EC 3.5.3.1 - Arginase

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IntEnz Enzyme Nomenclature
EC 3.5.3.1

Names

Accepted name:
arginase
Other names:
L-arginase
arginine amidinase
arginine transamidinase
canavanase
Systematic name:
L-arginine amidinohydrolase

Reaction

Cofactor

Comments:

Also hydrolyses α-N-substituted L-arginines and canavanine.

Links to other databases

Enzymes and pathways: NC-IUBMB , BRENDA , DIAGRAM , ExplorEnz , ENZYME@ExPASy , KEGG , MetaCyc , NIST 74 , UniPathway
Protein domains and families: PROSITE:PDOC00135
Structural data: CSA , EC2PDB
Gene Ontology: GO:0004053
CAS Registry Number: 9000-96-8
UniProtKB/Swiss-Prot: (47) [show] [UniProt]

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 : 336-343 (1961).
  2. Cabello, J., Basilio, C. and Prajoux, V.
    Kinetic properties of erythrocyte- and liver arginase.
    Biochim. Biophys. Acta 48 : 148-152 (1961).
  3. Dumitru, I.F.
    Study of L-arginine amidinohydrolase from vegetable origin. Purification, crystallization and molecular weight.
    Acta Vitamin. Enzymol. 27 : 207-210 (1973).
  4. Greenberg, D.M.
    Arginase
    In: Boyer, P.D., Lardy, H. and Myrbäck, K. (Eds.) The Enzymes , 2nd ed. vol. 4 , Academic Press , New York , 1960 , 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 : 446-453 (1956).

[EC 3.5.3.1 created 1961]