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https://en.wikipedia.org/wiki/Carnitinamidase | In enzymology, a carnitinamidase () is an enzyme that catalyzes the chemical reaction
L-carnitinamide + H2O L-carnitine + NH3
Thus, the two substrates of this enzyme are L-carnitinamide and H2O, whereas its two products are L-carnitine 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-carnitinamide amidohydrolase. Other names in common use include L-carnitinamidase, carnitine amidase, and L-carnitine amidase.
References
Further reading
EC 3.5.1
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Chenodeoxycholoyltaurine%20hydrolase | In enzymology, a chenodeoxycholoyltaurine hydrolase () is an enzyme that catalyzes the chemical reaction
chenodeoxycholoyltaurine + H2O chenodeoxycholate + taurine
Thus, the two substrates of this enzyme are chenodeoxycholoyltaurine and H2O, whereas its two products are chenodeoxycholate and taurine.
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 chenodeoxycholoyltaurine amidohydrolase. This enzyme participates in bile acid biosynthesis.
References
EC 3.5.1
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Chitin%20deacetylase | In enzymology, a chitin deacetylase () is an enzyme that catalyzes the chemical reaction
chitin + H2O chitosan + acetate
Thus, the two substrates of this enzyme are chitin and H2O, whereas its two products are chitosan 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 chitin amidohydrolase. This enzyme participates in aminosugars metabolism.
Structural studies
As of late 2007, only one structure has been solved for this class of enzymes, with the PDB accession code .
References
EC 3.5.1
Enzymes of known structure |
https://en.wikipedia.org/wiki/Choloylglycine%20hydrolase | In enzymology, a choloylglycine hydrolase () is an enzyme that catalyzes the chemical reaction
3alpha,7alpha,12alpha-trihydroxy-5beta-cholan-24-oylglycine + H2O 3alpha,7alpha,12alpha-trihydroxy-5beta-cholanate + glycine
Thus, the two substrates of this enzyme are 3alpha,7alpha,12alpha-trihydroxy-5beta-cholan-24-oylglycine and H2O, whereas its two products are 3alpha,7alpha,12alpha-trihydroxy-5beta-cholanate 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 3alpha,7alpha,12alpha-trihydroxy-5beta-cholan-24-oylglycine amidohydrolase. Other names in common use include glycocholase, bile salt hydrolase, and choloyltaurine hydrolase. This enzyme participates in bile acid biosynthesis.
Structural studies
As of late 2007, 4 structures have been solved for this class of enzymes, with PDB accession codes , , , and .
Research
A 2018 study has linked the enzyme in gut bacteria to obesity and carbohydrate metabolism dominating over fat metabolism.
References
EC 3.5.1
Enzymes of known structure
Obesity |
https://en.wikipedia.org/wiki/Citrullinase | In enzymology, a citrullinase () is an enzyme that catalyzes the chemical reaction
L-citrulline + H2O L-ornithine + CO2 + NH3
Thus, the two substrates of this enzyme are L-citrulline and H2O, whereas its 3 products are L-ornithine, 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 L-citrulline N5-carbamoyldihydrolase. Other names in common use include citrulline ureidase, citrulline hydrolase, and L-citrulline 5-N-carbamoyldihydrolase.
References
EC 3.5.1
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Creatinase | In enzymology, a creatinase () is an enzyme that catalyzes the chemical reaction
creatine + H2O sarcosine + urea
Thus, the two substrates of this enzyme are creatine and H2O, whereas its two products are sarcosine and urea.
The native enzyme was shown to be made up of two subunit monomers via SDS-polyacrylamide gel electrophoresis. The molecular weights of these subunits was estimated to be 47,000 g/mol. The enzyme works as a homodimer, and is induced by choline chloride. Each monomer of creatinase has two clearly defined domains, a small N-terminal domain, and a large C-terminal domain. Each of the two active sites is made by residues of the large domain of one monomer and some residues of the small domain of the other monomer. It has been suggested that a sulfhydryl group is located on or near the active site of the enzyme following inhibition experiments. Creatinase has been found to be most active at pH 8 and is most stable between ph 6-8 for 24 hrs. at 37 degrees.
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 creatine amidinohydrolase. This enzyme participates in arginine and proline metabolism.
