Pro-opiomelanocortin converting enzyme
{{Infobox enzyme
| Name = Pro-opiomelanocortin converting enzyme
| EC_number = 3.4.23.17
| CAS_number = 80891-34-5
| GO_code =
| image =
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Pro-opiomelanocortin converting enzyme ({{EC number|3.4.23.17}}, prohormone converting enzyme, pro-opiomelanocortin-converting enzyme, proopiomelanocortin proteinase, PCE) is an enzyme.{{cite journal | vauthors = 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 = The Journal of Biological Chemistry | volume = 260 | issue = 12 | pages = 7194–205 | date = June 1985 | pmid = 2987247 }}{{cite journal | vauthors = Loh YP | title = Kinetic studies on the processing of human beta-lipotropin by bovine pituitary intermediate lobe pro-opiomelanocortin-converting enzyme | journal = The Journal of Biological Chemistry | volume = 261 | issue = 26 | pages = 11949–55 | date = September 1986 | pmid = 3017955 }}{{cite journal | vauthors = 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 = The Journal of Biological Chemistry | volume = 264 | issue = 30 | pages = 17796–801 | date = October 1989 | pmid = 2553692 }} This enzyme catalyses the following chemical reaction
: Cleavage at paired basic residues in certain prohormones, either between them, or on the carboxyl side
This membrane-bound enzyme is isolated from cattle pituitary secretory vesicle.
References
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External links
- {{MeshName|Pro-opiomelanocortin+converting+enzyme}}
{{Aspartic acid proteases}}
{{Enzymes}}
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