The Enzyme Database

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EC 3.5.1.1     
Accepted name: asparaginase
Reaction: L-asparagine + H2O = L-aspartate + NH3
Other name(s): asparaginase II; L-asparaginase; colaspase; elspar; leunase; crasnitin; α-asparaginase
Systematic name: L-asparagine amidohydrolase
Links to other databases: BRENDA, EXPASY, GTD, KEGG, MetaCyc, PDB, CAS registry number: 9015-68-3
References:
1.  Halpern, Y.S. and Grossowicz, N. Hydrolysis of amides by extracts from mycobacteria. Biochem. J. 65 (1957) 716–720. [PMID: 13426090]
2.  Ho, P.P.K., Frank, B.H. and Burck, P.J. Crystalline L-asparaginase from Escherichia coli B. Science 165 (1969) 510–512. [DOI] [PMID: 4894591]
3.  Suld, H.M. and Herbut, P.A. Guinea pig serum and liver L-asparaginases. Comparison of serum and papain-digested liver L-asparaginases. J. Biol. Chem. 245 (1970) 2797–2801. [PMID: 4987975]
[EC 3.5.1.1 created 1961]
 
 
EC 3.5.1.2     
Accepted name: glutaminase
Reaction: L-glutamine + H2O = L-glutamate + NH3
Other name(s): glutaminase I; L-glutaminase; glutamine aminohydrolase
Systematic name: L-glutamine amidohydrolase
Links to other databases: BRENDA, EXPASY, GTD, KEGG, MetaCyc, PDB, CAS registry number: 9001-47-2
References:
1.  Kung, H.-F. and Wagner, C. γ-Glutamylmethylamide. A new intermediate in the metabolism of methylamine. J. Biol. Chem. 244 (1969) 4136–4140. [PMID: 5800436]
2.  Roberts, E. Glutaminase. In: Boyer, P.D., Lardy, H. and Myrbäck, K. (Ed.), The Enzymes, 2nd edn, vol. 4, Academic Press, New York, 1960, pp. 285–300.
[EC 3.5.1.2 created 1961]
 
 
EC 3.5.1.3     
Accepted name: ω-amidase
Reaction: a monoamide of a dicarboxylate + H2O = a dicarboxylate + NH3
Other name(s): α-keto acid-ω-amidase
Systematic name: ω-amidodicarboxylate amidohydrolase
Comments: Acts on glutaramate, succinamate and their 2-oxo derivatives.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 9025-19-8
References:
1.  Meister, A., Levintow, L., Greenfield, R.E. and Abendschein, P.A. Hydrolysis and transfer reactions catalyzed by ω-amidase preparations. J. Biol. Chem. 215 (1955) 441–460. [PMID: 14392177]
2.  Meister, A., Radhakrishnan, A.N. and Buckley, S.D. Enzymatic synthesis of L-pipecolic acid and L-proline. J. Biol. Chem. 229 (1957) 789–800. [PMID: 13502341]
[EC 3.5.1.3 created 1961]
 
 
EC 3.5.1.4     
Accepted name: amidase
Reaction: a monocarboxylic acid amide + H2O = a monocarboxylate + NH3
Other name(s): acylamidase; acylase (misleading); amidohydrolase (ambiguous); deaminase (ambiguous); fatty acylamidase; N-acetylaminohydrolase (ambiguous)
Systematic name: acylamide amidohydrolase
Links to other databases: BRENDA, EAWAG-BBD, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 9012-56-0
References:
1.  Bray, H.G., James, S.P., Raffan, I.M., Ryman, B.E. and Thorpe, W.V. The fate of certain organic acids and amides in the rabbit. 7. An amidase of rabbit liver. Biochem. J. 44 (1949) 618–625. [PMID: 16748573]
2.  Bray, H.G., James, S.P., Thorpe, W.V. and Wasdell, M.R. The fate of certain organic acids and amides in the rabbit. 11. Further observations on the hydrolysis of amides by tissue extracts. Biochem. J. 47 (1950) 294–299. [PMID: 14800883]
[EC 3.5.1.4 created 1961, modified 2011]
 
 
EC 3.5.1.5     
Accepted name: urease
Reaction: urea + H2O = CO2 + 2 NH3
Systematic name: urea amidohydrolase
Comments: A nickel protein.
Links to other databases: BRENDA, EAWAG-BBD, EXPASY, GTD, KEGG, MetaCyc, PDB, CAS registry number: 9002-13-5
References:
1.  Dixon, N.E., Gazzola, C., Blakeley, R.L. and Zerner, B. Metal ions in enzymes using ammonia or amides. Science 191 (1976) 1144–1150. [DOI] [PMID: 769157]
2.  Sumner, J.B. Urease. In: Sumner, J.B. and Myrbäck, K. (Ed.), The Enzymes, vol. 1, Academic Press, New York, 1951, pp. 873–892.
3.  Varner, J.E. Urease. In: Boyer, P.D., Lardy, H. and Myrbäck, K. (Ed.), The Enzymes, 2nd edn, vol. 4, Academic Press, New York, 1960, pp. 247–256.
[EC 3.5.1.5 created 1961]
 
 
EC 3.5.1.6     
Accepted name: β-ureidopropionase
Reaction: 3-ureidopropanoate + H2O = β-alanine + CO2 + NH3
For diagram of pyrimidine catabolism, click here
Glossary: 3-ureidopropanoate = N-carbamoyl-β-alanine
Other name(s): N-carbamoyl-β-alanine amidohydrolase
Systematic name: 3-ureidopropanoate amidohydrolase
Comments: The animal enzyme also acts on β-ureidoisobutyrate.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 9027-27-4
References:
1.  Campbell, L.L. Reductive degradation of pyrimidines. 5. Enzymatic conversion of N-carbamyl-β-alanine to β-alanine, carbon dioxide, and ammonia. J. Biol. Chem. 235 (1960) 2375–2378. [PMID: 13849303]
2.  Caravaca, J. and Grisolia, S. Enzymatic decarbamylation of carbamyl β-alanine and carbamyl β-aminoisobutyric acid. J. Biol. Chem. 231 (1958) 357–365. [PMID: 13538975]
3.  Traut, T.W. and Loechel, S. Pyrimidine catabolism: individual characterization of the three sequential enzymes with a new assay. Biochemistry 23 (1984) 2533–2539. [PMID: 6433973]
[EC 3.5.1.6 created 1961]
 
