| EC |
3.4.13.18 |
| Accepted name: |
cytosol nonspecific dipeptidase |
| Reaction: |
Hydrolysis of dipeptides, preferentially hydrophobic dipeptides including prolyl amino acids |
| Other name(s): |
N2-β-alanylarginine dipeptidase; glycyl-glycine dipeptidase; glycyl-leucine dipeptidase; iminodipeptidase; peptidase A; Pro-X dipeptidase; prolinase; prolyl dipeptidase; prolylglycine dipeptidase; L-prolylglycine dipeptidase; diglycinase; Gly-Leu hydrolase; glycyl-L-leucine dipeptidase; glycyl-L-leucine hydrolase; glycyl-L-leucine peptidase; L-amino-acyl-L-amino-acid hydrolase; glycylleucine peptidase; glycylleucine hydrolase; glycylleucine dipeptide hydrolase; non-specific dipeptidase; human cytosolic non-specific dipeptidase |
| Comments: |
A zinc enzyme with broad specificity, varying somewhat with source species. Activated and stabilized by dithiothreitol and Mn2+. Inhibited by bestatin and leucine. |
| Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, MEROPS, PDB, CAS registry number: 9025-31-4 |
| References: |
| 1. |
Bauer, K. Cytosol non-specific dipeptidase. In: Barrett, A.J., Rawlings, N.D. and Woessner, J.F. (Ed.), Handbook of Proteolytic Enzymes, Academic Press, London, 1998, pp. 1520–1522. |
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| [EC 3.4.13.18 created 1961 as EC 3.4.3.1 and EC 3.4.3.2, transferred 1972 to EC 3.4.13.1 and EC 3.4.13.2, transferred 1978 to EC 3.4.13.11, part transferred 1992 to EC 3.4.13.18, modified 2000 (EC 3.4.13.15 created 1989, incorporated 1992)] |
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