Peptidyl-glycinamidase
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. and 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. and 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. and 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.
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