 
EC 3.5.1.7     
Accepted name: ureidosuccinase
Reaction: N-carbamoyl-L-aspartate + H2O = L-aspartate + CO2 + NH3
Systematic name: N-carbamoyl-L-aspartate amidohydrolase
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 9024-81-1
References:
1.  Lieberman, I. and Kornberg, A. Enzymatic synthesis and breakdown of a pyrimidine, orotic acid. III. Ureidosuccinase. J. Biol. Chem. 212 (1955) 909–920. [PMID: 14353892]
[EC 3.5.1.7 created 1961]
 
 
EC 3.5.1.8     
Accepted name: formylaspartate deformylase
Reaction: N-formyl-L-aspartate + H2O = formate + L-aspartate
Other name(s): formylaspartic formylase (formylase I, formylase II)
Systematic name: N-formyl-L-aspartate amidohydrolase
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 9025-09-6
References:
1.  Ohmura, E. and Hayaishi, O. Enzymatic conversion of formylaspartic acid to aspartic acid. J. Biol. Chem. 227 (1957) 181–190. [PMID: 13449063]
[EC 3.5.1.8 created 1961]
 
 
EC 3.5.1.9     
Accepted name: arylformamidase
Reaction: N-formyl-L-kynurenine + H2O = formate + L-kynurenine
For diagram of tryptophan catabolism, click here
Other name(s): kynurenine formamidase; formylase; formylkynureninase; formylkynurenine formamidase; formamidase I; formamidase II
Systematic name: aryl-formylamine amidohydrolase
Comments: Also acts on other aromatic formylamines.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 156229-75-3
References:
1.  Hayaishi, O. and Stanier, R.Y. The bacterial oxidation of tryptophan. III. Enzymatic activities of cell-free extracts from bacteria employing the aromatic pathway. J. Bacteriol. 62 (1951) 691–709. [PMID: 14907621]
2.  Jakoby, W.B. Kynurenine formamidase from Neurospora. J. Biol. Chem. 207 (1954) 657–663. [PMID: 13163050]
3.  Mehler, A.H. and Knox, W.E. The conversion of tryptophan to kynurenine in liver. II. The enzymatic hydrolysis of formylkynurenine. J. Biol. Chem. 187 (1950) 431–438. [PMID: 14794728]
[EC 3.5.1.9 created 1961]
 
 
EC 3.5.1.10     
Accepted name: formyltetrahydrofolate deformylase
Reaction: 10-formyltetrahydrofolate + H2O = formate + tetrahydrofolate
For diagram of folate cofactors, click here
Systematic name: 10-formyltetrahydrofolate amidohydrolase
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 9025-08-5
References:
1.  Huennekens, F.M. Enzymatic deacylation of N10-formyltetrahydrofolic acid. Fed. Proc. 16 (1957) 199.
[EC 3.5.1.10 created 1961]
 
 
EC 3.5.1.11     
Accepted name: penicillin amidase
Reaction: penicillin + H2O = a carboxylate + 6-aminopenicillanate
For diagram of penicillin biosynthesis and metabolism, click here
Other name(s): penicillin acylase; benzylpenicillin acylase; novozym 217; semacylase; α-acylamino-β-lactam acylhydrolase; ampicillin acylase
Systematic name: penicillin amidohydrolase
Links to other databases: BRENDA, EXPASY, GTD, KEGG, MetaCyc, PDB, CAS registry number: 9014-06-6
References:
1.  Sakaguchi, K. and Murao, S. A preliminary report on a new enzyme, "penicillin-amidase". J. Agric. Chem. Soc. Jpn. 23 (1950) 411.
[EC 3.5.1.11 created 1961]
 
 
EC 3.5.1.12     
Accepted name: biotinidase
Reaction: biotin amide + H2O = biotin + NH3
Other name(s): amidohydrolase biotinidase
Systematic name: biotin-amide amidohydrolase
Comments: Also acts on biotin esters.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 9025-15-4
References:
1.  Knappe, J., Brümer, W. and Biederbick, K. Reinigung und Eigenschaften der Biotinidase aus Schweinenieren und Lactobacillus casei. Biochem. Z. 338 (1963) 599–613. [PMID: 14087327]
2.  Thoma, R.W. and Peterson, W.H. The enzymatic degradation of soluble bound biotin. J. Biol. Chem. 210 (1954) 569–579. [PMID: 13211594]
[EC 3.5.1.12 created 1961]
 
 
EC 3.5.1.13     
Accepted name: aryl-acylamidase
Reaction: an anilide + H2O = a carboxylate + aniline
Other name(s): AAA-1; AAA-2; brain acetylcholinesterase (is associated with AAA-2); pseudocholinesterase (associated with arylacylamidase)
Systematic name: aryl-acylamide amidohydrolase
Comments: Also acts on 4-substituted anilides.
Links to other databases: BRENDA, EAWAG-BBD, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 9025-18-7
References:
1.  Nimmo-Smith, R.H. Aromatic N-deacylation by chick-kidney mitochondria. Biochem. J. 75 (1960) 284–293. [PMID: 14427286]
[EC 3.5.1.13 created 1965]
 
