| EC |
3.4.14.2 |
| Accepted name: |
dipeptidyl-peptidase II |
| Reaction: |
Release of an N-terminal dipeptide, Xaa-Yaa┼, preferentially when Yaa is Ala or Pro. Substrates are oligopeptides, preferentially tripeptides |
| Other name(s): |
dipeptidyl aminopeptidase II; dipeptidyl arylamidase II; carboxytripeptidase; dipeptidyl peptidase II; DAP II; dipeptidyl(amino)peptidase II; dipeptidylarylamidase |
| Comments: |
A lysosomal serine-type peptidase in family S28 (Pro-X carboxypeptidase family); maximally active at acidic pH |
| Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, MEROPS, PDB, CAS registry number: 76199-23-0 |
| References: |
| 1. |
McDonald, J.K., Reilly, T.J., Zeitman, B.B. and Ellis, S. Dipeptidyl arylamidase II of the pituitary. Properties of lysyl-alanyl-β-naphthylamide hydrolysis: inhibition by cations, distribution in tissues and subcellular localization. J. Biol. Chem. 243 (1968) 4143–4150. [PMID: 4969969] |
| 2. |
McDonald, J.K. and Schwabe, C. Intracellular exopeptidases. In: Barrett, A.J. (Ed.), Proteinases in Mammalian Cells and Tissues, North-Holland Publishing Co., Amsterdam, 1977, pp. 311–391. |
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| [EC 3.4.14.2 created 1978] |
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