3.4.23.17: Pro-opiomelanocortin converting enzyme
This is an abbreviated version!
For detailed information about Pro-opiomelanocortin converting enzyme, go to the full flat file.
Word Map on EC 3.4.23.17
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3.4.23.17
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lobe
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pituitary
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beta-endorphin
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beta-lipotropin
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residue-specific
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acth
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parish
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pepstatin
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lys-arg
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adrenocorticotropin
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tuteja
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cooh-terminal
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glycopeptide
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endoprotease
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furin
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alpha-melanotropin
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convertase
- 3.4.23.17
- lobe
- pituitary
- beta-endorphin
- beta-lipotropin
-
residue-specific
- acth
-
parish
- pepstatin
- lys-arg
- adrenocorticotropin
-
tuteja
-
cooh-terminal
- glycopeptide
- endoprotease
- furin
-
alpha-melanotropin
-
convertase
Reaction
Cleavage at paired basic residues in certain prohormones, either between them, or on the carboxyl side =
Synonyms
EC 3.4.99.38, More, PCE, POMC converting enzyme, Pro-opiomelanocortin-converting enzyme, Prohormone converting enzyme, Proopiomelanocortin proteinase, Proteinase, proopiomelanocortin, yapsin A
ECTree
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Reference
Reference on EC 3.4.23.17 - Pro-opiomelanocortin converting enzyme
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Loh, Y.P.; Parish, D.C.; Tuteja, R.
Purification and characterization of a paired basic residue-specific pro-opiomelanocortin converting enzyme from bovine pituitary intermediate lobe secretory vesicles
J. Biol. Chem.
260
7194-7205
1985
Bos taurus
Loh, Y.P.
Kinetic studies on the processing of human beta-lipotropin by bovine pituitary intermediate lobe pro-opiomelanocortin-converting enzyme
J. Biol. Chem.
261
11949-11955
1986
Bos taurus
Estivariz, F.E.; Birch, N.P.; Loh, Y.P.
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
17796-17801
1989
Bos taurus
Loh, Y.P.; Cawley, N.X.
Processing enzymes of pepsin family: yeast aspartic protease 3 and pro-opiomelanocortin converting enzyme
Methods Enzymol.
248
136-146
1995
Bos taurus, Rattus norvegicus
Parish, D.C.; Tuteja, R.; Altstein, M.; Gainer, H.; Loh, Y.P.
Purification and characterization of a paired basic residue-specific prohormone-converting enzyme from bovine pituitary neural lobe secretory vesicles
J. Biol. Chem.
261
14392-14397
1986
Bos taurus
Azaryan, A.V.; Wong, M.; Friedman, T.C.; Cawley, N.X.; Estivariz, F.E.; Chen, H-C.; Loh, Y.P.
Purification and characterization of a paired basic residue-specific yeast aspartic protease encoded by the YAP3 gene. Similarity to the mammalian pro-opiomelanocortin-converting enzyme
J. Biol. Chem.
268
11968-11975
1993
Saccharomyces cerevisiae, Saccharomyces cerevisiae BJ 3501
Benjannet, S.; Rondeau, N.; Day, R.; Chretien, M.; Seidah, N.G.
PC1 and PC2 are proprotein convertases capable of cleaving proopiomelanocortin at distinct pairs of basic residues
Proc. Natl. Acad. Sci. USA
88
3564-3568
1991
Mus musculus
Loh, Y.P.; Gainer, H.
Characterization of pro-opiocortin-converting activity in purified secretory granules from rat pituitary neurointermediate lobe
Proc. Natl. Acad. Sci. USA
79
108-112
1982
Rattus norvegicus
Azaryan, A.V.; Schiller, M.R.; Hook, V.Y.H.
Chromaffin granule aspartic proteinase processes recombinant proopiomelanocortin (POMC)
Biochem. Biophys. Res. Commun.
215
937-944
1995
Bos taurus
Loh, Y.P.; Birch, N.P.; Castro, M.G.
Pro-opiomelanocortin and pro-vasopressin converting enzyme in pituitary secretory vesicles
Biochimie
70
11-16
1988
Bos taurus
Loh, Y.P.; Cawley, N.X.
Yapsin A
Handbook of Proteolytic Enzymes (Barrett, A. J. , Rawlings, N. D. , Woessner, J. F. , eds. )Academic Press
1
133-135
2004
Bos taurus
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