Biology:Dipeptidyl-peptidase II
From HandWiki
| Dipeptidyl-peptidase II | |||||||||
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| 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 | ||||||||
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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
- ↑ "Purification of dipeptidyl aminopeptidase II (dipeptidyl arylamidase II) of the anterior pituitary gland. Peptidase and dipeptide esterase activities". The Journal of Biological Chemistry 243 (15): 4143–50. August 1968. doi:10.1016/S0021-9258(18)93291-6. PMID 4969969.
- ↑ "Intracellular exopeptidases". Proteinases in Mammalian Cells and Tissues. Amsterdam: North-Holland Publishing Co.. 1977. pp. 311–391.
External links
- Dipeptidyl-peptidase+II at the US National Library of Medicine Medical Subject Headings (MeSH)
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