other than peptide bonds, specifically in compounds that have not been otherwise categorized within EC number 3.5. The systematic name of this enzyme class is riboflavin hydrolase. This enzyme participates in riboflavin metabolism.
References.
<templatestyles src="Reflist/styles.css" />
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[
{
"math_id": 0,
"text": "\\rightleftharpoons"
}
] |
https://en.wikipedia.org/wiki?curid=14503855
|
14503871
|
Ricinine nitrilase
|
In enzymology, a ricinine nitrilase (EC 3.5.5.2) is an enzyme that catalyzes the chemical reaction
ricinine + 2 H2O formula_0 3-carboxy-4-methoxy-N-methyl-2-pyridone + NH3
Thus, the two substrates of this enzyme are ricinine and H2O, whereas its two products are 3-carboxy-4-methoxy-N-methyl-2-pyridone and NH3.
This enzyme belongs to the family of hydrolases, those acting on carbon-nitrogen bonds other than peptide bonds, specifically in nitriles. The systematic name of this enzyme class is ricinine aminohydrolase. This enzyme participates in nitrogen metabolism.
References.
<templatestyles src="Reflist/styles.css" />
|
[
{
"math_id": 0,
"text": "\\rightleftharpoons"
}
] |
https://en.wikipedia.org/wiki?curid=14503871
|
14503889
|
S-adenosylhomocysteine deaminase
|
In enzymology, a S-adenosylhomocysteine deaminase (EC 3.5.4.28) is an enzyme that catalyzes the chemical reaction
S-adenosyl-L-homocysteine + H2O formula_0 S-inosyl-L-homocysteine + NH3
Thus, the two substrates of this enzyme are S-adenosyl-L-homocysteine and H2O, whereas its two products are S-inosyl-L-homocysteine and NH3.
This enzyme belongs to the family of hydrolases, those acting on carbon-nitrogen bonds other than peptide bonds, specifically in cyclic amidines. The systematic name of this enzyme class is S-adenosyl-L-homocysteine aminohydrolase. This enzyme is also called adenosylhomocysteine deaminase.
References.
<templatestyles src="Reflist/styles.css" />
|
[
{
"math_id": 0,
"text": "\\rightleftharpoons"
}
] |
https://en.wikipedia.org/wiki?curid=14503889
|
14503909
|
Sepiapterin deaminase
|
In enzymology, a sepiapterin deaminase (EC 3.5.4.24) is an enzyme that catalyzes the chemical reaction
sepiapterin + H2O formula_0 xanthopterin-B2 + NH3
Thus, the two substrates of this enzyme are sepiapterin and H2O whereas its two products are xanthopterin-B2 and NH3.
This enzyme belongs to the family of hydrolases, those acting on carbon-nitrogen bonds other than peptide bonds, specifically in cyclic amidines. The systematic name of this enzyme class is sepiapterin aminohydrolase.
References.
<templatestyles src="Reflist/styles.css" />
|
[
{
"math_id": 0,
"text": "\\rightleftharpoons"
}
] |
https://en.wikipedia.org/wiki?curid=14503909
|
14503924
|
(S)-N-acetyl-1-phenylethylamine hydrolase
|
Class of enzymes
In enzymology, a ("S")-"N"-acetyl-1-phenylethylamine hydrolase (EC 3.5.1.85) is an enzyme that catalyzes the chemical reaction
N-acetylphenylethylamine + H2O formula_0 phenethylamine + acetate
Thus, the two substrates of this enzyme are "N"-acetylphenylethylamine and H2O, whereas its two products are phenethylamine and acetate.
This enzyme belongs to the family of hydrolases, those acting on carbon-nitrogen bonds other than peptide bonds, specifically in linear amides. The systematic name of this enzyme class is ("S")-"N"-acetylphenylethylamine:H2O hydrolase. At least one compound, phenylmethanesulfonylfluoride is known to inhibit this enzyme.
References.
