EC |
3.5.3.1 |
Accepted name: |
arginase |
Reaction: |
L-arginine + H2O = L-ornithine + urea |
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For diagram of the urea cycle and arginine biosynthesis, click here |
Other name(s): |
arginine amidinase; canavanase; L-arginase; arginine transamidinase |
Systematic name: |
L-arginine amidinohydrolase |
Comments: |
Also hydrolyses α-N-substituted L-arginines and canavanine. |
Links to other databases: |
BRENDA, EXPASY, GTD, KEGG, MetaCyc, PDB, CAS registry number: 9000-96-8 |
References: |
1. |
Bach, S.J. and Killip, J.D. Studies on the purification and the kinetic properties of arginase from beef, sheep and horse liver. Biochim. Biophys. Acta 47 (1961) 336–343. [DOI] [PMID: 13685626] |
2. |
Cabello, J., Basilio, C. and Prajoux, V. Kinetic properties of erythrocyte- and liver arginase. Biochim. Biophys. Acta 48 (1961) 148–152. [DOI] [PMID: 13689647] |
3. |
Dumitru, I.F. Study of L-arginine amidinohydrolase from vegetable origin. Purification, crystallization and molecular weight. Acta Vitamin. Enzymol. 27 (1973) 207–210. [PMID: 4801830] |
4. |
Greenberg, D.M. Arginase. In: Boyer, P.D., Lardy, H. and Myrbäck, K. (Ed.), The Enzymes, 2nd edn, vol. 4, Academic Press, New York, 1960, pp. 257–267. |
5. |
Greenberg, D.M., Bagot, A.E. and Roholt, O.A. Liver arginase. III. Properties of highly purified arginase. Arch. Biochem. Biophys. 62 (1956) 446–453. [DOI] [PMID: 13328133] |
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[EC 3.5.3.1 created 1961] |
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EC |
3.5.3.10 |
Accepted name: |
D-arginase |
Reaction: |
D-arginine + H2O = D-ornithine + urea |
Systematic name: |
D-arginine amidinohydrolase |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 37289-14-8 |
References: |
1. |
Nadai, Y. Arginase. II. Distribution and properties of D-arginase. J. Biochem. (Tokyo) 45 (1958) 1011–1020. |
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[EC 3.5.3.10 created 1972] |
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EC |
3.5.3.11 |
Accepted name: |
agmatinase |
Reaction: |
agmatine + H2O = putrescine + urea |
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For diagram of arginine catabolism, click here |
Glossary: |
agmatine = (4-aminobutyl)guanidine
putrescine = butane-1,4-diamine |
Other name(s): |
agmatine ureohydrolase; SpeB |
Systematic name: |
agmatine amidinohydrolase |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 37289-16-0 |
References: |
1. |
Hirshfeld, I.N., Rosenfeld, H.J., Leifer, Z. and Maas, W.K. Isolation and characterization of a mutant of Escherichia coli blocked in the synthesis of putrescine. J. Bacteriol. 101 (1970) 725–730. [PMID: 4908780] |
2. |
Vicente, C. and Legaz, M.E. Preparation and properties of agmatine amidinohydrolase of Evernia prunastri. Physiol. Plant. 55 (1982) 335–339. |
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[EC 3.5.3.11 created 1972] |
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EC |
3.5.3.12 |
Accepted name: |
agmatine deiminase |
Reaction: |
agmatine + H2O = N-carbamoylputrescine + NH3 |
Glossary: |
agmatine = (4-aminobutyl)guanidine |
Other name(s): |
agmatine amidinohydrolase |
Systematic name: |
agmatine iminohydrolase |
Comments: |
The plant enzyme also catalyses the reactions of EC 2.1.3.3 (ornithine carbamoyltransferase), EC 2.1.3.6 (putrescine carbamoyltransferase) and EC 2.7.2.2 (carbamate kinase), thus functioning as a putrescine synthase, converting agmatine and ornithine into putrescine and citrulline, respectively. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 37289-17-1 |
References: |
1. |
Smith, T.A. Agmatine iminohydrolase in maize. Phytochemistry 8 (1969) 2111–2117. |
2. |
Srivenugopal, K.S. and Adiga, P.R. Enzymic conversion of agmatine to putrescine in Lathyrus sativus seedlings. Purification and properties of a multifunctional enzyme (putrescine synthase). J. Biol. Chem. 256 (1981) 9532–9541. [PMID: 6895223] |
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[EC 3.5.3.12 created 1972] |
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EC |
3.5.3.13 |
Accepted name: |
formimidoylglutamate deiminase |
Reaction: |
N-formimidoyl-L-glutamate + H2O = N-formyl-L-glutamate + NH3 |
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Other name(s): |
formiminoglutamate deiminase; formiminoglutamic iminohydrolase |
Systematic name: |
N-formimidoyl-L-glutamate iminohydrolase |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 9054-85-7 |
