Dipeptidyl-peptidase III
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| Dipeptidyl-peptidase III | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 3.4.14.4 | ||||||||
| CAS no. | 77464-87-0 | ||||||||
| 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 III (EC 3.4.14.4, dipeptidyl aminopeptidase III, dipeptidyl arylamidase III, enkephalinase B, red cell angiotensinase) is an enzyme.[1][2] This enzyme catalyses the following chemical reaction
- Release of an N-terminal dipeptide from a peptide comprising four or more residues, with broad specificity. Also acts on dipeptidyl 2-naphthylamides.
This cytosolic peptidase that is active at neutral pH.
References
- ^ McDonald JK (1998). "Dipeptidyl-peptidase III". In Barrett AJ, Rawlings NA, Woessner JG (eds.). Handbook of Proteolytic Enzymes. London: Handbook of Proteolytic Enzymes. pp. 536–538.
- ^ Fukasawa K, Fukasawa KM, Iwamoto H, Hirose J, Harada M (June 1999). "The HELLGH motif of rat liver dipeptidyl peptidase III is involved in zinc coordination and the catalytic activity of the enzyme". Biochemistry. 38 (26): 8299–303. doi:10.1021/bi9904959. PMID 10387075.
External links
- Dipeptidyl-peptidase+III at the U.S. National Library of Medicine Medical Subject Headings (MeSH)
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