Structural studies
As of late 2007, two structures have been solved for this class of enzymes, with PDB accession codes and .
References
EC 3.5.3
Enzymes of known structure |
https://en.wikipedia.org/wiki/Creatininase | In enzymology, a creatininase () is an enzyme that catalyses the hydrolysis of creatinine to creatine, which can then be metabolised to urea and sarcosine by creatinase.
creatinine + H2O creatine
Thus, the two substrates of this enzyme are creatinine and H2O, whereas its product is creatine.
Creatininase is a member of the urease-related amidohydrolases, 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 creatinine amidohydrolase. This enzyme is also called creatinine hydrolase. This enzyme participates in arginine and proline metabolism.
Structural studies
Creatininase from Pseudomonas putida has a core structure consisting of 3-layers, alpha/beta/alpha.
As of late 2007, 4 structures have been solved for this class of enzymes, with PDB accession codes , , , and .
References
EC 3.5.2
Enzymes of known structure |
https://en.wikipedia.org/wiki/Creatinine%20deaminase | In enzymology, a creatinine deaminase () is an enzyme that catalyzes the chemical reaction
creatinine + H2O 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
EC 3.5.4
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Cyanoalanine%20nitrilase | In enzymology, a cyanoalanine nitrilase () is an enzyme that catalyzes the chemical reaction
3-cyano-L-alanine + 2 H2O 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
EC 3.5.5
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Cyanuric%20acid%20amidohydrolase | In enzymology, a cyanuric acid amidohydrolase () is an enzyme that catalyzes the chemical reaction
cyanuric acid + H2O 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
EC 3.5.2
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Cytosine%20deaminase | In enzymology, a cytosine deaminase () is an enzyme that catalyzes the chemical reaction
cytosine + H2O 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 , , , , , , , , , , , , and .
References
EC 3.5.4
Enzymes of known structure |
https://en.wikipedia.org/wiki/D-benzoylarginine-4-nitroanilide%20amidase | In enzymology, a D-benzoylarginine-4-nitroanilide amidase () is an enzyme that catalyzes the chemical reaction
N-benzoyl-D-arginine-4-nitroanilide + H2O 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
EC 3.5.1
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/DCTP%20deaminase | In enzymology, a dCTP deaminase () is an enzyme that catalyzes the chemical reaction
dCTP + H2O 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 , , , , , , , , and .
References
EC 3.5.4
Enzymes of known structure |
https://en.wikipedia.org/wiki/DCTP%20deaminase%20%28dUMP-forming%29 | In enzymology, a dCTP deaminase (dUMP-forming) () is an enzyme that catalyzes the chemical reaction
dCTP + 2 H2O 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 , , and .
References
EC 3.5.4
Enzymes of known structure |
https://en.wikipedia.org/wiki/Deoxycytidine%20deaminase | In enzymology, a deoxycytidine deaminase () is an enzyme that catalyzes the chemical reaction
deoxycytidine + H2O 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
EC 3.5.4
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/D-glutaminase | In enzymology, a D-glutaminase () is an enzyme that catalyzes the chemical reaction
D-glutamine + H2O 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
EC 3.5.1
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Diaminohydroxyphosphoribosylaminopyrimidine%20deaminase | In enzymology, a diaminohydroxyphosphoribosylaminopyrimidine deaminase () is an enzyme that catalyzes the chemical reaction
2,5-diamino-6-hydroxy-4-(5-phosphoribosylamino)pyrimidine + H2O 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 , , , , , and .
References
EC 3.5.4
Enzymes of known structure |
https://en.wikipedia.org/wiki/Diguanidinobutanase | In enzymology, a diguanidinobutanase () is an enzyme that catalyzes the chemical reaction
1,4-diguanidinobutane + H2O 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
EC 3.5.3
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Dihydropyrimidinase | In enzymology, a dihydropyrimidinase () is an enzyme that catalyzes the chemical reaction
5,6-dihydrouracil + H2O 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 , , , , , , , , , and .
