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Information on EC 3.4.23.17 - Pro-opiomelanocortin converting enzyme
for references in articles please use BRENDA:EC3.4.23.17
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EC Tree 3 Hydrolases
3.4 Acting on peptide bonds (peptidases)
3.4.23 Aspartic endopeptidases
3.4.23.17 Pro-opiomelanocortin converting enzyme
IUBMB Comments
A 70 kDa membrane-bound enzyme isolated from cattle pituitary secretory vesicle.
The enzyme appears in viruses and cellular organisms
- 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 Schemes
showCleavage at paired basic residues in certain prohormones, either between them, or on the carboxyl side
Synonyms
pro-opiomelanocortin-converting enzyme, pro-opiomelanocortin converting enzyme, prohormone converting enzyme, more
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
EC 3.4.99.38
-
-
formerly
-
PCE
Pro-opiomelanocortin-converting enzyme
-
-
-
-
Prohormone converting enzyme
-
-
-
-
Proopiomelanocortin proteinase
-
-
-
-
Proteinase, proopiomelanocortin
-
-
-
-
PCE
-
-
-
-
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
Cleavage at paired basic residues in certain prohormones, either between them, or on the carboxyl side
-
-
-
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
hydrolysis of peptide bond
-
-
aspartic endopeptidase
-
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CAS REGISTRY NUMBER
COMMENTARY
80891-34-5
-
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
NH2-terminal pro-opiomelanocortin1-77 + H2O
Lys-gamma3-melanotropin + NH2-terminal pro-opiomelanocortin1-49
pro-insulin + H2O
insulin chain A + insulin chain B
-
Substrates: cleavage of a Lys-Arg-/- and Arg-Arg-/- bonds
Products: -
Products: -
?
pro-vasopressin + H2O
neurophysin + glycopeptide
-
Substrates: cleavage at a monobasic residue
Products: -
Products: -
?
pro-vasopressin + H2O
vasopressin + pro-sequence of vasopressin
-
Substrates: cleavage of a Lys-Arg-/- bond
Products: -
Products: -
?
NH2-terminal pro-opiomelanocortin1-77 + H2O
Lys-gamma3-melanotropin + NH2-terminal pro-opiomelanocortin1-49
-
Substrates: preferential cleavage between Arg49-Lys50
Products: + gamma-melanotropin, minor product
Products: + gamma-melanotropin, minor product
?
NH2-terminal pro-opiomelanocortin1-77 + H2O
Lys-gamma3-melanotropin + NH2-terminal pro-opiomelanocortin1-49
-
Substrates: O-linked glycosylation at Thr45 greatly inhibits the ability to cleave the Arg49-Lys50 bond
Products: -
Products: -
?
NH2-terminal pro-opiomelanocortin1-77 + H2O
Lys-gamma3-melanotropin + NH2-terminal pro-opiomelanocortin1-49
-
Substrates: preferential cleavage between Arg49-Lys50
Products: -
Products: -
?
NH2-terminal pro-opiomelanocortin1-77 + H2O
Lys-gamma3-melanotropin + NH2-terminal pro-opiomelanocortin1-49
-
Substrates: O-linked glycosylation at Thr45 greatly inhibits the ability to cleave the Arg49-Lys50 bond
Products: -
Products: -
?
NH2-terminal pro-opiomelanocortin1-77 + H2O
Lys-gamma3-melanotropin + NH2-terminal pro-opiomelanocortin1-49
-
Substrates: -
Products: -
Products: -
?
NH2-terminal pro-opiomelanocortin1-77 + H2O
Lys-gamma3-melanotropin + NH2-terminal pro-opiomelanocortin1-49
-
Substrates: -
Products: -
Products: -
?
Pro-insulin + H2O
Insulin A-chain + insulin B-chain
-
Substrates: -
Products: enzyme cleaves pro-insulin at the Lys-Arg pair to yield the A chain of insulin and at the Arg-Arg pair to yield the B-chain and the A-chain linked to C-chain (A-C) intermediate
Products: enzyme cleaves pro-insulin at the Lys-Arg pair to yield the A chain of insulin and at the Arg-Arg pair to yield the B-chain and the A-chain linked to C-chain (A-C) intermediate
?
Pro-opiomelanocortin + H2O
?
-
Substrates: may function as a pro-opiomelanocortin processing enzyme in the pituitary intermediate lobe
Products: -
Products: -
?
Pro-opiomelanocortin + H2O
?
-
Substrates: physiological role of PC1 and PC2 as distinct proprotein convertases acting alone or together to produce a set of tissue-specific maturation products in the brain and in the peripheral tissues
Products: -
Products: -
?
Pro-opiomelanocortin + H2O
Adrenocorticotropin + beta-lipotropin
-
Substrates: -
Products: -
Products: -
?
Pro-opiomelanocortin + H2O
Adrenocorticotropin + beta-lipotropin
-
Substrates: -
Products: a 27000 and 22000 Da band detected by anti-N-proopiomelanocortin immunoblots and to 26000 Da, 22000 Da and 14000 DA bands that are immunoreactive with anti-beta-lipotropin
Products: a 27000 and 22000 Da band detected by anti-N-proopiomelanocortin immunoblots and to 26000 Da, 22000 Da and 14000 DA bands that are immunoreactive with anti-beta-lipotropin
?
