Peptidyl-glycinamidase
| Peptidyl-glycinamidase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC number | 3.4.19.2 | ||||||||
| CAS number | 94047-14-0 | ||||||||
| Databases | |||||||||
| IntEnz | IntEnz view | ||||||||
| BRENDA | BRENDA entry | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | KEGG entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
| PDB structures | RCSB PDB PDBe PDBsum | ||||||||
| |||||||||
Peptidyl-glycinamidase (EC 3.4.19.2, carboxyamidase, peptidyl carboxy-amidase, peptidyl-aminoacylamidase, carboxamidopeptidase, peptidyl amino acid amide hydrolase) is an enzyme.[1][2][3] This enzyme catalyses the following chemical reaction
- Cleavage of C-terminal glycinamide from polypeptides
This enzyme inactivates vasopressin and oxytocin by splitting off glycinamide.
References
- ↑ Fruhaufová, L.; Suska-Brezezinska, E.; Barth, T.; Rychlik, I. (1973). "Rat liver enzyme inactivating oxytocin and its deamino-carba analogues". Coll. Czech. Chem. Commun. 38: 2793–2798. doi:10.1135/cccc19732793.
- ↑ Nardacci, N.J.; Mukhopadhyay, S.; Campbell, B.J. (1975). "Partial purification and characterization of the antidiuretic hormone in toad bladder". Biochim. Biophys. Acta. 377: 146–157. doi:10.1016/0005-2744(75)90295-8. PMID 1122284.
- ↑ Simmons, W.H.; Walter, R. (1980). "Carboxamidopeptidase: purificaction and characterization of a neurohypophyseal hormone inactivating peptidase from toad skin". Biochemistry. 19: 39–48. doi:10.1021/bi00542a007. PMID 6766314.
External links
- Peptidyl-glycinamidase at the US National Library of Medicine Medical Subject Headings (MeSH)
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