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
| 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 | ||||||||
| |||||||||
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". Collection of Czechoslovak Chemical Communications. 38 (9): 2793–2798. doi:10.1135/cccc19732793.
- Nardacci NJ, Mukhopadhyay S, Campbell BJ (January 1975). "Partial purification and characterization of the antidiuretic hormone-inactivating enzyme from renal plasma membranes". Biochimica et Biophysica Acta (BBA) - Enzymology. 377 (1): 146–57. doi:10.1016/0005-2744(75)90295-8. PMID 1122284.
- Simmons WH, Walter R (January 1980). "Carboxamidopeptidase: purification and characterization of a neurohypophyseal hormone inactivating peptidase from toad skin". Biochemistry. 19 (1): 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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