MetaCyc Reaction:

Superclasses: Reactions Classified By Conversion Type Simple Reactions Chemical Reactions
Reactions Classified By Substrate Small-Molecule Reactions

EC Number:

Enzymes and Genes:

Agrobacterium tumefaciens : arginase Inferred from experiment : arcA
Arabidopsis thaliana col : arginase Inferred from experiment : arginase
Bacillus subtilis : arginase Inferred from experiment : rocF
Homo sapiens : arginase 1 Inferred from experiment : ARG1
arginase 2 Inferred from experiment : ARG2
Saccharomyces cerevisiae : arginase Inferred from experiment : CAR1
Solanum lycopersicum : arginase Inferred from experiment : ARG1
arginase Inferred from experiment : ARG2

In Pathway: urea cycle , L-arginine degradation VI (arginase 2 pathway) , L-arginine degradation VII (arginase 3 pathway) , putrescine biosynthesis IV , L-arginine degradation I (arginase pathway) , L-Nδ-acetylornithine biosynthesis , L-citrulline biosynthesis

The reaction direction shown, that is, A + B ↔ C + D versus C + D ↔ A + B, is in accordance with the Enzyme Commission system.

Mass balance status: Balanced.

Enzyme Commission Primary Name: arginase

Enzyme Commission Synonyms: arginine amidinase, canavanase, L-arginase, arginine transamidinase

Standard Gibbs Free Energy (ΔrG in kcal/mol): -3.572998 Inferred by computational analysis [Latendresse13]

Enzyme Commission Summary:
Also hydrolyses α-N-substituted L-arginines and canavanine.

Citations: [Bach61, Cabello61, Dumitru73, Greenberg56, Greenberg60]

Gene-Reaction Schematic: ?

Gene-Reaction Schematic

Unification Links: KEGG:R00551 , Rhea:20569

Relationship Links: BRENDA:EC: , ENZYME:EC: , IUBMB-ExplorEnz:EC: , UniProt:RELATED-TO:O49046 , UniProt:RELATED-TO:O68051 , UniProt:RELATED-TO:O76895 , UniProt:RELATED-TO:P00812 , UniProt:RELATED-TO:P05089 , UniProt:RELATED-TO:P07824 , UniProt:RELATED-TO:P14012 , UniProt:RELATED-TO:P33280 , UniProt:RELATED-TO:P37818 , UniProt:RELATED-TO:P39138 , UniProt:RELATED-TO:P40906 , UniProt:RELATED-TO:P49900 , UniProt:RELATED-TO:P53608 , UniProt:RELATED-TO:P72703 , UniProt:RELATED-TO:Q7M0Z3 , UniProt:RELATED-TO:Q10066


Bach61: Bach SJ, Killip JD (1961). "Studies on the purification and the kinetic properties of arginase from beef, sheep and horse liver." Biochim Biophys Acta 47;336-43. PMID: 13685626

Cabello61: Cabello J, Basilio C, Prajoux V (1961). "Kinetic properties of erythrocyte- and liver arginase." Biochim Biophys Acta 48;148-52. PMID: 13689647

Dumitru73: Dumitru IF (1973). "Study of L-arginine amidinohydrolase from vegetable origin. Purification, crystallization and molecular weight." Acta Vitaminol Enzymol 27(5);207-10. PMID: 4801830

Greenberg56: Greenberg DM, Bagot AE, Roholt OA (1956). "Liver arginase. III. Properties of highly purified arginase." Arch Biochem Biophys 62(2);446-53. PMID: 13328133

Greenberg60: Greenberg, D.M (1960). "Arginase." The Enzymes, 2nd edn, vol. 4, Academic Press, New York.

Latendresse13: Latendresse M. (2013). "Computing Gibbs Free Energy of Compounds and Reactions in MetaCyc."

Report Errors or Provide Feedback
Please cite the following article in publications resulting from the use of MetaCyc: Caspi et al, Nucleic Acids Research 42:D459-D471 2014
Page generated by SRI International Pathway Tools version 19.0 on Wed Oct 7, 2015, biocyc13.