 
EC 3.5.1.14     
Accepted name: N-acyl-aliphatic-L-amino acid amidohydrolase
Reaction: (1) an N-acyl-aliphatic-L-amino acid + H2O = an aliphatic L-amino acid + a carboxylate
(2) an N-acetyl-L-cysteine-S-conjugate + H2O = an L-cysteine-S-conjugate + acetate
Glossary: N-acetyl-L-cysteine-S-conjugate = mercapturic acid
Other name(s): aminoacylase 1; aminoacylase I; dehydropeptidase II; histozyme; hippuricase; benzamidase; acylase I; hippurase; amido acid deacylase; L-aminoacylase; acylase; aminoacylase; L-amino-acid acylase; α-N-acylaminoacid hydrolase; long acyl amidoacylase; short acyl amidoacylase; ACY1 (gene name); N-acyl-L-amino-acid amidohydrolase
Systematic name: N-acyl-aliphatic-L-amino acid amidohydrolase (carboxylate-forming)
Comments: Contains Zn2+. The enzyme is found in animals and is involved in the hydrolysis of N-acylated or N-acetylated amino acids (except L-aspartate). It acts on mercapturic acids (S-conjugates of N-acetyl-L-cysteine) and neutral aliphatic N-acyl-α-amino acids. Some bacterial aminoacylases demonstrate substrate specificity of both EC 3.5.1.14 and EC 3.5.1.114. cf. EC 3.5.1.15, aspartoacylase and EC 3.5.1.114, N-acyl-aromatic-L-amino acid amidohydrolase.
Links to other databases: BRENDA, EXPASY, GTD, KEGG, MetaCyc, PDB, CAS registry number: 9012-37-7
References:
1.  Birnbaum, S.M., Levintow, L., Kingsley, R.B. and Greenstein, J.P. Specificity of amino acid acylases. J. Biol. Chem. 194 (1952) 455–470. [PMID: 14927637]
2.  Fones, W.S. and Lee, M. Hydrolysis of N-acyl derivatives of alanine and phenylalanine by acylase I and carboxypeptidase. J. Biol. Chem. 201 (1953) 847–856. [PMID: 13061423]
3.  Henseling, J. and Rohm, K.H. Aminoacylase I from hog kidney: anion effects and the pH dependence of kinetic parameters. Biochim. Biophys. Acta 959 (1988) 370–377. [DOI] [PMID: 3355856]
4.  Heese, D., Berger, S. and Rohm, K.H. Nuclear magnetic relaxation studies of the role of the metal ion in Mn2+-substituted aminoacylase I. Eur. J. Biochem. 188 (1990) 175–180. [DOI] [PMID: 2318199]
5.  Palm, G.J. and Rohm, K.H. Aminoacylase I from porcine kidney: identification and characterization of two major protein domains. J. Protein Chem. 14 (1995) 233–240. [PMID: 7662111]
6.  Uttamsingh, V., Keller, D.A. and Anders, M.W. Acylase I-catalyzed deacetylation of N-acetyl-L-cysteine and S-alkyl-N-acetyl-L-cysteines. Chem. Res. Toxicol. 11 (1998) 800–809. [DOI] [PMID: 9671543]
7.  Lindner, H., Hopfner, S., Tafler-Naumann, M., Miko, M., Konrad, L. and Rohm, K.H. The distribution of aminoacylase I among mammalian species and localization of the enzyme in porcine kidney. Biochimie 82 (2000) 129–137. [DOI] [PMID: 10727768]
[EC 3.5.1.14 created 1965, modified 2013]
 
 
EC 3.5.1.15     
Accepted name: aspartoacylase
Reaction: N-acyl-L-aspartate + H2O = a carboxylate + L-aspartate
Other name(s): aminoacylase II; N-acetylaspartate amidohydrolase; acetyl-aspartic deaminase; acylase II
Systematic name: N-acyl-L-aspartate amidohydrolase
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 9031-86-1
References:
1.  Birnbaum, S.M. Aminoacylase. Amino acid aminoacylases I and II from hog kidney. Methods Enzymol. 2 (1955) 115–119.
2.  Birnbaum, S.M., Levintow, L., Kingsley, R.B. and Greenstein, J.P. Specificity of amino acid acylases. J. Biol. Chem. 194 (1952) 455–470. [PMID: 14927637]
[EC 3.5.1.15 created 1965]
 
 
EC 3.5.1.16     
Accepted name: acetylornithine deacetylase
Reaction: N2-acetyl-L-ornithine + H2O = acetate + L-ornithine
For diagram of ornithine biosynthesis, click here
Other name(s): acetylornithinase; N-acetylornithinase; 2-N-acetyl-L-ornithine amidohydrolase
Systematic name: N2-acetyl-L-ornithine amidohydrolase
Comments: Also hydrolyses N-acetylmethionine.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 9025-12-1
References:
1.  Vogel, H.J. Path of ornithine synthesis in Escherichia coli. Proc. Natl. Acad. Sci. USA 39 (1953) 578–583. [DOI] [PMID: 16589307]
2.  Vogel, H.J. and Bonner, D.M. Acetylornithine deacetylase of Escherichia coli : partial purification and some properties. J. Biol. Chem. 218 (1956) 97–106. [PMID: 13278318]
[EC 3.5.1.16 created 1965]
 
 
EC 3.5.1.17     
Accepted name: acyl-lysine deacylase
Reaction: N6-acyl-L-lysine + H2O = a carboxylate + L-lysine
Other name(s): ε-lysine acylase; 6-N-acyl-L-lysine amidohydrolase
Systematic name: N6-acyl-L-lysine amidohydrolase
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 9025-11-0
References:
1.  Paik, W.K., Bloch-Frankenthal, L., Birnbaum, S.M., Winitz, M. and Greenstein, J.P. ε-Lysine acylase. Arch. Biochem. Biophys. 69 (1957) 56–66. [PMID: 13445179]
[EC 3.5.1.17 created 1965]
 
 
EC 3.5.1.18     
Accepted name: succinyl-diaminopimelate desuccinylase
Reaction: N-succinyl-LL-2,6-diaminoheptanedioate + H2O = succinate + LL-2,6-diaminoheptanedioate
Other name(s): N-succinyl-L-α,ε-diaminopimelic acid deacylase
Systematic name: N-succinyl-LL-2,6-diaminoheptanedioate amidohydrolase
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 9024-94-6
References:
1.  Kindler, S.H. and Gilvarg, C. N-Succinyl-L-2,6-diaminopimelic acid deacylase. J. Biol. Chem. 235 (1960) 3532–3535. [PMID: 13756049]
[EC 3.5.1.18 created 1965]
 
