Tripeptide aminopeptidase
| Tripeptide aminopeptidase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC number | 3.4.11.4 | ||||||||
| CAS number | 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 zinc enzyme, widely distributed in mammalian tissues.
References
- ↑ Doumeng, C.; Maroux, S. (1979). "Aminopeptidase, a cytosol enzyme from rabbit intestinal mucosa". Biochem. J. 177: 801–808. PMID 109082.
- ↑ Sachs, L.; Marks, N. (1982). "A highly specific aminotripeptidase of rat brain cytosol. Substrate specificity and effects of inhibitors". Biochim. Biophys. Acta. 706: 229–238. doi:10.1016/0167-4838(82)90491-5. PMID 7126601.
External links
- Tripeptide aminopeptidase at the US National Library of Medicine Medical Subject Headings (MeSH)
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