References
EC 3.5.2
Enzymes of known structure |
https://en.wikipedia.org/wiki/Dimethylargininase | 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 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 i |
https://en.wikipedia.org/wiki/Enamidase | In enzymology, an enamidase () is an enzyme that catalyzes the chemical reaction
6-oxo-1,4,5,6-tetrahydronicotinate + 2 H2O 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
EC 3.5.2
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Formamidase | In enzymology, a formamidase () is an enzyme that catalyzes the chemical reaction
formamide + H2O 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 , , , and .
References
EC 3.5.1
Enzymes of known structure |
https://en.wikipedia.org/wiki/Formimidoylaspartate%20deiminase | In enzymology, a formimidoylaspartate deiminase () is an enzyme that catalyzes the chemical reaction
N-formimidoyl-L-aspartate + H2O 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
EC 3.5.3
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Formimidoylglutamase | In enzymology, a formimidoylglutamase () is an enzyme that catalyzes the chemical reaction
N-formimidoyl-L-glutamate + H2O 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 and .
References
EC 3.5.3
Enzymes of known structure |
https://en.wikipedia.org/wiki/Formimidoylglutamate%20deiminase | In enzymology, a formimidoylglutamate deiminase () is an enzyme that catalyzes the chemical reaction
N-formimidoyl-L-glutamate + H2O 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
EC 3.5.3
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Formylaspartate%20deformylase | In enzymology, a formylaspartate deformylase () is an enzyme that catalyzes the chemical reaction
N-formyl-L-aspartate + H2O 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
EC 3.5.1
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Formylmethionine%20deformylase | In enzymology, a formylmethionine deformylase () is an enzyme that catalyzes the chemical reaction
N-formyl-L-methionine + H2O 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 , , , , , , , , , , , , , and .
References
EC 3.5.1
Enzymes of known structure |
https://en.wikipedia.org/wiki/Formyltetrahydrofolate%20deformylase | In enzymology, a formyltetrahydrofolate deformylase () is an enzyme that catalyzes the chemical reaction
10-formyltetrahydrofolate + H2O 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
EC 3.5.1
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Gamma-glutamyl-gamma-aminobutyrate%20hydrolase | In enzymology, a gamma-glutamyl-gamma-aminobutyrate hydrolase () is an enzyme that catalyzes the chemical reaction
4-(gamma-glutamylamino)butanoate + H2O 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
EC 3.5.1
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Glucosamine-6-phosphate%20deaminase | In enzymology, a glucosamine-6-phosphate deaminase () is an enzyme that catalyzes the chemical reaction
D-glucosamine 6-phosphate + H2O 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 , , , , and .
References
EC 3.5.99
Enzymes of known structure |
https://en.wikipedia.org/wiki/Glutamin-%28asparagin-%29ase | In enzymology, a glutamin-(asparagin-)ase () is an enzyme that catalyzes the chemical reaction
L-glutamine + H2O 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 , , and .
References
EC 3.5.1
Enzymes of known structure |
https://en.wikipedia.org/wiki/Glutaryl-7-aminocephalosporanic-acid%20acylase | In enzymology, a glutaryl-7-aminocephalosporanic-acid acylase () is an enzyme that catalyzes the chemical reaction
(7R)-7-(4-carboxybutanamido)cephalosporanate + H2O (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
EC 3.5.1
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Glutathionylspermidine%20amidase | In enzymology, a glutathionylspermidine amidase () is an enzyme that catalyzes the chemical reaction
glutathionylspermidine + H2O 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 , , , , and .
References
EC 3.5.1
Enzymes of known structure |
https://en.wikipedia.org/wiki/GTP%20cyclohydrolase%20II | In enzymology, a GTP cyclohydrolase II () is an enzyme that catalyzes the chemical reaction
GTP + 3 H2O 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 and .