 
EC 3.5.1.19     
Accepted name: nicotinamidase
Reaction: nicotinamide + H2O = nicotinate + NH3
Other name(s): nicotinamide deaminase; nicotinamide amidase; YNDase
Systematic name: nicotinamide amidohydrolase
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 9033-32-3
References:
1.  Petrack, B., Greengard, P., Craston, A. and Sheppy, F. Nicotinamide deamidase from mammalian liver. J. Biol. Chem. 240 (1965) 1725–1730. [PMID: 14285515]
2.  Sarma, D.S.R., Rajalakshmi, S. and Sarma, S. Studies on the enzymes involved in nicotinamide adenine dinucleotide metabolism in Aspergillus niger. Biochim. Biophys. Acta 81 (1964) 311–322.
[EC 3.5.1.19 created 1972]
 
 
EC 3.5.1.20     
Accepted name: citrullinase
Reaction: L-citrulline + H2O = L-ornithine + CO2 + NH3
Other name(s): citrulline ureidase; citrulline hydrolase; L-citrulline 5-N-carbamoyldihydrolase
Systematic name: L-citrulline N5-carbamoyldihydrolase
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 59088-17-4
References:
1.  Hill, D.L. and Chambers, P. The biosynthesis of proline by Tetrahymena pyriformis. Biochim. Biophys. Acta 148 (1967) 435–447. [DOI] [PMID: 6075416]
[EC 3.5.1.20 created 1972]
 
 
EC 3.5.1.21     
Accepted name: N-acetyl-β-alanine deacetylase
Reaction: N-acetyl-β-alanine + H2O = acetate + β-alanine
Systematic name: N-acetyl-β-alanine amidohydrolase
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 37289-04-6
References:
1.  Fujimoto, D., Koyama, T. and Tamiya, N. N-Acetyl-β-alanine deacetylase in hog kidney. Biochim. Biophys. Acta 167 (1968) 407–413.
[EC 3.5.1.21 created 1972]
 
 
EC 3.5.1.22     
Accepted name: pantothenase
Reaction: (R)-pantothenate + H2O = (R)-pantoate + β-alanine
For diagram of pantothenate catabolism, click here
Other name(s): pantothenate hydrolase; pantothenate amidohydrolase
Systematic name: (R)-pantothenate amidohydrolase
Links to other databases: BRENDA, EXPASY, GTD, KEGG, MetaCyc, CAS registry number: 9076-90-8
References:
1.  Nurmikko, V., Salo, E., Hakola, H., Makinen, K. and Snell, E.E. The bacterial degradation of pantothenic acid. II. Pantothenate hydrolase. Biochemistry 5 (1966) 399–402. [PMID: 5940928]
[EC 3.5.1.22 created 1972]
 
 
EC 3.5.1.23     
Accepted name: ceramidase
Reaction: a ceramide + H2O = a carboxylate + sphingosine
Glossary: a ceramide = an N-acylsphingosine
Other name(s): acylsphingosine deacylase; glycosphingolipid ceramide deacylase
Systematic name: N-acylsphingosine amidohydrolase
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 37289-06-8
References:
1.  Nilsson, A. The presence of spingomyelin- and ceramide-cleaving enzymes in the small intestinal tract. Biochim. Biophys. Acta 176 (1969) 339–347. [DOI] [PMID: 5775951]
2.  Yavin, E. and Gatt, S. Enzymatic hydrolysis of sphingolipids. 8. Further purification and properties of rat brain ceramidase. Biochemistry 8 (1969) 1692–1698. [PMID: 5805303]
[EC 3.5.1.23 created 1972, modified 1990]
 
 
EC 3.5.1.24     
Accepted name: choloylglycine hydrolase
Reaction: glycocholate + H2O = cholate + glycine
For diagram of cholic acid conjugates biosynthesis, click here
Glossary: glycocholate = N-(3α,7α,12α-trihydroxy-5β-cholan-24-oyl)glycine
cholate = 3α,7α,12α-trihydroxy-5β-cholan-24-oate
Other name(s): glycocholase; bile salt hydrolase; choloyltaurine hydrolase; 3α,7α,12α-trihydroxy-5β-cholan-24-oylglycine amidohydrolase
Systematic name: glycocholate amidohydrolase
Comments: Also acts on the 3α,12α-dihydroxy-derivative, and on choloyl-taurine.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 37289-07-9
References:
1.  Nair, P.P., Gordon, M. and Reback, J. The enzymatic cleavage of the carbon-nitrogen bond in 3α,7α,12α-trihydroxy-5-β-cholan-24-oylglycine. J. Biol. Chem. 242 (1967) 7–11. [PMID: 6016335]
2.  Stellwag, E.J. and Hylemon, P.B. Purification and characterization of bile salt hydrolase from Bacteroides fragilis subsp. fragilis. Biochim. Biophys. Acta 452 (1976) 165–176. [DOI] [PMID: 10993]
[EC 3.5.1.24 created 1972]
 
 
EC 3.5.1.25     
Accepted name: N-acetylglucosamine-6-phosphate deacetylase
Reaction: N-acetyl-D-glucosamine 6-phosphate + H2O = D-glucosamine 6-phosphate + acetate
For diagram of the biosynthesis of UDP-N-acetylglucosamine, click here
Other name(s): acetylglucosamine phosphate deacetylase; acetylaminodeoxyglucosephosphate acetylhydrolase; 2-acetamido-2-deoxy-D-glucose-6-phosphate amidohydrolase
Systematic name: N-acetyl-D-glucosamine-6-phosphate amidohydrolase
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 9027-50-3
References:
1.  White, R.J. and Pasternak, C.A. The purification and properties of N-acetylglucosamine 6-phosphate deacetylase from Escherichia coli. Biochem. J. 105 (1967) 121–125. [PMID: 4861885]
2.  Yamano, N., Matsushita, Y., Kamada, Y., Fujishima, S., Arita, M. Purification and characterization of N-acetylglucosamine 6-phosphate deacetylase with activity against N-acetylglucosamine from Vibrio cholerae non-O1. Biosci. Biotechnol. Biochem. 60 (1996) 1320–1323. [DOI] [PMID: 8987551]
[EC 3.5.1.25 created 1972 (EC 3.5.1.80 created 1999, incorporated 2002)]
 
