Continued from EC 3.4.99
EC 3.5.1 In Linear Amides
EC 3.5.2 In Cyclic Amides
EC 3.5.3 In Linear Amidines
EC 3.5.4 In Cyclic Amidines
EC 3.5.5 In Nitriles
EC 3.5.99 In Other Compounds
EC 3.5.1.1 asparaginase
EC 3.5.1.2 glutaminase
EC 3.5.1.3 ω-amidase
EC 3.5.1.4 amidase
EC 3.5.1.5 urease
EC 3.5.1.6 β-ureidopropionase
EC 3.5.1.7 ureidosuccinase
EC 3.5.1.8 formylaspartate deformylase
EC 3.5.1.9 arylformamidase
EC 3.5.1.10 formyltetrahydrofolate deformylase
EC 3.5.1.11 penicillin amidase
EC 3.5.1.12 biotinidase
EC 3.5.1.13 aryl-acylamidase
EC 3.5.1.14 N-acyl-aliphatic-L-amino acid amidohydrolase
EC 3.5.1.15 aspartoacylase
EC 3.5.1.16 acetylornithine deacetylase
EC 3.5.1.17 acyl-lysine deacylase
EC 3.5.1.18 succinyl-diaminopimelate desuccinylase
EC 3.5.1.19 nicotinamidase
EC 3.5.1.20 citrullinase
EC 3.5.1.21 N-acetyl-β-alanine deacetylase
EC 3.5.1.22 pantothenase
EC 3.5.1.23 ceramidase
EC 3.5.1.24 choloylglycine hydrolase
EC 3.5.1.25 N-acetylglucosamine-6-phosphate deacetylase
EC 3.5.1.26 N4-(β-N-acetylglucosaminyl)-L-asparaginase
EC 3.5.1.27 deleted, covered by EC 3.5.1.88
EC 3.5.1.28 N-acetylmuramoyl-L-alanine amidase
EC 3.5.1.29 2-(acetamidomethylene)succinate hydrolase
EC 3.5.1.30 5-aminopentanamidase
EC 3.5.1.31 formylmethionine deformylase
EC 3.5.1.32 hippurate hydrolase
EC 3.5.1.33 N-acetylglucosamine deacetylase
EC 3.5.1.34 deleted, same as EC 3.4.13.5
EC 3.5.1.35 D-glutaminase
EC 3.5.1.36 N-methyl-2-oxoglutaramate hydrolase
EC 3.5.1.37 deleted, same as EC 3.5.1.26
EC 3.5.1.38 glutamin-(asparagin-)ase
EC 3.5.1.39 alkylamidase
EC 3.5.1.40 acylagmatine amidase
EC 3.5.1.41 chitin deacetylase
EC 3.5.1.42 nicotinamide-nucleotide amidase
EC 3.5.1.43 peptidyl-glutaminase
EC 3.5.1.44 protein-glutamine glutaminase
EC 3.5.1.45 now EC 6.3.4.6
EC 3.5.1.46 6-aminohexanoate-dimer hydrolase
EC 3.5.1.47 N-acetyldiaminopimelate deacetylase
EC 3.5.1.48 acetylspermidine deacetylase
EC 3.5.1.49 formamidase
EC 3.5.1.50 pentanamidase
See the following file for:
EC 3.5.1.51 to EC 3.5.1.138
Accepted name: asparaginase
Reaction: L-asparagine + H2O = L-aspartate + NH3
Other name(s): asparaginase II; L-asparaginase; colaspase; elspar; leunase; crasnitin; α-asparaginase; crisantaspase
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.
2. Ho, P.P.K., Frank, B.H. and Burck, P.J. Crystalline L-asparaginase from Escherichia coli B. Science 165 (1969) 510-512.
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]
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. (Eds.), The Enzymes, 2nd edn., vol. 4, Academic Press, New York, 1960, pp. 285-300.
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.
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.
