Tripeptide aminopeptidase
| Tripeptide aminopeptidase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 3.4.11.4 | ||||||||
| CAS no. | 9056-26-2 | ||||||||
| Databases | |||||||||
| IntEnz | IntEnz view | ||||||||
| BRENDA | BRENDA entry | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | KEGG entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
| PDB structures | RCSB PDB PDBe PDBsum | ||||||||
| |||||||||
Tripeptide aminopeptidase (EC 3.4.11.4, tripeptidase, aminotripeptidase, aminoexotripeptidase, lymphopeptidase, imidoendopeptidase, peptidase B, alanine-phenylalanine-proline arylamidase, peptidase T) is an enzyme.[1][2] This enzyme catalyses the following chemical reaction:
- Release of the N-terminal residue from a tripeptide
This is a zinc enzyme, widely distributed in mammalian tissues.
References
- ^ Doumeng C, Maroux S (March 1979). "Aminotripeptidase, a cytosol enzyme from rabbit intestinal mucosa". The Biochemical Journal. 177 (3): 801–8. PMC 1186443. PMID 109082.
- ^ Sachs L, Marks N (September 1982). "A highly specific aminotripeptidase of rat brain cytosol. Substrate specificity and effects of inhibitors". Biochimica et Biophysica Acta. 706 (2): 229–38. doi:10.1016/0167-4838(82)90491-5. PMID 7126601.
External links
- Tripeptide+aminopeptidase at the U.S. National Library of Medicine Medical Subject Headings (MeSH)