 
EC 3.5.1.26     
Accepted name: N4-(β-N-acetylglucosaminyl)-L-asparaginase
Reaction: N4-(β-N-acetyl-D-glucosaminyl)-L-asparagine + H2O = N-acetyl-β-D-glucosaminylamine + L-aspartate
Other name(s): aspartylglucosylamine deaspartylase; aspartylglucosylaminase; aspartylglucosaminidase; aspartylglycosylamine amidohydrolase; N-aspartyl-β-glucosaminidase; glucosylamidase; β-aspartylglucosylamine amidohydrolase; 4-N-(β-N-acetyl-D-glucosaminyl)-L-asparagine amidohydrolase
Systematic name: N4-(β-N-acetyl-D-glucosaminyl)-L-asparagine amidohydrolase
Comments: Acts only on asparagine-oligosaccharides containing one amino acid, i.e., the asparagine has free α-amino and α-carboxyl groups [cf. EC 3.5.1.52, peptide-N4-(N-acetyl-β-glucosaminyl)asparagine amidase]
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 9075-24-5
References:
1.  Kohno, M. and Yamashina, I. Purification and properties of 4-L-aspartylglycosylamine amidohydrolase from hog kidney. Biochim. Biophys. Acta 258 (1972) 600–617. [DOI] [PMID: 5010303]
2.  Mahadevan, S. and Tappel, A.L. β-Aspartylglucosylamine amido hydrolase of rat liver and kidney. J. Biol. Chem. 242 (1967) 4568–4576. [PMID: 6061403]
3.  Tarentino, A.L. and Maley, F. The purification and properties of a β-aspartyl N-acetylglucosylamine amidohydrolase from hen oviduct. Arch. Biochem. Biophys. 130 (1969) 295–303. [PMID: 5778645]
[EC 3.5.1.26 created 1972 (EC 3.5.1.37 created 1972, incorporated 1976)]
 
 
EC 3.5.1.27      
Deleted entry: N-formylmethionylaminoacyl-tRNA deformylase. The activity is covered by EC 3.5.1.88, peptide deformylase
[EC 3.5.1.27 created 1972, deleted 2014]
 
 
EC 3.5.1.28     
Accepted name: N-acetylmuramoyl-L-alanine amidase
Reaction: Hydrolyses the link between N-acetylmuramoyl residues and L-amino acid residues in certain cell-wall glycopeptides
Glossary: thiamine diphosphate = 3-[(4-amino-2-methylpyrimidin-5-yl)methyl]-5-(2-diphosphoethyl)-4-methyl-1,3-thiazolium
Other name(s): 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; murein hydrolase; N-acetylmuramoyl-L-alanine amidase type I; N-acetylmuramoyl-L-alanine amidase type II
Systematic name: peptidoglycan amidohydrolase
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 9013-25-6
References:
1.  Ghuysen, J.-M., Dierickx, L., Coyette, J., Leyh-Bouille, M., Guinand, M. and Campbell, J.N. An improved technique for the preparation of Streptomyces peptidases and N-acetylmuramyl-L-alanine amidase active on bacterial wall peptidoglycans. Biochemistry 8 (1969) 213–222. [PMID: 5777325]
2.  Herbold, D.R. and Glaser, L. Interaction of N-acetylmuramic acid L-alanine amidase with cell wall polymers. J Biol Chem 250 (1975) 7231–7238. [PMID: 809432]
3.  Herbold, D.R. and Glaser, L. Bacillus subtilis N-acetylmuramic acid L-alanine amidase. J. Biol. Chem. 250 (1975) 1676–1682. [PMID: 803507]
4.  Ward, J.B., Curtis, C.A.M., Taylor, C. and Buxton, R.S. Purification and characterization of two phage PBSX-induced lytic enzymes of Bacillus subtilis 168: an N-acetylmuramoyl-L-alanine amidase and an N-acetylmuramidase. J. Gen. Microbiol. 128 (1982) 1171–1178. [DOI] [PMID: 6126517]
[EC 3.5.1.28 created 1972 (EC 3.4.19.10 created 1992, incorporated 1997)]
 
 
EC 3.5.1.29     
Accepted name: 2-(acetamidomethylene)succinate hydrolase
Reaction: 2-(acetamidomethylene)succinate + 2 H2O = acetate + succinate semialdehyde + NH3 + CO2
Other name(s): α-(N-acetylaminomethylene)succinic acid hydrolase
Systematic name: 2-(acetamidomethylene)succinate amidohydrolase (deaminating, decarboxylating)
Comments: Involved in the degradation of pyridoxin in Pseudomonas.
Links to other databases: BRENDA, EAWAG-BBD, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 37289-09-1
References:
1.  Huynh, M.S. and Snell, E.E. Enzymes of vitamin B6 degradation. Purification and properties of two N-acetylamidohydrolases. J. Biol. Chem. 260 (1985) 2379–2383. [PMID: 3972793]
2.  Nyns, E.J., Zach, D. and Snell, E.E. The bacterial oxidation of vitamin B6. 8. Enzymatic breakdown of α-(N-acetylaminomethylene) succinic acid. J. Biol. Chem. 244 (1969) 2601–2605. [PMID: 5769993]
[EC 3.5.1.29 created 1972]
 
