KEGG   ENZYME: 3.4.23.17
Entry
EC 3.4.23.17                Enzyme                                 
Name
pro-opiomelanocortin converting enzyme;
prohormone converting enzyme;
pro-opiomelanocortin-converting enzyme;
proopiomelanocortin proteinase;
PCE
Class
Hydrolases;
Acting on peptide bonds (peptidases);
Aspartic endopeptidases
Reaction(IUBMB)
Cleavage at paired basic residues in certain prohormones, either between them, or on the carboxyl side
Comment
A 70 kDa membrane-bound enzyme isolated from cattle pituitary secretory vesicle.
History
EC 3.4.23.17 created 1989 as EC 3.4.99.38, transferred 1992 to EC 3.4.23.17
Reference
1  [PMID:2987247]
  Authors
Loh YP, Parish DC, Tuteja R.
  Title
Purification and characterization of a paired basic residue-specific pro-opiomelanocortin converting enzyme from bovine pituitary intermediate lobe secretory vesicles.
  Journal
J Biol Chem 260:7194-205 (1985)
Reference
2  [PMID:3017955]
  Authors
Loh YP.
  Title
Kinetic studies on the processing of human beta-lipotropin by bovine pituitary intermediate lobe pro-opiomelanocortin-converting enzyme.
  Journal
J Biol Chem 261:11949-55 (1986)
Reference
3  [PMID:2553692]
  Authors
Estivariz FE, Birch NP, Loh YP.
  Title
Generation of Lys-gamma 3-melanotropin from pro-opiomelanocortin 1-77 by a bovine intermediate lobe secretory vesicle membrane-associated aspartic protease and purified pro-opiomelanocortin converting enzyme.
  Journal
J Biol Chem 264:17796-801 (1989)
Other DBs
ExplorEnz - The Enzyme Database: 3.4.23.17
IUBMB Enzyme Nomenclature: 3.4.23.17
ExPASy - ENZYME nomenclature database: 3.4.23.17
BRENDA, the Enzyme Database: 3.4.23.17
CAS: 80891-34-5

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