Pro-opiomelanocortin converting enzyme (EC 3.4.23.17, prohormone converting enzyme, pro-opiomelanocortin-converting enzyme, proopiomelanocortin proteinase, PCE) is an enzyme.[1][2][3] This enzyme catalyses the following chemical reaction
| Pro-opiomelanocortin converting enzyme | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 3.4.23.17 | ||||||||
| CAS no. | 80891-34-5 | ||||||||
| Databases | |||||||||
| IntEnz | IntEnz view | ||||||||
| BRENDA | BRENDA entry | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | KEGG entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
| PDB structures | RCSB PDB PDBe PDBsum | ||||||||
| |||||||||
- 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 edit
- ^ Loh YP, Parish DC, Tuteja R (June 1985). "Purification and characterization of a paired basic residue-specific pro-opiomelanocortin converting enzyme from bovine pituitary intermediate lobe secretory vesicles". The Journal of Biological Chemistry. 260 (12): 7194–205. PMID 2987247.
- ^ Loh YP (September 1986). "Kinetic studies on the processing of human beta-lipotropin by bovine pituitary intermediate lobe pro-opiomelanocortin-converting enzyme". The Journal of Biological Chemistry. 261 (26): 11949–55. PMID 3017955.
- ^ Estivariz FE, Birch NP, Loh YP (October 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". The Journal of Biological Chemistry. 264 (30): 17796–801. PMID 2553692.
External links edit
- Pro-opiomelanocortin+converting+enzyme at the U.S. National Library of Medicine Medical Subject Headings (MeSH)