 
EC 3.5.1.30     
Accepted name: 5-aminopentanamidase
Reaction: 5-aminopentanamide + H2O = 5-aminopentanoate + NH3
Other name(s): 5-aminovaleramidase; 5-aminonorvaleramidase
Systematic name: 5-aminopentanamide amidohydrolase
Comments: The enzyme from Pseudomonas putida also acts on 4-aminobutanamide and, more slowly, on 6-aminohexanamide.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 9054-60-8
References:
1.  Reitz, M.S. and Rodwell, V.W. δ-Aminovaleramidase of Pseudomonas putida. J. Biol. Chem. 245 (1970) 3091–3096. [PMID: 5432799]
2.  Takeda, H., Yamamoto, S., Kojima, Y. and Hayaishi, O. Studies on monooxygenases. I. General properties of crystalline L-lysine monooxygenase. J. Biol. Chem. 244 (1969) 2935–2941. [PMID: 5772467]
[EC 3.5.1.30 created 1972, modified 1976]
 
 
EC 3.5.1.31     
Accepted name: formylmethionine deformylase
Reaction: N-formyl-L-methionine + H2O = formate + L-methionine
Systematic name: N-formyl-L-methionine amidohydrolase
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 9032-86-4
References:
1.  Aronson, J.N. and Lugay, J.C. N-Formylmethionine deformylase from Euglena gracilis. Biochem. Biophys. Res. Commun. 34 (1969) 311–314. [DOI] [PMID: 5767026]
[EC 3.5.1.31 created 1972]
 
 
EC 3.5.1.32     
Accepted name: hippurate hydrolase
Reaction: hippurate + H2O = benzoate + glycine
Glossary: hippurate = N-benzoylglycine
Systematic name: N-benzoylamino-acid amidohydrolase
Comments: Acts on various N-benzoylamino acids.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 37278-43-6
References:
1.  Röhr, M. Hippurathydrolase, ein neues Enzym aus Mikroorganismen. I Mitt. Induzierte Biosynthese in Fusarium semitectum. Darstellung einer gereinigten Enzympraparation und Untersuchungen zur Substratspezifitat. Monatchefte Chem. 99 (1968) 2255–2277.
2.  Röhr, M. Hippurathydrolase, ein neues Enzym aus Mikroorganismen. II Mitt. Enzymeigenschaften. Monatchefte Chem. 99 (1968) 2278–2290.
[EC 3.5.1.32 created 1972]
 
 
EC 3.5.1.33     
Accepted name: N-acetylglucosamine deacetylase
Reaction: N-acetyl-D-glucosamine + H2O = D-glucosamine + acetate
Other name(s): acetylaminodeoxyglucose acetylhydrolase; N-acetyl-D-glucosaminyl N-deacetylase
Systematic name: N-acetyl-D-glucosamine amidohydrolase
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 9012-32-2
References:
1.  Roseman, S. Glucosamine metabolism. I. N-Acetylglucosamine deacetylase. J. Biol. Chem. 226 (1957) 115–123. [PMID: 13428742]
[EC 3.5.1.33 created 1972]
 
 
EC 3.5.1.34      
Deleted entry:  acetylhistidine deacetylase. Identical with EC 3.4.13.5, Xaa-methyl-His dipeptidase
[EC 3.5.1.34 created 1972, deleted 1981]
 
 
EC 3.5.1.35     
Accepted name: D-glutaminase
Reaction: D-glutamine + H2O = D-glutamate + NH3
Systematic name: D-glutamine amidohydrolase
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 37289-12-6
References:
1.  Domnas, A. and Catimo, E.C. The behavior of amidohydrolases and L-glutamate in synchronized populations of Blastocladiella emeronii. Phytochemistry 4 (1965) 273–284.
[EC 3.5.1.35 created 1972]
 
 
EC 3.5.1.36     
Accepted name: N-methyl-2-oxoglutaramate hydrolase
Reaction: N-methyl-2-oxoglutaramate + H2O = 2-oxoglutarate + methylamine
Other name(s): 5-hydroxy-N-methylpyroglutamate synthase
Systematic name: N-methyl-2-oxoglutaramate methylamidohydrolase
Comments: In the reverse reaction, the product cyclizes non-enzymically to 2-hydroxy-N-methyl-5-oxo-L-proline.
Links to other databases: BRENDA, EXPASY, GTD, KEGG, MetaCyc, CAS registry number: 9073-53-4
References:
1.  Hersh, L.B. 5-Hydroxy-N-methylpyroglutamate synthetase. Purification and mechanism of action. J. Biol. Chem. 245 (1970) 3526–3535. [PMID: 5470822]
2.  Hersh, L.B., Tsai, L. and Stadtman, E.R. The enzymatic synthesis of 5-hydroxy-N-methylpyroglutamic acid. J. Biol. Chem. 244 (1969) 4677–4683. [PMID: 5808511]
[EC 3.5.1.36 created 1972]
 
 
EC 3.5.1.37      
Deleted entry:  4-L-aspartylglycosylamine amidohydrolase. Identical with EC 3.5.1.26 N4-(β-N-acetylglucosaminyl)-L-asparaginase
[EC 3.5.1.37 created 1972, deleted 1976]
 