References
EC 3.5.4
Enzymes of known structure |
https://en.wikipedia.org/wiki/GTP%20cyclohydrolase%20IIa | In enzymology, a GTP cyclohydrolase IIa () is an enzyme that catalyzes the chemical reaction
GTP + 3 H2O 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
EC 3.5.4
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Guanidinoacetase | In enzymology, a guanidinoacetase () is an enzyme that catalyzes the chemical reaction
guanidinoacetate + H2O 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
EC 3.5.3
Manganese enzymes
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Guanidinobutyrase | In enzymology, a guanidinobutyrase () is an enzyme that catalyzes the chemical reaction
4-guanidinobutanoate + H2O 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
EC 3.5.3
Manganese enzymes
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Guanidinopropionase | In enzymology, a guanidinopropionase () is an enzyme that catalyzes the chemical reaction
3-guanidinopropanoate + H2O 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
EC 3.5.3
Manganese enzymes
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Guanosine%20deaminase | In enzymology, a guanosine deaminase () is an enzyme that catalyzes the chemical reaction
guanosine + H2O 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
EC 3.5.4
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Hippurate%20hydrolase | In enzymology, a hippurate hydrolase () is an enzyme that catalyzes the chemical reaction
hippurate + H2O 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
EC 3.5.1
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Hydroxydechloroatrazine%20ethylaminohydrolase | In enzymology, a hydroxydechloroatrazine ethylaminohydrolase () is an enzyme that catalyzes the chemical reaction
4-(ethylamino)-2-hydroxy-6-(isopropylamino)-1,3,5-triazine + H2O 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
EC 3.5.99
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Hydroxyisourate%20hydrolase | In enzymology, a hydroxyisourate hydrolase () is an enzyme that catalyzes the chemical reaction
5-hydroxyisourate + H2O 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 and .
See also
2-oxo-4-hydroxy-4-carboxy-5-ureidoimidazoline decarboxylase
References
EC 3.5.2
Enzymes of known structure |
https://en.wikipedia.org/wiki/Imidazolonepropionase | In enzymology, an imidazolonepropionase () is an enzyme that catalyzes the chemical reaction
(S)-3-(5-oxo-4,5-dihydro-3H-imidazol-4-yl)propanoate + H2O 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 , , , , , and .
References
EC 3.5.2
Enzymes of known structure |
https://en.wikipedia.org/wiki/IMP%20cyclohydrolase | In enzymology, an IMP cyclohydrolase () is an enzyme that catalyzes the chemical reaction
IMP + H2O 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 |
https://en.wikipedia.org/wiki/L-lysine-lactamase | In enzymology, a L-lysine-lactamase () is an enzyme that catalyzes the chemical reaction
L-lysine 1,6-lactam + H2O 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
EC 3.5.2
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Long-chain-fatty-acyl-glutamate%20deacylase | In enzymology, a long-chain-fatty-acyl-glutamate deacylase () is an enzyme that catalyzes the chemical reaction
N-long-chain-fatty-acyl-L-glutamate + H2O 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
EC 3.5.1
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Maleimide%20hydrolase | In enzymology, a maleimide hydrolase () is an enzyme that catalyzes the chemical reaction
maleimide + H2O 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
EC 3.5.2
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Mandelamide%20amidase | In enzymology, a mandelamide amidase () is an enzyme that catalyzes the chemical reaction
(R)-mandelamide + H2O (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
EC 3.5.1
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Methenyltetrahydrofolate%20cyclohydrolase | In enzymology, a methenyltetrahydrofolate cyclohydrolase () is an enzyme that catalyzes the chemical reaction
5,10-methenyltetrahydrofolate + H2O 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:
Citrovorum factor cyclodehydrase
cyclohydrolase
formyl-methenyl-methylenetetrahydrofolate synthetase (combined).
Structural studies
As of late 2007, 6 structures have been solved for this class of enzymes, with PDB accession codes , , , , , and .
References
EC 3.5.4
Enzymes of known structure |
https://en.wikipedia.org/wiki/Methenyltetrahydromethanopterin%20cyclohydrolase | In enzymology, a methenyltetrahydromethanopterin cyclohydrolase () is an enzyme that catalyzes the chemical reaction
5,10-methenyl-5,6,7,8-tetrahydromethanopterin + H2O 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
EC 3.5.4
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Methylguanidinase | In enzymology, a methylguanidinase () is an enzyme that catalyzes the chemical reaction
methylguanidine + H2O 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
EC 3.5.3
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Mimosinase | In enzymology, a mimosinase () is an enzyme that catalyzes the chemical reaction
(S)-2-amino-3-(3-hydroxy-4-oxo-4H-pyridin-1-yl)propanoate + H2O 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
EC 3.5.1
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/N-acetyl-beta-alanine%20deacetylase | In enzymology, a N-acetyl-beta-alanine deacetylase () is an enzyme that catalyzes the chemical reaction
N-acetyl-beta-alanine + H2O 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
EC 3.5.1
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Aculeacin-A%20deacylase | In enzymology, an aculeacin-A deacylase () is an enzyme that catalyzes the chemical reaction that cleaves the amide bond in aculeacin A and related neutral lipopeptide antibiotics, releasing the long-chain fatty acid side chain.