<templatestyles src="Reflist/styles.css" />
|
[
{
"math_id": 0,
"text": "\\rightleftharpoons"
}
] |
https://en.wikipedia.org/wiki?curid=14503924
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14503942
|
Succinyl-diaminopimelate desuccinylase
|
In enzymology, a succinyl-diaminopimelate desuccinylase (EC 3.5.1.18) is an enzyme that catalyzes the chemical reaction
N-succinyl-LL-2,6-diaminoheptanedioate + H2O formula_0 succinate + LL-2,6-diaminoheptanedioate
Thus, the two substrates of this enzyme are N-succinyl-LL-2,6-diaminoheptanedioate and H2O, whereas its two products are succinate and LL-2,6-diaminoheptanedioate.
This enzyme belongs to the family of hydrolases, those acting on carbon-nitrogen bonds other than peptide bonds, specifically in linear amides. The systematic name of this enzyme class is N-succinyl-LL-2,6-diaminoheptanedioate amidohydrolase. This enzyme is also called N-succinyl-L-alpha,epsilon-diaminopimelic acid deacylase. This enzyme participates in lysine biosynthesis.
References.
<templatestyles src="Reflist/styles.css" />
|
[
{
"math_id": 0,
"text": "\\rightleftharpoons"
}
] |
https://en.wikipedia.org/wiki?curid=14503942
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14503962
|
Succinylglutamate desuccinylase
|
In enzymology, a succinylglutamate desuccinylase (EC 3.5.1.96) is an enzyme that catalyzes the chemical reaction
N-succinyl-L-glutamate + H2O formula_0 succinate + L-glutamate
Thus, the two substrates of this enzyme are N-succinyl-L-glutamate and H2O, whereas its two products are succinate and L-glutamate.
This enzyme belongs to the family of hydrolases, those acting on carbon-nitrogen bonds other than peptide bonds, specifically in linear amides. The systematic name of this enzyme class is N-succinyl-L-glutamate amidohydrolase. Other names in common use include N2-succinylglutamate desuccinylase, SGDS, and AstE. This enzyme participates in arginine and proline metabolism.
References.
<templatestyles src="Reflist/styles.css" />
|
[
{
"math_id": 0,
"text": "\\rightleftharpoons"
}
] |
https://en.wikipedia.org/wiki?curid=14503962
|
14503968
|
Theanine hydrolase
|
In enzymology, a theanine hydrolase (EC 3.5.1.65) is an enzyme that catalyzes the chemical reaction
N5-ethyl-L-glutamine + H2O formula_0 L-glutamate + ethylamine
Thus, the two substrates of this enzyme are N5-ethyl-L-glutamine and H2O, whereas its two products are L-glutamate and ethylamine.
This enzyme belongs to the family of hydrolases, those acting on carbon-nitrogen bonds other than peptide bonds, specifically in linear amides. The systematic name of this enzyme class is N5-ethyl-L-glutamine amidohydrolase. Other names in common use include L-theanine amidohydrolase, and 5-N-ethyl-L-glutamine amidohydrolase.
References.
<templatestyles src="Reflist/styles.css" />
|
[
{
"math_id": 0,
"text": "\\rightleftharpoons"
}
] |
https://en.wikipedia.org/wiki?curid=14503968
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145040
|
Conservation of mass
|
Scientific law that a closed system's mass remains constant
In physics and chemistry, the law of conservation of mass or principle of mass conservation states that for any system closed to all transfers of matter and energy, the mass of the system must remain constant over time.
The law implies that mass can neither be created nor destroyed, although it may be rearranged in space, or the entities associated with it may be changed in form. For example, in chemical reactions, the mass of the chemical components before the reaction is equal to the mass of the components after the reaction. Thus, during any chemical reaction and low-energy thermodynamic processes in an isolated system, the total mass of the reactants, or starting materials, must be equal to the mass of the products.
The concept of mass conservation is widely used in many fields such as chemistry, mechanics, and fluid dynamics. Historically, mass conservation in chemical reactions was primarily demonstrated in the 17th century and finally confirmed by Antoine Lavoisier in the late 18th century. The formulation of this law was of crucial importance in the progress from alchemy to the modern natural science of chemistry.
In reality, the conservation of mass only holds approximately and is considered part of a series of assumptions in classical mechanics. The law has to be modified to comply with the laws of quantum mechanics and special relativity under the principle of mass–energy equivalence, which states that energy and mass form one conserved quantity. For very energetic systems the conservation of mass only is shown not to hold, as is the case in nuclear reactions and particle-antiparticle annihilation in particle physics.