 
EC 3.5.1.38     
Accepted name: glutamin-(asparagin-)ase
Reaction: (1) L-glutamine + H2O = L-glutamate + NH3
(2) L-asparagine + H2O = L-aspartate + NH3
Other name(s): glutaminase-asparaginase; ansB (gene name); L-asparagine/L-glutamine amidohydrolase; L-ASNase/L-GLNase
Systematic name: L-glutamine(L-asparagine) amidohydrolase
Comments: The enzyme from the bacterium Achromobacter hydrolyses L-asparagine at 0.8 of the rate of L-glutamine; the D-isomers are also hydrolysed, but more slowly. cf. EC 3.5.1.2, glutaminase and EC 3.5.1.1, asparaginase.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 39335-03-0
References:
1.  Roberts, J., Holcenberg, J.S. and Dolowy, W.C. Isolation, crystallization, and properties of Achromobacteraceae glutaminase-asparaginase with antitumor activity. J. Biol. Chem. 247 (1972) 84–90. [PMID: 5017769]
2.  Tanaka, S., Robinson, E.A., Appella, E., Miller, M., Ammon, H.L., Roberts, J., Weber, I.T. and Wlodawer, A. Structures of amidohydrolases. Amino acid sequence of a glutaminase-asparaginase from Acinetobacter glutaminasificans and preliminary crystallographic data for an asparaginase from Erwinia chrysanthemi. J. Biol. Chem. 263 (1988) 8583–8591. [PMID: 3379033]
3.  Lubkowski, J., Wlodawer, A., Ammon, H.L., Copeland, T.D. and Swain, A.L. Structural characterization of Pseudomonas 7A glutaminase-asparaginase. Biochemistry 33 (1994) 10257–10265. [PMID: 8068664]
4.  Ortlund, E., Lacount, M.W., Lewinski, K. and Lebioda, L. Reactions of Pseudomonas 7A glutaminase-asparaginase with diazo analogues of glutamine and asparagine result in unexpected covalent inhibitions and suggests an unusual catalytic triad Thr-Tyr-Glu. Biochemistry 39 (2000) 1199–1204. [DOI] [PMID: 10684596]
[EC 3.5.1.38 created 1976]
 
 
EC 3.5.1.39     
Accepted name: alkylamidase
Reaction: N-methylhexanamide + H2O = hexanoate + methylamine
Systematic name: N-methylhexanamide amidohydrolase
Comments: The enzyme hydrolyses N-monosubstituted and N,N-disubstituted amides, and there is some activity towards primary amides. It has little or no activity towards short-chain substrates.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 62213-19-8
References:
1.  Chen, P.R.S. and Dauterman, W.C. Alkylamidase of sheep liver. Biochim. Biophys. Acta 250 (1971) 216–223. [DOI] [PMID: 5141674]
[EC 3.5.1.39 created 1976]
 
 
EC 3.5.1.40     
Accepted name: acylagmatine amidase
Reaction: benzoylagmatine + H2O = benzoate + agmatine
Glossary: agmatine = (4-aminobutyl)guanidine
Other name(s): acylagmatine amidohydrolase; acylagmatine deacylase
Systematic name: benzoylagmatine amidohydrolase
Comments: Also acts on acetylagmatine, propanoylagmatine and bleomycin B2
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 39419-74-4
References:
1.  Umezawa, H., Takahashi, Y., Fujii, A., Saino, T., Shirai, T. and Takita, T. Preparation of bleomycinic acid. Hydrolysis of bleomycin B2 by a Fusarium acylagmatine amidohydrolase. J. Antibiot. 26 (1974) 117–119. [PMID: 4131159]
[EC 3.5.1.40 created 1976]
 
 
EC 3.5.1.41     
Accepted name: chitin deacetylase
Reaction: chitin + H2O = chitosan + acetate
Systematic name: chitin amidohydrolase
Comments: Hydrolyses the N-acetamido groups of N-acetyl-D-glucosamine residues in chitin.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 56379-60-3
References:
1.  Araki, Y. and Ito, E. A pathway of chitosan formation in Mucor rouxii: enzymatic deacetylation of chitin. Biochem. Biophys. Res. Commun. 56 (1974) 669–675. [DOI] [PMID: 4826874]
[EC 3.5.1.41 created 1976]
 
 
EC 3.5.1.42     
Accepted name: nicotinamide-nucleotide amidase
Reaction: β-nicotinamide D-ribonucleotide + H2O = β-nicotinate D-ribonucleotide + NH3
Other name(s): NMN deamidase; nicotinamide mononucleotide deamidase; nicotinamide mononucleotide amidohydrolase
Systematic name: nicotinamide-D-ribonucleotide amidohydrolase
Comments: Also acts more slowly on β-nicotinamide D-ribonucleoside.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 37355-58-1
References:
1.  Imai, T. Purification and properties of nicotinamide mononucleotide amidohydrolase from Azotobacter vinelandii. J. Biochem. (Tokyo) 73 (1973) 139–153. [PMID: 4144084]
[EC 3.5.1.42 created 1976]
 
 
EC 3.5.1.43     
Accepted name: peptidyl-glutaminase
Reaction: α-N-peptidyl-L-glutamine + H2O = α-N-peptidyl-L-glutamate + NH3
Other name(s): peptidoglutaminase I; peptideglutaminase; peptidoglutaminase
Systematic name: peptidyl-L-glutamine amidohydrolase
Comments: Specific for the hydrolysis of the γ-amide of glutamine substituted at the α-amino group, e.g., glycyl-L-glutamine, N-acetyl-L-glutamine and L-leucylglycyl-L-glutamine.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 37228-70-9
References:
1.  Kikuchi, M., Hayashida, H., Nakano, E. and Sakaguchi, K. Peptidoglutaminase. Enzymes for selective deamidation of γ-amide of peptide-bound glutamine. Biochemistry 10 (1971) 1222–1229. [PMID: 4928623]
[EC 3.5.1.43 created 1976]
 
 
EC 3.5.1.44     
Accepted name: protein-glutamine glutaminase
Reaction: protein L-glutamine + H2O = protein L-glutamate + NH3
Other name(s): peptidoglutaminase II; glutaminyl-peptide glutaminase; destabilase; peptidylglutaminase II
Systematic name: protein-L-glutamine amidohydrolase
Comments: Specific for the hydrolysis of the γ-amide of glutamine substituted at the carboxyl position or both the α-amino and carboxyl positions, e.g., L-glutaminylglycine and L-phenylalanyl-L-glutaminylglycine.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 62213-11-0
References:
1.  Kikuchi, M., Hayashida, H., Nakano, E. and Sakaguchi, K. Peptidoglutaminase. Enzymes for selective deamidation of γ-amide of peptide-bound glutamine. Biochemistry 10 (1971) 1222–1229. [PMID: 4928623]
[EC 3.5.1.44 created 1976, modified 1983]
 
 
EC 3.5.1.45      
Deleted entry:  urease (ATP-hydrolysing). Now listed only as EC 6.3.4.6 urea carboxylase
[EC 3.5.1.45 created 1978, deleted 1986]
 