This enzyme belongs to the family of hydrolases, specifically those acting on carbon-nitrogen bonds other than peptide bonds in linear amides. The systematic name of this enzyme class is aculeacin-A amidohydrolase. This enzyme is also called aculeacin A acylase.
References
EC 3.5.1
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/N-acetyldiaminopimelate%20deacetylase | In enzymology, a N-acetyldiaminopimelate deacetylase () is an enzyme that catalyzes the chemical reaction
N-acetyl-LL-2,6-diaminoheptanedioate + H2O 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
EC 3.5.1
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/N-acetylglucosamine-6-phosphate%20deacetylase | In enzymology, N-acetylglucosamine-6-phosphate deacetylase (), 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 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 amido |
https://en.wikipedia.org/wiki/N-acetylglucosamine%20deacetylase | In enzymology, a N-acetylglucosamine deacetylase () is an enzyme that catalyzes the chemical reaction
N-acetyl-D-glucosamine + H2O 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 and .
References
EC 3.5.1
Enzymes of known structure |
https://en.wikipedia.org/wiki/N-acetylglucosaminylphosphatidylinositol%20deacetylase | In enzymology, a N-acetylglucosaminylphosphatidylinositol deacetylase () is an enzyme that catalyzes the chemical reaction
6-(N-acetyl-alpha-D-glucosaminyl)-1-phosphatidyl-1D-myo-inositol + H2O 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
EC 3.5.1
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/N-acetylmuramoyl-L-alanine%20amidase | In enzymology, a N-acetylmuramoyl-L-alanine amidase () is an enzyme that catalyzes a chemical reaction that cleaves the link between N-acetylmuramoyl residues and L-amino acid residues in certain cell-wall glycopeptides.
This enzyme belongs to the family of hydrolases, specifically those acting on carbon-nitrogen bonds other than peptide bonds in linear amides. The systematic name of this enzyme class is peptidoglycan amidohydrolase. Other names in common use include acetylmuramyl-L-alanine amidase, N-acetylmuramyl-L-alanine amidase, N-acylmuramyl-L-alanine amidase, acetylmuramoyl-alanine amidase, N-acetylmuramic acid L-alanine amidase, acetylmuramyl-alanine amidase, N-acetylmuramylalanine amidase, N-acetylmuramoyl-L-alanine amidase type I, and N-acetylmuramoyl-L-alanine amidase type II. This enzyme participates in peptidoglycan biosynthesis. Autolysins and some phage lysins are examples of N-acetylmuramoyl-L-alanine amidases.
See also
Phage lysins
Autolysins
PGLYRP2
References
EC 3.5.1
Enzymes of known structure |
https://en.wikipedia.org/wiki/N-acyl-D-amino-acid%20deacylase | In enzymology, a N-acyl-D-amino-acid deacylase () is an enzyme that catalyzes the chemical reaction
N-acyl-D-amino acid + H2O 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 , , , , , , , and .
References
EC 3.5.1
Zinc enzymes
Enzymes of known structure |
https://en.wikipedia.org/wiki/N-acyl-D-aspartate%20deacylase | In enzymology, a N-acyl-D-aspartate deacylase () is an enzyme that catalyzes the chemical reaction
N-acyl-D-aspartate + H2O 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
EC 3.5.1
Zinc enzymes
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/N-acyl-D-glutamate%20deacylase | In enzymology, a N-acyl-D-glutamate deacylase () is an enzyme that catalyzes the chemical reaction
N-acyl-D-glutamate + H2O 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
EC 3.5.1
Zinc enzymes
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/VideoBrain%20Family%20Computer | The VideoBrain Family Computer (model 101) is an 8-bit home computer manufactured by Umtech Incorporated, starting in 1977. It is based on the Fairchild Semiconductor F8 CPU. It was not a large commercial success and was discontinued from the market less than three years after its initial release. Some of its lack of success has been attributed to the decision to substitute the APL/S programming language over the then-standard BASIC. Due to the high cost of RAM memory, it only contained 1 KB. It had a full-travel keyboard, unlike some early home computers that featured membrane keypads (and earlier kit machines that used switches), but with a very non-standard layout. It was designed by David Chung and Albert Yu.