Mass is also not generally conserved in open systems. Such is the case when any energy or matter is allowed into, or out of, the system. However, unless radioactivity or nuclear reactions are involved, the amount of energy entering or escaping such systems (as heat, mechanical work, or electromagnetic radiation) is usually too small to be measured as a change in the mass of the system.
For systems that include large gravitational fields, general relativity has to be taken into account; thus mass–energy conservation becomes a more complex concept, subject to different definitions, and neither mass nor energy is as strictly and simply conserved as is the case in special relativity.
Formulation and examples.
The law of conservation of mass can only be formulated in classical mechanics, in which the energy scales associated with an isolated system are much smaller than formula_0, where formula_1 is the mass of a typical object in the system, measured in the frame of reference where the object is at rest, and formula_2 is the speed of light.
The law can be formulated mathematically in the fields of fluid mechanics and continuum mechanics, where the conservation of mass is usually expressed using the continuity equation, given in differential form as formula_3 where formula_4 is the density (mass per unit volume), formula_5 is the time, formula_6 is the divergence, and formula_7 is the flow velocity field.
The interpretation of the continuity equation for mass is the following: For a given closed surface in the system, the change, over any time interval, of the mass enclosed by the surface is equal to the mass that traverses the surface during that time interval: positive if the matter goes in and negative if the matter goes out. For the whole isolated system, this condition implies that the total mass formula_8, the sum of the masses of all components in the system, does not change over time, i.e. formula_9 where formula_10 is the differential that defines the integral over the whole volume of the system.
The continuity equation for the mass is part of the Euler equations of fluid dynamics. Many other convection–diffusion equations describe the conservation and flow of mass and matter in a given system.
In chemistry, the calculation of the amount of reactant and products in a chemical reaction, or stoichiometry, is founded on the principle of conservation of mass. The principle implies that during a chemical reaction the total mass of the reactants is equal to the total mass of the products. For example, in the following reaction
<templatestyles src="Block indent/styles.css"/>CH4 + 2 O2 → CO2 + 2 H2O,
where one molecule of methane (CH4) and two oxygen molecules O2 are converted into one molecule of carbon dioxide (CO2) and two of water (H2O). The number of molecules resulting from the reaction can be derived from the principle of conservation of mass, as initially four hydrogen atoms, 4 oxygen atoms and one carbon atom are present (as well as in the final state); thus the number water molecules produced must be exactly two per molecule of carbon dioxide produced.
Many engineering problems are solved by following the mass distribution of a given system over time; this methodology is known as mass balance.
History.
As early as 520 BCE, Jain philosophy, a non-creationist philosophy based on the teachings of Mahavira, stated that the universe and its constituents such as matter cannot be destroyed or created. The Jain text Tattvarthasutra (2nd century CE) states that a substance is permanent, but its modes are characterised by creation and destruction.
An important idea in ancient Greek philosophy was that "Nothing comes from nothing", so that what exists now has always existed: no new matter can come into existence where there was none before. An explicit statement of this, along with the further principle that nothing can pass away into nothing, is found in Empedocles (c.4th century BCE): "For it is impossible for anything to come to be from what is not, and it cannot be brought about or heard of that what is should be utterly destroyed."
A further principle of conservation was stated by Epicurus around the 3rd century BCE, who wrote in describing the nature of the Universe that "the totality of things was always such as it is now, and always will be".
Discoveries in chemistry.
By the 18th century the principle of conservation of mass during chemical reactions was widely used and was an important assumption during experiments, even before a definition was widely established, though an expression of the law can be dated back to Hero of Alexandria’s time, as can be seen in the works of Joseph Black, Henry Cavendish, and Jean Rey. One of the first to outline the principle was Mikhail Lomonosov in 1756. He may have demonstrated it by experiments and certainly had discussed the principle in 1748 in correspondence with Leonhard Euler, though his claim on the subject is sometimes challenged. According to the Soviet physicist Yakov Dorfman:The universal law was formulated by Lomonosov on the basis of general philosophical materialistic considerations, it was never questioned or tested by him, but on the contrary, served him as a solid starting position in all research throughout his life. A more refined series of experiments were later carried out by Antoine Lavoisier who expressed his conclusion in 1773 and popularized the principle of conservation of mass. The demonstrations of the principle disproved the then popular phlogiston theory that said that mass could be gained or lost in combustion and heat processes.