 
EC 3.5.1.46     
Accepted name: 6-aminohexanoate-oligomer exohydrolase
Reaction: (1) [N-(6-aminohexanoyl)]n + H2O = [N-(6-aminohexanoyl)]n-1 + 6-aminohexanoate
(2) N-(6-aminohexanoyl)-6-aminohexanoate + H2O = 2 6-aminohexanoate
Other name(s): 6-aminohexanoate-dimer hydrolase; nylB (gene name); 6-aminohexanoic acid oligomer hydrolase (ambiguous); N-(6-aminohexanoyl)-6-aminohexanoate amidohydrolase; nylon-6 hydrolase (ambiguous)
Systematic name: N-(6-aminohexanoyl)-6-aminohexanoate exoamidohydrolase
Comments: The enzyme is involved in degradation of nylon-6 oligomers. It degrades linear oligomers of 6-aminohexanoate with a degree of polymerization of 2–20 by exo-type cleavage, removing residues sequentially from the N-terminus. Activity decreases with the increase of the polymerization number of the oligomer. cf. EC 3.5.1.117, 6-aminohexanoate-oligomer endohydrolase and EC 3.5.2.12, 6-aminohexanoate-cyclic-dimer hydrolase.
Links to other databases: BRENDA, EAWAG-BBD, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 75216-15-8
References:
1.  Kinoshita, S., Terada, T., Taniguchi, T., Takeney, Y., Masuda, S., Matsunaga, N. and Okada, H. Purification and characterization of 6-aminohexanoic-acid-oligomer hydrolase of Flavobacterium sp. KI72. Eur. J. Biochem. 116 (1981) 547–551. [DOI] [PMID: 7262074]
[EC 3.5.1.46 created 1983, modified 2014]
 
 
EC 3.5.1.47     
Accepted name: N-acetyldiaminopimelate deacetylase
Reaction: N-acetyl-LL-2,6-diaminoheptanedioate + H2O = acetate + LL-2,6-diaminoheptanedioate
Other name(s): N-acetyl-L-diaminopimelic acid deacylase; N-acetyl-LL-diaminopimelate deacylase; 6-N-acetyl-LL-2,6-diaminoheptanedioate amidohydrolase
Systematic name: N6-acetyl-LL-2,6-diaminoheptanedioate amidohydrolase
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 99193-93-8
References:
1.  Bartlett, A.T.M. and White, P.J. Species of Bacillus that make a vegetative peptidoglycan containing lysine lack diaminopimelate epimerase but have diaminopimelate dehydrogenase. J. Gen. Microbiol. 131 (1985) 2145–2152.
2.  Saleh, F. and White, P.J. Metabolism of DD-2,6-diaminopimelic acid by a diaminopimelate-requiring mutant of Bacillus megaterium. J. Gen. Microbiol. 115 (1979) 95–100.
3.  Sundharadas, G. and Gilvarg, C. Biosynthesis of α,ε-diaminopimelic acid in Bacillus megaterium. J. Biol. Chem. 242 (1967) 3983–3984. [PMID: 4962540]
[EC 3.5.1.47 created 1984 (EC 3.1.1.62 created 1989, incorporated 1992)]
 
 
EC 3.5.1.48     
Accepted name: acetylspermidine deacetylase
Reaction: N8-acetylspermidine + H2O = acetate + spermidine
Glossary: spermidine = N-(3-aminopropyl)butane-1,4-diamine
spermine = N,N′-bis(3-aminopropyl)butane-1,4-diamine
Other name(s): N8-monoacetylspermidine deacetylase; N8-acetylspermidine deacetylase; N-acetylspermidine deacetylase; N1-acetylspermidine amidohydrolase (incorrect); 8-N-acetylspermidine amidohydrolase
Systematic name: N8-acetylspermidine amidohydrolase
Comments: It was initially thought that N1-acetylspermidine was the substrate for this deacetylase reaction [1] but this has since been disproved by Marchant et al. [3].
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 67339-07-5
References:
1.  Libby, P.R. Properties of an acetylspermidine deacetylase from rat liver. Arch. Biochem. Biophys. 188 (1978) 360–363. [DOI] [PMID: 28089]
2.  Blankenship, J. Deacetylation of N8-acetylspermidine by subcellular fractions of rat tissue. Arch. Biochem. Biophys. 189 (1978) 20–27. [DOI] [PMID: 708044]
3.  Marchant, P., Manneh, V.A. and Blankenship, J. N1-Acetylspermidine is not a substrate for N-acetylspermidine deacetylase. Biochim. Biophys. Acta 881 (1986) 297–299. [DOI] [PMID: 3955076]
[EC 3.5.1.48 created 1984, modified 2005]
 
 
EC 3.5.1.49     
Accepted name: formamidase
Reaction: formamide + H2O = formate + NH3
Systematic name: formamide amidohydrolase
Comments: Also acts, more slowly, on acetamide, propanamide and butanamide.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 9013-59-6
References:
1.  Clarke, P.H. The aliphatic amidases of Pseudomonas aeruginosa. Adv. Microb. Physiol. 4 (1970) 179–222.
2.  Friedich, C.G. and Mitrenga, G. Utilization of aliphatic amides and formation of two different amidases by Alcaligenes eutrophus. J. Gen. Microbiol. 125 (1981) 367–374.
[EC 3.5.1.49 created 1984]
 
 
EC 3.5.1.50     
Accepted name: pentanamidase
Reaction: pentanamide + H2O = pentanoate + NH3
Other name(s): valeramidase
Systematic name: pentanamide amidohydrolase
Comments: Also acts, more slowly, on other short-chain aliphatic amides. Different from EC 3.5.1.49 formamidase.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 81032-50-0
References:
1.  Friedich, C.G. and Mitrenga, G. Utilization of aliphatic amides and formation of two different amidases by Alcaligenes eutrophus. J. Gen. Microbiol. 125 (1981) 367–374.
[EC 3.5.1.50 created 1984]
 
 


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