Pro-opiomelanocortin + H2O
Adrenocorticotropin + beta-lipotropin
-
Substrates: cleaves the peptide bonds either between the Lys and Arg or on the carboxyl side of the Arg at Lys-Arg pairs of pro-opiomelanocortin
Products: + beta-endorphin + MW 16000 NH2-terminal glycopeptide
Products: + beta-endorphin + MW 16000 NH2-terminal glycopeptide
?
Pro-opiomelanocortin + H2O
Adrenocorticotropin + beta-lipotropin
-
Substrates: cleaves the peptide bonds either between the Lys and Arg or on the carboxyl side of the Arg at Lys-Arg pairs of pro-opiomelanocortin
Products: ACTH of MW 21000-23000, 13000 and 4500
Products: ACTH of MW 21000-23000, 13000 and 4500
?
Pro-opiomelanocortin + H2O
Adrenocorticotropin + beta-lipotropin
-
Substrates: -
Products: -
Products: -
?
Pro-opiomelanocortin + H2O
Adrenocorticotropin + beta-lipotropin
-
Substrates: -
Products: PC2: beta-endorphin + an N-terminally extended corticotropin containing the joining peptide + either alpha-melanotropin or desacetyl-alpha-melanotropin
Products: PC2: beta-endorphin + an N-terminally extended corticotropin containing the joining peptide + either alpha-melanotropin or desacetyl-alpha-melanotropin
?
Pro-opiomelanocortin + H2O
Adrenocorticotropin + beta-lipotropin
-
Substrates: -
Products: PC2 cleaves at the five pairs of basic residues, PC1 cleaves two of them preferentially
Products: PC2 cleaves at the five pairs of basic residues, PC1 cleaves two of them preferentially
?
Pro-opiomelanocortin + H2O
Adrenocorticotropin + beta-lipotropin
-
Substrates: -
Products: PC1: corticotropin + beta-lipotropin
Products: PC1: corticotropin + beta-lipotropin
?
Pro-opiomelanocortin + H2O
Adrenocorticotropin + beta-lipotropin
-
Substrates: -
Products: -
Products: -
?
Pro-opiomelanocortin + H2O
Adrenocorticotropin + beta-lipotropin
-
Substrates: -
Products: + alpha-melanotropin MW 16000 + NH2-terminal glycopeptide + an endorphin-related peptide
Products: + alpha-melanotropin MW 16000 + NH2-terminal glycopeptide + an endorphin-related peptide
?
Pro-opiomelanocortin + H2O
Adrenocorticotropin + beta-lipotropin
-
Substrates: -
Products: ACTH of MW 21000 and 13000
Products: ACTH of MW 21000 and 13000
?
Pro-opiomelanocortin + H2O
Adrenocorticotropin + beta-lipotropin
-
Substrates: -
Products: -
Products: -
?
Pro-opiomelanocortin + H2O
Adrenocorticotropin + beta-lipotropin
-
Substrates: -
Products: -
Products: -
?
pro-opiomelanocortin + H2O
opiomelanocortin + pro-sequence of opiomelanocortin
-
Substrates: hormone activation
Products: -
Products: -
?
pro-opiomelanocortin + H2O
opiomelanocortin + pro-sequence of opiomelanocortin
-
Substrates: -
Products: -
Products: -
?
Provasopressin + H2O
Arginine vasopressin-Gly10-Lys11-Arg12
-
Substrates: cleavage occurs primarily on the carboxyl side of the arginine in the pair of Lys-Arg basic residues separating the vasopressin peptide from the neurophysin moiety in the precursor
Products: major product
Products: major product
?
Provasopressin + H2O
Arginine vasopressin-Gly10-Lys11-Arg12
-
Substrates: human vasopressin prohormone
Products: major product
Products: major product
?
Provasopressin + H2O
Arginine vasopressin-Gly10-Lys11-Arg12
-
Substrates: -
Products: -
Products: -
?
Small synthetic peptides with paired basic residues + H2O
?
-
Substrates: -
Products: -
Products: -
?
Small synthetic peptides with paired basic residues + H2O
?
-
Substrates: -
Products: -
Products: -
?
Small synthetic peptides with paired basic residues + H2O
?
-
Substrates: -
Products: -
Products: -
?
Human beta-lipotropin + H2O
additional information
-
-
Substrates: cleavage at two of the three pairs of basic residues of human beta-lipotropin, at Lys37-Lys38 and Lys57-Arg58, but not at Lys86-Lys87, the cleavage at Lys57-Arg58 occurs primarily between these basic residues
Products: at enzyme concentration of 20 ng/0.1 ml: gamma-lipotropin + a beta-melanotropin linked to beta-endorphin intermediate + beta-endorpin, at enzyme concentration of 40 ng/0.1 ml: complete cleavage to yield beta-endorphin + beta-melanotrophin
Products: at enzyme concentration of 20 ng/0.1 ml: gamma-lipotropin + a beta-melanotropin linked to beta-endorphin intermediate + beta-endorpin, at enzyme concentration of 40 ng/0.1 ml: complete cleavage to yield beta-endorphin + beta-melanotrophin
?
