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 number3.4.19.2
CAS number94047-14-0
Databases
IntEnzIntEnz view
BRENDABRENDA entry
ExPASyNiceZyme view
KEGGKEGG entry
MetaCycmetabolic pathway
PRIAMprofile
PDB structuresRCSB PDB PDBe PDBsum

This enzyme inactivates vasopressin and oxytocin by splitting off glycinamide.

References

  1. 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.
  2. 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.
  3. 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.
This article is issued from Wikipedia. The text is licensed under Creative Commons - Attribution - Sharealike. Additional terms may apply for the media files.