|Superclasses:||Reactions Classified By Conversion Type → Simple Reactions → Chemical Reactions → Protein-Modification Reactions|
|Reactions Classified By Substrate → Macromolecule Reactions → Protein-Reactions → Protein-Modification Reactions|
EC Number: 188.8.131.52
Supersedes EC number: 184.108.40.206
The reaction direction shown, that is, A + B ↔ C + D versus C + D ↔ A + B, is in accordance with the Enzyme Commission system.
Mass balance status: Undetermined; a substrate lacks a chemical formula
Enzyme Commission Primary Name: peptidyl-glycinamidase
Enzyme Commission Synonyms: carboxyamidase, peptidyl carboxy-amidase, peptidyl-aminoacylamidase, carboxamidopeptidase, peptidyl amino acid amide hydrolase
Enzyme Commission Summary:
The enzyme catalyses the cleavage of C-terminal glycinamide from polypeptides.
Inactivates vasopressin and oxytocin by splitting off glycinamide. Also cleaves ester substrates of trypsin and chymotrypsin. Although glycinamide is by far the preferred leaving group, other aminoacylamides may also be released, e.g. phenylalaninamide. The toad skin enzyme is inhibited by diisopropyl fluorophosphate.
Nardacci75: Nardacci NJ, Mukhopadhyay S, Campbell BJ (1975). "Partial purification and characterization of the antidiuretic hormone-inactivating enzyme from renal plasma membranes." Biochim Biophys Acta 377(1);146-57. PMID: 1122284
Simmons80: Simmons WH, Walter R (1980). "Carboxamidopeptidase: purification and characterization of a neurohypophyseal hormone inactivating peptidase from toad skin." Biochemistry 19(1);39-48. PMID: 6766314
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