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]
Accepted name: urease
Reaction: urea + 2 H2O = hydrogen carbonate + 2 NH3 (overall reaction)
(1a) urea + H2O = carbamate + NH3
(1b) carbamate + H2O = hydrogen carbonate + NH3 (spontaneous)
Systematic name: urea amidohydrolase
Comments: A nickel protein. Urease catalyses the hydrolysis of urea to yield ammonia and carbamate, which spontaneously hydrolyses to form carbonic acid and a second molecule of ammonia. In aqueous solutions the products convert to ammonium and hydrogen carbonate. The enzyme is widespread and is found in many bacteria, some archaea, and many eukaryotes, including plants, some invertebrates, and numerous eukaryotic microorganisms. Urease is one of the earlier enzymes to be studied, first obtained In 1874 [1,2], and named urease in 1890 [3]. The crystallization of urease in 1926 was a significant landmark in biochemistry, showing for the first time ever that enzymes are proteins and can be crystallized [4]. In 1975 it was found that the enzyme contains nickel ions in its active site [5,6].
Links to other databases: BRENDA, EAWAG-BBD, EXPASY, GTD, KEGG, MetaCyc, PDB, CAS registry number: 9002-13-5
References:
1. Musculus, F. Sur un Papier Reactif de l’Uree. Comptes Rendus 78 (1874) 132-134.
2. Musculus, F. Sur le Ferment de l’Uree. Comptes Rendus 82 (1876) 333-336.
3. Miquel, P. Sur un Ferment Soluble de l’Uree. Comptes Rendus 111 (1890) 397-399.
4. Sumner, J.B. The isolation and crystallization of the enzyme urease. Journal of Biological Chemistry 69(2) (1926) 435-441.
5. Dixon, N.E., Gazzola, T.C., Blakeley, R.L. and Zermer, B. Jack bean urease (EC 3.5.1.5). A metalloenzyme. A simple biological role for nickel? J. Am. Chem. Soc. 97 (1975) 4131-4133. [PMID: 1159216]
6. Dixon, N.E., Gazzola, C., Blakeley, R.L. and Zerner, B. Metal ions in enzymes using ammonia or amides. Science 191 (1976) 1144-1150. [PMID: 769157]
7. Sumner, J.B. Urease. In: Sumner, J.B. and Myrbäck, K. (Ed.), The Enzymes, vol. 1, Academic Press, New York, 1951, pp. 873-892.
8. 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.
Accepted name: β-ureidopropionase
Reaction: 3-ureidopropanoate + H2O = β-alanine + CO2 + NH3
For diagram 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.
2. Caravaca, J. and Grisolia, S. Enzymatic decarbamylation of carbamyl β-alanine and carbamyl β-aminoisobutyric acid. J. Biol. Chem. 231 (1958) 357-365.
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]
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.
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.
Accepted name: arylformamidase
Reaction: N-formyl-L-kynurenine + H2O = formate + L-kynurenine
For diagram of reaction 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.
2. Jakoby, W.B. Kynurenine formamidase from Neurospora. J. Biol. Chem. 207 (1954) 657-663.
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.
Accepted name: formyltetrahydrofolate deformylase
Reaction: 10-formyltetrahydrofolate + H2O = formate + tetrahydrofolate
For diagram of reaction 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 only.
Accepted name: penicillin amidase
Reaction: penicillin + H2O = a carboxylate + 6-aminopenicillanate
For diagram 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 only.
Accepted name: biotinidase
Reaction: biocytin + H2O = biotin + L-lysine
Glossary: biocytin = ε-N-biotinyl-L-lysine
Other name(s): amidohydrolase biotinidase; biocytinase; biotin-amide amidohydrolase
Systematic name: biocytin amidohydrolase
Comments: The enzyme, found in many bacterial species as well as animals, liberates biotin from biocytin and short biotinylated peptides, but not from biotinylated proteins. It also has activity on biotin esters and biotin amides.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 9025-15-4
References:
1. Thoma, R.W. and Peterson, W.H. The enzymatic degradation of soluble bound biotin. J. Biol. Chem. 210 (1954) 569-579. [PMID: 13211594]
2. 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]
3. Pispa, J. and Koivusalo, M. Actinomycin D-sensitive increase in the biotinidase activity in mouse liver and serum after ethionine feeding. Acta Chem. Scand. 26 (1972) 2133-2135. [PMID: 5081874]
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.
