Pro-opiomelanocortin converting enzyme

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Pro-opiomelanocortin converting enzyme
Identifiers
EC no.3.4.23.17
CAS no.80891-34-5
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IntEnzIntEnz view
BRENDABRENDA entry
ExPASyNiceZyme view
KEGGKEGG entry
MetaCycmetabolic pathway
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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

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

  1. ^ 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.
  2. ^ 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.
  3. ^ 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.

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