The conservation of mass was obscure for millennia because of the buoyancy effect of the Earth's atmosphere on the weight of gases. For example, a piece of wood weighs less after burning; this seemed to suggest that some of its mass disappears, or is transformed or lost. This was not disproved until careful experiments were performed in which chemical reactions such as rusting were allowed to take place in sealed glass ampoules; it was found that the chemical reaction did not change the weight of the sealed container and its contents. Weighing of gases using scales was not possible until the invention of the vacuum pump in the 17th century.
Once understood, the conservation of mass was of great importance in progressing from alchemy to modern chemistry. Once early chemists realized that chemical substances never disappeared but were only transformed into other substances with the same weight, these scientists could for the first time embark on quantitative studies of the transformations of substances. The idea of mass conservation plus a surmise that certain "elemental substances" also could not be transformed into others by chemical reactions, in turn led to an understanding of chemical elements, as well as the idea that all chemical processes and transformations (such as burning and metabolic reactions) are reactions between invariant amounts or weights of these chemical elements.
Following the pioneering work of Lavoisier, the exhaustive experiments of Jean Stas supported the consistency of this law in chemical reactions, even though they were carried out with other intentions. His research indicated that in certain reactions the loss or gain could not have been more than 2 to 4 parts in 100,000. The difference in the accuracy aimed at and attained by Lavoisier on the one hand, and by Morley and Stas on the other, is enormous.
Modern physics.
The law of conservation of mass was challenged with the advent of special relativity. In one of the Annus Mirabilis papers of Albert Einstein in 1905, he suggested an equivalence between mass and energy. This theory implied several assertions, like the idea that internal energy of a system could contribute to the mass of the whole system, or that mass could be converted into electromagnetic radiation. However, as Max Planck pointed out, a change in mass as a result of extraction or addition of chemical energy, as predicted by Einstein's theory, is so small that it could not be measured with the available instruments and could not be presented as a test of special relativity. Einstein speculated that the energies associated with newly discovered radioactivity were significant enough, compared with the mass of systems producing them, to enable their change of mass to be measured, once the energy of the reaction had been removed from the system. This later indeed proved to be possible, although it was eventually to be the first artificial nuclear transmutation reaction in 1932, demonstrated by Cockcroft and Walton, that proved the first successful test of Einstein's theory regarding mass loss with energy gain.
The law of conservation of mass and the analogous law of conservation of energy were finally generalized and unified into the principle of mass–energy equivalence, described by Albert Einstein's equation formula_11. Special relativity also redefines the concept of mass and energy, which can be used interchangeably and are defined relative to the frame of reference. Several quantities had to be defined for consistency, such as the "rest mass" of a particle (mass in the rest frame of the particle) and the "relativistic mass" (in another frame). The latter term is usually less frequently used.
Generalization.
Special relativity.
In special relativity, the conservation of mass does not apply if the system is open and energy escapes. However, it does continue to apply to totally closed (isolated) systems. If energy cannot escape a system, its mass cannot decrease. In relativity theory, so long as any type of energy is retained within a system, this energy exhibits mass.
Also, mass must be differentiated from matter, since matter may "not" be perfectly conserved in isolated systems, even though mass is always conserved in such systems. However, matter is so nearly conserved in chemistry that violations of matter conservation were not measured until the nuclear age, and the assumption of matter conservation remains an important practical concept in most systems in chemistry and other studies that do not involve the high energies typical of radioactivity and nuclear reactions.
The mass associated with chemical amounts of energy is too small to measure.
The change in mass of certain kinds of open systems where atoms or massive particles are not allowed to escape, but other types of energy (such as light or heat) are allowed to enter, escape or be merged, went unnoticed during the 19th century, because the change in mass associated with addition or loss of small quantities of thermal or radiant energy in chemical reactions is very small. (In theory, mass would not change at all for experiments conducted in isolated systems where heat and work were not allowed in or out.)
