The Enzyme Database

Your query returned 11 entries.    printer_iconPrintable version



EC 3.5.3.1     
Accepted name: arginase
Reaction: L-arginine + H2O = L-ornithine + urea
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. (Eds), 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]
[EC 3.5.3.1 created 1961]
 
 
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.
[EC 3.5.3.10 created 1972]
 
 
EC 3.5.3.11     
Accepted name: agmatinase
Reaction: agmatine + H2O = putrescine + urea
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, 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.
[EC 3.5.3.11 created 1972]
 
 
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]
[EC 3.5.3.12 created 1972]
 
 
EC 3.5.3.13     
Accepted name: formimidoylglutamate deiminase
Reaction: N-formimidoyl-L-glutamate + H2O = N-formyl-L-glutamate + NH3
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.
[EC 3.5.3.13 created 1975, modified 2000]
 
 
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]
[EC 3.5.3.14 created 1976]
 
 
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]
[EC 3.5.3.15 created 1983]
 
 
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]
[EC 3.5.3.16 created 1984]
 
 
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, 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.
[EC 3.5.3.17 created 1989]
 
 
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]
[EC 3.5.3.18 created 1992]
 
 
EC 3.5.3.19      
Transferred entry: ureidoglycolate hydrolase. Now EC 3.5.1.116, ureidoglycolate amidohydrolase
[EC 3.5.3.19 created 1992, deleted 2014]
 
 


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