History
The VideoBrain Family Computer was designed and produced by Umtech Inc., doing business as the VideoBrain Computer Company of California in 1977. It was not widely available, although Macy's department store briefly carried the computer on its shelves. It was sold in various configurations, and the price ranged from $500 to $1100 depending on the accessories chosen. New software for the VideoBrain was available on cartridge, which was a first for home computer systems (Later price reductions brought costs down to $300 for the computer by itself, and $350–900 for the packaged deals).
Available software ranged in price from $20 to $40 for video games and educational software, and $70 to $150 for productivity tools.
Design
The VideoBrain Family Computer wa |
https://en.wikipedia.org/wiki/Glycosphingolipid%20deacylase | In enzymology, a glycosphingolipid deacylase () is an enzyme that catalyzes a chemical reaction that cleaves gangliosides and neutral glycosphingolipids, releasing fatty acids to form the lyso-derivatives.
This enzyme belongs to the family of hydrolases, specifically those acting on carbon-nitrogen bonds other than peptide bonds, specifically in linear amides. The systematic name of this enzyme class is glycosphingolipid amidohydrolase. This enzyme is also called glycosphingolipid ceramide deacylase.
References
EC 3.5.1
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/N%CE%B1-benzyloxycarbonylleucine%20hydrolase | In enzymology, Nα-benzyloxycarbonylleucine hydrolase () is an enzyme that catalyzes the chemical reaction
Nα-benzyloxycarbonyl-L-leucine + H2O benzyl alcohol + CO2 + L-leucine
Thus, the two substrates of this enzyme are Nα-benzyloxycarbonyl-L-leucine and H2O, whereas its three products are benzyl alcohol, CO2, and L-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
EC 3.5.1
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/N-benzyloxycarbonylglycine%20hydrolase | In enzymology, a N-benzyloxycarbonylglycine hydrolase () is an enzyme that catalyzes the chemical reaction
N-benzyloxycarbonylglycine + H2O 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
EC 3.5.1
Zinc enzymes
Cobalt enzymes
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/N-carbamoyl-D-amino%20acid%20hydrolase | In enzymology, a N-carbamoyl-D-amino acid hydrolase () is an enzyme that catalyzes the chemical reaction
N-carbamoyl-D-amino acid + H2O 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 , , , , , , and .
References
EC 3.5.1
Enzymes of known structure |
https://en.wikipedia.org/wiki/N-carbamoyl-L-amino-acid%20hydrolase | In enzymology, a N-carbamoyl-L-amino-acid hydrolase () is an enzyme that catalyzes the chemical reaction
N-carbamoyl-L-2-amino acid (a 2-ureido carboxylate) + H2O 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
EC 3.5.1
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/N-carbamoylputrescine%20amidase | In enzymology, a N-carbamoylputrescine amidase () is an enzyme that catalyzes the chemical reaction
N-carbamoylputrescine + H2O 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
EC 3.5.1
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Peptide-N4-%28N-acetyl-beta-glucosaminyl%29asparagine%20amidase | In enzymology, a peptide-N4-(N-acetyl-beta-glucosaminyl)asparagine amidase () is an enzyme that catalyzes a chemical reaction that cleaves a N4-(acetyl-beta-D-glucosaminyl)asparagine residue in which the glucosamine residue may be further glycosylated, to yield a (substituted) N-acetyl-beta-D-glucosaminylamine and a peptide containing an aspartate residue. This enzyme belongs to the family of hydrolases, specifically those acting on carbon-nitrogen bonds other than peptide bonds in linear amides.
The NGLY1 gene encodes the ortholog of this enzyme in humans.