Mass conservation remains correct if energy is not lost.
The conservation of relativistic mass implies the viewpoint of a single observer (or the view from a single inertial frame) since changing inertial frames may result in a change of the total energy (relativistic energy) for systems, and this quantity determines the relativistic mass.
The principle that the mass of a system of particles must be equal to the sum of their rest masses, though true in classical physics, may be false in special relativity. Rest masses cannot be summed to derive the total mass of a system because this practice does not take into account other forms of energy, such as kinetic energy, potential energy, and the energy of massless particles such as photons. All forms of energy in a system affect the total mass of the system.
For moving massive particles in a system, examining the rest masses of the various particles also amounts to introducing many different inertial observation frames, which is prohibited if total system energy and momentum are to be conserved. Additionally, in the rest frame of any one particle this procedure ignores the momenta of other particles, which affect the system mass if the other particles are in motion in this frame.
For the special type of mass called invariant mass, changing the inertial frame of observation for a whole closed system has no effect on the measure of invariant mass of the system, which remains both conserved and invariant (unchanging), even for different observers who view the entire system. Invariant mass is a system combination of energy and momentum, which is invariant for any observer, because in any inertial frame, the energies and momenta of the various particles always add to the same quantity (the momentum may be negative, so the addition amounts to a subtraction). The invariant mass is the relativistic mass of the system when viewed in the center of momentum frame. It is the minimum mass which a system may exhibit, as viewed from all possible inertial frames.
The conservation of both relativistic and invariant mass applies even to systems of particles created by pair production, where energy for new particles may come from kinetic energy of other particles, or from one or more photons as part of a system that includes other particles besides a photon. Again, neither the relativistic nor the invariant mass of totally closed (that is, isolated) systems changes when new particles are created. However, different inertial observers will disagree on the value of this conserved mass, if it is the relativistic mass (i.e., relativistic mass is conserved but not invariant). However, all observers agree on the value of the conserved mass if the mass being measured is the invariant mass (i.e., invariant mass is both conserved and invariant).
The mass–energy equivalence formula gives a different prediction in non-isolated systems, since if energy is allowed to escape a system, both relativistic mass and invariant mass will escape also. In this case, the mass–energy equivalence formula predicts that the change in mass of a system is associated with the change in its energy due to energy being added or subtracted: formula_12 This form of the equation in terms of changes was the form in which it was originally presented by Einstein. In this sense, mass changes in any system are explained if the mass of the energy added or removed from the system is taken into account.
The formula implies that bound systems have an invariant mass (rest mass for the system) less than the sum of their parts, if the binding energy has been allowed to escape the system after the system has been bound. This may happen by converting system potential energy into some other kind of active energy, such as kinetic energy or photons, which easily escape a bound system. The difference in system masses, called a mass defect, is a measure of the binding energy in bound systems – in other words, the energy needed to break the system apart. The greater the mass defect, the larger the binding energy. The binding energy (which itself has mass) must be released (as light or heat) when the parts combine to form the bound system, and this is the reason the mass of the bound system decreases when the energy leaves the system. The total invariant mass is actually conserved, when the mass of the binding energy that has escaped, is taken into account.
General relativity.
In general relativity, the total invariant mass of photons in an expanding volume of space will decrease, due to the red shift of such an expansion. The conservation of both mass and energy therefore depends on various corrections made to energy in the theory, due to the changing gravitational potential energy of such systems.
References.
<templatestyles src="Reflist/styles.css" />
|
[
{
"math_id": 0,
"text": "mc^2"
},
{
"math_id": 1,
"text": "m"
},
{
"math_id": 2,
"text": "c"
},
{
"math_id": 3,
"text": "\\frac{\\partial \\rho}{\\partial t} + \\nabla\\cdot(\\rho \\mathbf{v}) = 0,"
},
{
"math_id": 4,
"text": "\\rho"
},
{
"math_id": 5,
"text": "t"
},
{
"math_id": 6,
"text": "\\nabla\\cdot"
},
{
"math_id": 7,
"text": "\\mathbf{v}"
},
{
"math_id": 8,
"text": "M"
},
{
"math_id": 9,
"text": "\\frac{\\text{d}M}{\\text{d}t} = \\frac{\\text{d}}{\\text{d}t} \\int \\rho \\, \\text{d}V = 0,"
},
{
"math_id": 10,
"text": "\\text{d}V"
},
{
"math_id": 11,
"text": "E = mc^2"
},
{
"math_id": 12,
"text": "\\Delta m = \\Delta E/c^2."
