Peptidyl-glycinamidase

Peptidyl-glycinamidase
Identifiers
EC no.3.4.19.2
CAS no.94047-14-0
Databases
IntEnzIntEnz view
BRENDABRENDA entry
ExPASyNiceZyme view
KEGGKEGG entry
MetaCycmetabolic pathway
PRIAMprofile
PDB structuresRCSB PDB PDBe PDBsum
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PMCarticles
PubMedarticles
NCBIproteins

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

  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.