Nomenclature
The systematic name of this enzyme class is N-linked-glycopeptide-(N-acetyl-beta-D-glucosaminyl)-L-asparagine amidohydrolase. Other names in common use include:
glycopeptide N-glycosidase,
glycopeptidase,
N-oligosaccharide glycopeptidase,
N-glycanase,
Jack-bean glycopeptidase,
PNGase A, and
PNGase F
Structural studies
The enzyme uses a catalytic triad of cysteine-histidine-aspartate in its active site for hydrolysis by covalent catalysis. A peptide with similar functionality was discovered in 2014 by group at Fudan University in Shanghai, China. This peptide also cleaves alpha 1,3 linkages, and has been named PNGase F-II.
References
Further reading
EC 3.5.1
Enzymes of known structure |
https://en.wikipedia.org/wiki/N-carbamoylsarcosine%20amidase | In enzymology, a N-carbamoylsarcosine amidase () is an enzyme that catalyzes the chemical reaction
N-carbamoylsarcosine + H2O 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 .
References
EC 3.5.1
Enzymes of known structure |
https://en.wikipedia.org/wiki/N-feruloylglycine%20deacylase | In enzymology, a N-feruloylglycine deacylase () is an enzyme that catalyzes the chemical reaction
N-feruloylglycine + H2O 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
EC 3.5.1
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/N-formylglutamate%20deformylase | In enzymology, a N-formylglutamate deformylase () is an enzyme that catalyzes the chemical reaction
N-formyl-L-glutamate + H2O 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
EC 3.5.1
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/N-formylmethionylaminoacyl-tRNA%20deformylase | In enzymology, a N-formylmethionylaminoacyl-tRNA deformylase () is an enzyme that catalyzes the chemical reaction
N-formyl-L-methionylaminoacyl-tRNA + H2O 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 , , and .
References
EC 3.5.1
Enzymes of known structure |
https://en.wikipedia.org/wiki/Nicotinamidase | In enzymology, a nicotinamidase () is an enzyme that catalyzes the chemical reaction
nicotinamide + H2O 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 , , and .
References
EC 3.5.1
Enzymes of known structure |
https://en.wikipedia.org/wiki/Nicotinamide-nucleotide%20amidase | In enzymology, a nicotinamide-nucleotide amidase () is an enzyme that catalyzes the chemical reaction
beta-nicotinamide D-ribonucleotide + H2O 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
EC 3.5.1
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/N-isopropylammelide%20isopropylaminohydrolase | In enzymology, a N-isopropylammelide isopropylaminohydrolase () is an enzyme that catalyzes the chemical reaction
N-isopropylammelide + H2O 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 .
References
EC 3.5.99
Enzymes of known structure |
https://en.wikipedia.org/wiki/N-%28long-chain-acyl%29ethanolamine%20deacylase | In enzymology, a N-(long-chain-acyl)ethanolamine deacylase () is an enzyme that catalyzes the chemical reaction
N-(long-chain-acyl)ethanolamine + H2O 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
EC 3.5.1
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/N-malonylurea%20hydrolase | In enzymology, a N-malonylurea hydrolase () is an enzyme that catalyzes the chemical reaction
3-oxo-3-ureidopropanoate + H2O 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
EC 3.5.1
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/N-methyl-2-oxoglutaramate%20hydrolase | In enzymology, a N-methyl-2-oxoglutaramate hydrolase () is an enzyme that catalyzes the chemical reaction
N-methyl-2-oxoglutaramate + H2O 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
EC 3.5.1
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/N-methylhydantoinase%20%28ATP-hydrolysing%29 | In enzymology, an N-methylhydantoinase (ATP-hydrolysing) () is an enzyme that catalyzes the chemical reaction
ATP + N-methylimidazolidine-2,4-dione + 2 H2O 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
EC 3.5.2
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/N%2CN-dimethylformamidase | In enzymology, a N,N-dimethylformamidase () is an enzyme that catalyzes the chemical reaction
N,N-dimethylformamide + H2O 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
EC 3.5.1
Iron enzymes
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/N-substituted%20formamide%20deformylase | In enzymology, a N-substituted formamide deformylase () is an enzyme that catalyzes the chemical reaction
N-benzylformamide + H2O 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
EC 3.5.1
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/N-succinylarginine%20dihydrolase | In enzymology, a N-succinylarginine dihydrolase () is an enzyme that catalyzes the chemical reaction
N2-succinyl-L-arginine + 2 H2O 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
EC 3.5.3
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Omega-amidase | In enzymology, an omega-amidase () is an enzyme that catalyzes the chemical reaction
a monoamide of a dicarboxylic acid + H2O 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 act |
https://en.wikipedia.org/wiki/Pantetheine%20hydrolase | In enzymology, a pantetheine hydrolase () is an enzyme that catalyzes the chemical reaction
(R)-pantetheine + H2O (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.