References: |
1. |
Wickner, R.B. and Tabor, H. N-Formimino-L-glutamate iminohydrolase (Pseudomonas sp.). Methods Enzymol. 17B (1971) 80–84. |
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[EC 3.5.3.13 created 1975, modified 2000] |
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EC |
3.5.3.14 |
Accepted name: |
amidinoaspartase |
Reaction: |
N-amidino-L-aspartate + H2O = L-aspartate + urea |
Other name(s): |
amidinoaspartic amidinohydrolase |
Systematic name: |
N-amidino-L-aspartate amidinohydrolase |
Comments: |
Also acts slowly on N-amidino-L-glutamate. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 37325-60-3 |
References: |
1. |
Milstien, S. and Goldman, P. Metabolism of guanidinosuccinic acid. I. Characterization of a specific amidino hydrolase from Pseudomonas chlororaphis. J. Biol. Chem. 247 (1972) 6280–6283. [PMID: 4651648] |
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[EC 3.5.3.14 created 1976] |
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EC |
3.5.3.15 |
Accepted name: |
protein-arginine deiminase |
Reaction: |
protein L-arginine + H2O = protein L-citrulline + NH3 |
Other name(s): |
peptidylarginine deiminase; PAD |
Systematic name: |
protein-L-arginine iminohydrolase |
Comments: |
Also acts on N-acyl-L-arginine and, more slowly, on L-arginine esters. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 75536-80-0 |
References: |
1. |
Fujisaki, M. and Sugawara, K. Properties of peptidylarginine deiminase from the epidermis of newborn rats. J. Biochem. (Tokyo) 89 (1981) 257–263. [PMID: 7217033] |
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[EC 3.5.3.15 created 1983] |
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EC |
3.5.3.16 |
Accepted name: |
methylguanidinase |
Reaction: |
methylguanidine + H2O = methylamine + urea |
Other name(s): |
methylguanidine hydrolase |
Systematic name: |
methylguanidine amidinohydrolase |
Comments: |
Acts on some other alkylguanidines, but very slowly. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 73200-93-8 |
References: |
1. |
Nakajima, M., Shirokane, Y. and Mizusawa, K. A new amidinohydrolase, methylguanidine amidinohydrolase from Alcaligenes sp. N-42. FEBS Lett. 110 (1980) 43–46. [DOI] [PMID: 7353662] |
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[EC 3.5.3.16 created 1984] |
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EC |
3.5.3.17 |
Accepted name: |
guanidinopropionase |
Reaction: |
3-guanidinopropanoate + H2O = β-alanine + urea |
Other name(s): |
GPase; GPH |
Systematic name: |
3-guanidinopropanoate amidinopropionase |
Comments: |
Requires Mn2+. Also acts, more slowly, on taurocyamine and 4-guanidinobutanoate. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 68821-77-2 |
References: |
1. |
Yorifuji, T., Sugai, I., Matsumoto, H. and Tabuchi, A. Characterization of 3-guanidinopropionate amidinohydrolase from Pseudomonas aeruginosa and a comparative study with 4-guanidinobutyrate amidinohydrolase from another Pseudomonas. Agric. Biol. Chem. 46 (1982) 1361–1363. |
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[EC 3.5.3.17 created 1989] |
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EC |
3.5.3.18 |
Accepted name: |
dimethylargininase |
Reaction: |
Nω,Nω′-dimethyl-L-arginine + H2O = dimethylamine + L-citrulline |
Other name(s): |
dimethylarginine dimethylaminohydrolase; NG,NG-dimethylarginine dimethylaminohydrolase; NG,NG-dimethyl-L-arginine dimethylamidohydrolase; ω,ω’-di-N-methyl-L-arginine dimethylamidohydrolase; Nω,Nω′-methyl-L-arginine dimethylamidohydrolase (incorrect) |
Systematic name: |
Nω,Nω′-dimethyl-L-arginine dimethylamidohydrolase |
Comments: |
Also acts on Nω-methyl-L-arginine. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 123644-75-7 |
References: |
1. |
Ogawa, T., Kimoto, M. and Sasaoka, K. Purification and properties of a new enzyme, NG,NG-dimethylarginine dimethylaminohydrolase, from rat kidney. J. Biol. Chem. 264 (1989) 10205–10209. [PMID: 2722865] |
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[EC 3.5.3.18 created 1992] |
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EC
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3.5.3.19
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Transferred entry: | ureidoglycolate hydrolase. Now EC 3.5.1.116, ureidoglycolate amidohydrolase
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[EC 3.5.3.19 created 1992, deleted 2014] |
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