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. [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. [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. [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. [PMID: 10727768]
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.
Accepted name: acetylornithine deacetylase
Reaction: N2-acetyl-L-ornithine + H2O = acetate + L-ornithine
For diagram click here.
Other name(s): acetylornithinase; N-acetylornithinase
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.
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.
Accepted name: acyl-lysine deacylase
Reaction: N6-acyl-L-lysine + H2O = a carboxylate + L-lysine
Other name(s): ε-lysine acylase
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.
Accepted name: succinyl-diaminopimelate desuccinylase
Reaction: N-succinyl-LL-2,6-diaminoheptanedioate + H2O = succinate + LL-2,6-diaminoheptanedioate
For diagram click here.
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.
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.
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.
Accepted name: citrullinase
Reaction: L-citrulline + H2O = L-ornithine + CO2 + NH3
Other name(s): citrulline ureidase; citrulline hydrolase; L-citrulline N5-carbamoyldihydrolase
Systematic name: L-citrulline N5-carbamoyldihydrolase
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, CAS registry number: 59088-17-4
References: 1996
1. Hill, D.L. and Chambers, P. The biosynthesis of proline by Tetrahymena pyriformis. Biochim. Biophys. Acta 148 (1967) 435-447. [PMID: 6075416]
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.
Accepted name: pantothenase
Reaction: (R)-pantothenate + H2O = (R)-pantoate + β-alanine
For diagram of reaction 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]
Accepted name: ceramidase
Reaction: an N-acylsphingosine + H2O = a carboxylate + sphingosine
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. [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]
Accepted name: choloylglycine hydrolase
Reaction: glycocholate + H2O = cholate + glycine
For diagram 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
Systematic name: 3α,7α,12α-trihydroxy-5β-cholan-24-oylglycine 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. [PMID: 10993]
Accepted name: N-acetylglucosamine-6-phosphate deacetylase
Reaction: N-acetyl-D-glucosamine 6-phosphate + H2O = D-glucosamine 6-phosphate + acetate
For diagram 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. [PMID: 8987551]
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
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. [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 3.5.1.27 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)]
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
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. [PMID: 6126517]
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]
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]
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. [PMID: 5767026]
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 Enzympräparation und Untersuchungen zur Substratspezifität. Monatchefte Chem. 99 (1968) 2255-2277.
2. Röhr, M. Hippurathydrolase, ein neues Enzym aus Mikroorganismen. II Mitt. Enzymeigenschaften. Monatchefte Chem. 99 (1968) 2278-2290.
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.
[EC 3.5.1.34 Deleted entry: acetylhistidine deacetylase. Identical with EC 3.4.13.5 X-methyl-His dipeptidase (EC 3.5.1.34 created 1972, deleted 1981)]
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.
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 3.5.1.37 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)]
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: L-Asparagine is hydrolysed at 0.8 of the rate of L-glutamine; the D-isomers are also hydrolysed, but more slowly.
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. [PMID: 10684596]
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. [PMID: 5141674]
Accepted name: acylagmatine amidase
Reaction: benzoylagmatine + H2O = benzoate + agmatine
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.
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. [PMID: 4826874]
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]
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]
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 3.5.1.45 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)]
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. [PMID: 7262074]
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
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]
Accepted name: acetylspermidine deacetylase
Reaction: N8-acetylspermidine + H2O = acetate + spermidine
Glossary: spermidine
spermine
Other name(s): N8-monoacetylspermidine deacetylase; N8-acetylspermidine deacetylase; N-acetylspermidine deacetylase; N1-acetylspermidine amidohydrolase (incorrect)
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. [PMID: 28089]
2. Blankenship, J. Deacetylation of N8-acetylspermidine by subcellular fractions of rat tissue. Arch. Biochem. Biophys. 189 (1978) 20-27. [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. [PMID: 3955076]
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.
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.