Dipeptidyl-peptidase II
| Dipeptidyl-peptidase II | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC number | 3.4.14.2 | ||||||||
| CAS number | 76199-23-0 | ||||||||
| Databases | |||||||||
| IntEnz | IntEnz view | ||||||||
| BRENDA | BRENDA entry | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | KEGG entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
| PDB structures | RCSB PDB PDBe PDBsum | ||||||||
| |||||||||
Dipeptidyl-peptidase II (EC 3.4.14.2, dipeptidyl aminopeptidase II, dipeptidyl arylamidase II, carboxytripeptidase, dipeptidyl peptidase II, DAP II, dipeptidyl(amino)peptidase II, dipeptidylarylamidase) is an enzyme.[1][2] This enzyme catalyses the following chemical reaction
- Release of an N-terminal dipeptide, Xaa-Yaa!, preferentially when Yaa is Ala or Pro. Substrates are oligopeptides, preferentially tripeptides
This lysosomal serine-type peptidase is maximally active at acidic pH.
References
- ↑ McDonald, J.K.; Reilly, T.J.; Zeitman, B.B.; Ellis, S. (1968). "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: 4143–4150. PMID 4969969.
- ↑ McDonald, J.K.; Schwabe, C. (1977). "Intracellular exopeptidases". In Barrett, A.J. Proteinases in Mammalian Cells and Tissues. Amsterdam: North-Holland Publishing Co. pp. 311–391.
External links
- Dipeptidyl-peptidase II at the US National Library of Medicine Medical Subject Headings (MeSH)
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