References
EC 3.5.1
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Pantothenase | In enzymology, a pantothenase () is an enzyme that catalyzes the chemical reaction
(R)-pantothenate + H2O (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
EC 3.5.1
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Penicillin%20amidase | In enzymology, a penicillin amidase () is an enzyme that catalyzes the chemical reaction
penicillin + H2O 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 , , , , , , , , , , , , , , , , , , , , , , , , , , , , , , , , , and .
References
EC 3.5.1
Enzymes of known structure |
https://en.wikipedia.org/wiki/Pentanamidase | In enzymology, a pentanamidase () is an enzyme that catalyzes the chemical reaction
pentanamide + H2O 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
EC 3.5.1
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Peptide%20deformylase | In enzymology, a peptide deformylase () 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.
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 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 , , , , , , , , , , , , , , , , , , , , , , , , , , , , , , , , , an |
https://en.wikipedia.org/wiki/Peptidyl-glutaminase | In enzymology, a peptidyl-glutaminase () is an enzyme that catalyzes the chemical reaction
alpha-N-peptidyl-L-glutamine + H2O 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
EC 3.5.1
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Phosphoribosyl-AMP%20cyclohydrolase | In enzymology, a phosphoribosyl-AMP cyclohydrolase () is an enzyme that catalyzes the chemical reaction
1-(5-phosphoribosyl)-AMP + H2O 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 .
References
EC 3.5.4
Enzymes of known structure |
https://en.wikipedia.org/wiki/Phthalyl%20amidase | In enzymology, a phthalyl amidase () is an enzyme that catalyzes the chemical reaction
a phthalylamide + H2O 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
EC 3.5.1
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Proclavaminate%20amidinohydrolase | In enzymology, a proclavaminate amidinohydrolase () is an enzyme that catalyzes the chemical reaction
amidinoproclavaminate + H2O 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
EC 3.5.3
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Protein-arginine%20deiminase | In enzymology, a protein-arginine deiminase () is an enzyme that catalyzes a form of post translational modification called arginine de-imination or citrullination:
protein L-arginine + H2O protein L-citrulline + NH3
Thus, the two substrates of this enzyme are protein L-arginine (arginine residue inside a protein) and H2O, whereas its two products are protein L-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 , , , , , , and .
Mammalian proteins
Mammals have 5 protein-arginine deiminases, with symbols
PADI1, PADI2, PADI3, PADI4, PADI6
except for rodents, there the letter case is different:
Padi1, Padi2, Padi3, Padi4, Padi6
The different case is just a historical artifact. It doesn't indicate that the rodent proteins are special.
References
EC 3.5.3
Enzymes of known structure |
https://en.wikipedia.org/wiki/Protein-glutamine%20glutaminase | In enzymology, a protein-glutamine glutaminase () is an enzyme that catalyzes the chemical reaction
protein L-glutamine + H2O 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
EC 3.5.1
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Pterin%20deaminase | In enzymology, a pterin deaminase () is an enzyme that catalyzes the chemical reaction
2-amino-4-hydroxypteridine + H2O 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
EC 3.5.4
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Pyrithiamine%20deaminase | In enzymology, a pyrithiamine deaminase () is an enzyme that catalyzes the chemical reaction
1-(4-amino-2-methylpyrimid-5-ylmethyl)-3-(beta-hydroxyethyl)-2- methylpyridinium bromide + H2O 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
EC 3.5.4
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Riboflavinase | In enzymology, a riboflavinase () is an enzyme that catalyzes the chemical reaction
riboflavin + H2O 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
EC 3.5.99
Enzymes of unknown structure |
https://en.wikipedia.org/wiki/Ricinine%20nitrilase | In enzymology, a ricinine nitrilase () is an enzyme that catalyzes the chemical reaction
ricinine + 2 H2O 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
EC 3.5.5
Enzymes of unknown structure |
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