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MetaCyc Reaction: 3.4.23.17

Superclasses: Reactions Classified By Conversion TypeSimple ReactionsChemical Reactions
Reactions Classified By SubstrateSmall-Molecule Reactions

EC Number: 3.4.23.17

Supersedes EC number: 3.4.99.38

The direction shown, i.e. which substrates are on the left and right sides, is in accordance with the direction in which it was curated.

Mass balance status: Balance undetermined; a substrate lacks a chemical formula

Enzyme Commission Primary Name: pro-opiomelanocortin converting enzyme

Enzyme Commission Synonyms: prohormone converting enzyme, pro-opiomelanocortin-converting enzyme, proopiomelanocortin proteinase, PCE

Enzyme Commission Summary:
This enzyme catalyzes cleavage of certain prohormones, such as proopiomelanocortin, at paired basic residues, generating several peptides, some of which are functional hormones. A 70 kDa membrane-bound enzyme has been isolated from cattle pituitary secretory vesicle.

Citations: [Loh85, Loh86, Estivariz89]

Relationship Links: BRENDA:EC:3.4.23.17, ENZYME:EC:3.4.23.17, IUBMB-ExplorEnz:EC:3.4.23.17


References

Estivariz89: Estivariz FE, Birch NP, Loh YP (1989). "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." J Biol Chem 264(30);17796-801. PMID: 2553692

Loh85: Loh YP, Parish DC, Tuteja R (1985). "Purification and characterization of a paired basic residue-specific pro-opiomelanocortin converting enzyme from bovine pituitary intermediate lobe secretory vesicles." J Biol Chem 260(12);7194-205. PMID: 2987247

Loh86: Loh YP (1986). "Kinetic studies on the processing of human beta-lipotropin by bovine pituitary intermediate lobe pro-opiomelanocortin-converting enzyme." J Biol Chem 261(26);11949-55. PMID: 3017955


Report Errors or Provide Feedback
Please cite the following article in publications resulting from the use of MetaCyc: Caspi et al, Nucleic Acids Research 42:D459-D471 2014
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