Human beta-lipotropin + H2O
additional information
-
-
Substrates: -
Products: beta-endorphin(1-31) + beta-endorphin(1-29) + beta-endorphin(1-28) + gamma-lipotropin + beta-melanocyte-stimulating hormone
Products: beta-endorphin(1-31) + beta-endorphin(1-29) + beta-endorphin(1-28) + gamma-lipotropin + beta-melanocyte-stimulating hormone
?
Human beta-lipotropin + H2O
additional information
-
-
Substrates: -
Products: beta-endorphin(1-31) + beta-endorphin(1-29) + beta-endorphin(1-28) + gamma-lipotropin + beta-melanocyte-stimulating hormone
Products: beta-endorphin(1-31) + beta-endorphin(1-29) + beta-endorphin(1-28) + gamma-lipotropin + beta-melanocyte-stimulating hormone
?
additional information
?
-
-
Substrates: poorly cleaved: benzyloxycarbonyl-Val-Lys-Lys-Arg 4-methoxy-2-naphthylamide
Products: -
Products: -
?
additional information
?
-
-
Substrates: not: Lys-Lys-Arg-Arg residues in ACTH1-39
Products: -
Products: -
?
additional information
?
-
-
Substrates: the enzyme is highly specific for mono- and dibasic residues of prohormones, overview
Products: -
Products: -
?
additional information
?
-
-
Substrates: the enzyme is highly specific for mono- and dibasic residues of prohormones
Products: -
Products: -
?
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
pro-insulin + H2O
insulin chain A + insulin chain B
-
Substrates: cleavage of a Lys-Arg-/- and Arg-Arg-/- bonds
Products: -
Products: -
?
pro-vasopressin + H2O
neurophysin + glycopeptide
-
Substrates: cleavage at a monobasic residue
Products: -
Products: -
?
pro-vasopressin + H2O
vasopressin + pro-sequence of vasopressin
-
Substrates: cleavage of a Lys-Arg-/- bond
Products: -
Products: -
?
additional information
?
-
-
Substrates: the enzyme is highly specific for mono- and dibasic residues of prohormones, overview
Products: -
Products: -
?
Pro-opiomelanocortin + H2O
?
-
Substrates: may function as a pro-opiomelanocortin processing enzyme in the pituitary intermediate lobe
Products: -
Products: -
?
Pro-opiomelanocortin + H2O
?
-
Substrates: physiological role of PC1 and PC2 as distinct proprotein convertases acting alone or together to produce a set of tissue-specific maturation products in the brain and in the peripheral tissues
Products: -
Products: -
?
pro-opiomelanocortin + H2O
opiomelanocortin + pro-sequence of opiomelanocortin
-
Substrates: hormone activation
Products: -
Products: -
?
pro-opiomelanocortin + H2O
opiomelanocortin + pro-sequence of opiomelanocortin
-
Substrates: -
Products: -
Products: -
?
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Ca2+
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
-
not: diisopropyl fluorophosphate; phenylmethane sulfonylfluoride
-
additional information
-
EDTA; Nalpha-p-tosyl-L-lysine chloromethylketone hydrochloride; chloroquine; not: diisopropyl fluorophosphate
-
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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DISEASE
TITLE OF PUBLICATION
LINK TO PUBMED
Neuroblastoma
Post-translational processing of human procorticotrophin-releasing factor in transfected mouse neuroblastoma and Chinese hamster ovary cell lines.
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
4 - 4.5
4 - 5.5
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
3 - 6
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
a recombinant vaccinia virus vector is used to coexpress mouse prohormone convertase PC1 and PC2 in the constitutively secreting cell line BSC-40 and in the endocrine tissue-derived cell lines PC12 and AtT-20
-
-
brenda
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
-
intermediate lobe, anterior lobe, and neural lobe secretory granules
brenda
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
Highest Expressing Human Cell Lines
Cell Line LinksPlease wait a moment until the data is sorted. This message will disappear when the data is sorted.
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
68000
70000
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
-
immunogenic cross-reactive with anti-yapsin 1 antibodies due to high structural homology
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POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
glycoprotein
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
a recombinant vaccinia virus vector is used to coexpress mouse prohormone convertase PC1 and PC2 in the constitutively secreting cell line BSC-40 and in the endocrine tissue-derived cell lines PC12 and AtT-20
-
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
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
brenda
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
brenda
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
brenda
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
brenda
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
brenda
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
brenda
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
brenda
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
brenda
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
brenda
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
brenda
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
-
brenda
Cawley, N.; Li, Z.; Loh, Y.
Biosynthesis, trafficking, and secretion of pro-opiomelanocortin-derived peptides
J. Mol. Endocrinol.
56
T77-T97
2016
Bos taurus
brenda
EXTERNAL LINKS (specific for EC-Number 3.4.23.17)
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