}
] |
https://en.wikipedia.org/wiki?curid=145040
|
14504000
|
Tryptophanamidase
|
In enzymology, a tryptophanamidase (EC 3.5.1.57) is an enzyme that catalyzes the chemical reaction
L-tryptophanamide + H2O formula_0 L-tryptophan + NH3
Thus, the two substrates of this enzyme are L-tryptophanamide and H2O, whereas its two products are L-tryptophan and NH3.
This enzyme belongs to the family of hydrolases, those acting on carbon-nitrogen bonds other than peptide bonds, specifically in linear amides. The systematic name of this enzyme class is L-tryptophanamide amidohydrolase. Other names in common use include tryptophan aminopeptidase, and L-tryptophan aminopeptidase. It employs one cofactor, manganese.
References.
<templatestyles src="Reflist/styles.css" />
|
[
{
"math_id": 0,
"text": "\\rightleftharpoons"
}
] |
https://en.wikipedia.org/wiki?curid=14504000
|
14504011
|
Ureidoglycolate hydrolase
|
Class of enzymes
In enzymology, an ureidoglycolate hydrolase (EC 3.5.3.19) is an enzyme that catalyzes the chemical reaction
(S)-ureidoglycolate + H2O formula_0 glyoxylate + 2 NH3 + CO2
Thus, the two substrates of this enzyme are (S)-ureidoglycolate and H2O, whereas its 3 products are glyoxylate, NH3, and CO2.
This enzyme belongs to the family of hydrolases, those acting on carbon-nitrogen bonds other than peptide bonds, specifically in linear amidines. The systematic name of this enzyme class is (S)-ureidoglycolate amidohydrolase (decarboxylating). 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 1XSQ, 1XSR, 1YQC, and 2BDR.
References.
<templatestyles src="Reflist/styles.css" />
|
[
{
"math_id": 0,
"text": "\\rightleftharpoons"
}
] |
https://en.wikipedia.org/wiki?curid=14504011
|
14504024
|
Ureidosuccinase
|
Class of enzymes
In enzymology, an ureidosuccinase (EC 3.5.1.7) is an enzyme that catalyzes the chemical reaction
N-carbamoyl-L-aspartate + H2O formula_0 L-aspartate + CO2 + NH3
Thus, the two substrates of this enzyme are N-carbamoyl-L-aspartate and H2O, whereas its 3 products are L-aspartate, CO2, and NH3.
This enzyme belongs to the family of hydrolases, those acting on carbon-nitrogen bonds other than peptide bonds, specifically in linear amides. The systematic name of this enzyme class is N-carbamoyl-L-aspartate amidohydrolase. This enzyme participates in alanine and aspartate metabolism.
References.
<templatestyles src="Reflist/styles.css" />
|
[
{
"math_id": 0,
"text": "\\rightleftharpoons"
}
] |
https://en.wikipedia.org/wiki?curid=14504024
|
14504042
|
Urethanase
|
Class of enzymes
In enzymology, an urethanase (EC 3.5.1.75) is an enzyme that catalyzes the chemical reaction
urethane + H2O formula_0 ethanol + CO2 + NH3
Thus, the two substrates of this enzyme are urethane and H2O, whereas its 3 products are ethanol, CO2, and NH3.
This enzyme belongs to the family of hydrolases, those acting on carbon-nitrogen bonds other than peptide bonds, specifically in linear amides. The systematic name of this enzyme class is urethane amidohydrolase (decarboxylating). This enzyme is also called urethane hydrolase.
References.
<templatestyles src="Reflist/styles.css" />
|
[
{
"math_id": 0,
"text": "\\rightleftharpoons"
}
] |
https://en.wikipedia.org/wiki?curid=14504042
|
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