Enzyme Nomenclature

Continued from EC 3.4.99

EC 3.5

Acting on Carbon-Nitrogen Bonds, other than Peptide Bonds

Sections

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 In Linear Amides

Contents

See separate file for EC 3.5.1.51 to EC 3.5.1.127.

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 3.5.1.127


Entries

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.

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]

[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. (Eds.), 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.

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.

[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, EXPASY, KEGG, Metacyc, PDB, UM-BBD, 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, EXPASY, GTD, KEGG, Metacyc, PDB, UM-BBD, 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.

2. Sumner, J.B. Urease, in Sumner, J.B. and Myrbäck, K. (Eds.), 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. (Eds.), 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 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]

[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.

[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.

[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 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.

[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 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.

[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 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.

[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.

2. Thoma, R.W. and Peterson, W.H. The enzymatic degradation of soluble bound biotin. J. Biol. Chem. 210 (1954) 569-579.

[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, EXPASY, KEGG, Metacyc, UM-BBD, 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.

[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. [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]

[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.

[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 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.

[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

Systematic name: N6-acyl-L-lysine amidohydrolase

Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, 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.

[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

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.

[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.

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 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]

[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 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]

[EC 3.5.1.22 created 1972]

EC 3.5.1.23

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]

[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 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]

[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 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]

[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

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 3.5.1.26 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

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]

[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, EXPASY, KEGG, Metacyc, UM-BBD, 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. [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 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.

[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, CAS registry number: 9012-32-2

References:

1. Roseman, S. Glucosamine metabolism. I. N-Acetylglucosamine deacetylase. J. Biol. Chem. 226 (1957) 115-123.

[EC 3.5.1.33 created 1972]

[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)]

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: 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]

[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. [PMID: 5141674]

[EC 3.5.1.39 created 1976]

EC 3.5.1.40

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.

[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. [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, EXPASY, KEGG, MetaCyc, PDB, UM-BBD, 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]

[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

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
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, 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]

[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]


Continued with EC 3.5.1.51 to EC 3.5.1.127
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