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Information on EC 3.4.24.62 - magnolysin
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3.4.24.62 magnolysinSpecify your search results
The enzyme appears in viruses and cellular organisms
Reaction Schemes
Hydrolysis of polypeptides with Arg or Lys in P1 and P2, e.g. to hydrolyse pro-oxytocin at -Lys-Arg-/-Ala-Val-. The specificity further depends on the organization of a beta-turn-alpha-helix of nine or more residues containing the paired basic amino acids near the centre
Synonyms
magnolysin, pro-ocytocin convertase, 
more
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
Bovine neurosecretory granule protease cleaving pro-oxytocin/neurophysin
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pro-ocytocin convertase
pro-ocytocin/neurophysin-converting enzyme
Pro-oxytocin convertase
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Pro-oxytocin/neurophysin convertase
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Proteinase, prooxyphysin
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-
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
Hydrolysis of polypeptides with Arg or Lys in P1 and P2, e.g. to hydrolyse pro-oxytocin at -Lys-Arg-/-Ala-Val-. The specificity further depends on the organization of a beta-turn-alpha-helix of nine or more residues containing the paired basic amino acids near the centre
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
hydrolysis of peptide bond
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CAS REGISTRY NUMBER
COMMENTARY
110353-43-0
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162875-09-4
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
Pro-oxytocin/neurophysin(1-20) + H2O
Pro-oxytocin/neurophysin(1-12) + pro-oxytocin/neurophysin(13-20)
[Arg11,Lys12]-Pro-oxytocin/neurophysin(1-20) + H2O
?
-
i.e. peptide VI, hydrolysis at the same rate as pro-oxytocin/neurophysin(1-20)
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?
Pro-oxytocin/neurophysin + H2O
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involved in post-translational processing
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?
Pro-oxytocin/neurophysin + H2O
?
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primary cleavage at the Arg12-Ala13 bond
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?
Pro-oxytocin/neurophysin(1-20) + H2O
Pro-oxytocin/neurophysin(1-12) + pro-oxytocin/neurophysin(13-20)
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obtained by hemisynthesis
i.e. peptide II (i.e. oxytocinGly10Lys11Arg12 and peptide III)
?
Pro-oxytocin/neurophysin(1-20) + H2O
Pro-oxytocin/neurophysin(1-12) + pro-oxytocin/neurophysin(13-20)
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synthetic eicosapeptide reproducing the entire sequence of amino-terminal domain of bovine proOc/Np precursor
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?
Pro-oxytocin/neurophysin(1-20) + H2O
Pro-oxytocin/neurophysin(1-12) + pro-oxytocin/neurophysin(13-20)
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strictly selective for basic amino acid doublet Lys11-Arg12, cleavage site: Arg12-Ala13
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?
Pro-oxytocin/neurophysin(1-20) + H2O
Pro-oxytocin/neurophysin(1-12) + pro-oxytocin/neurophysin(13-20)
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strictly selective for basic amino acid doublet Lys11-Arg12, cleavage site: Arg12-Ala13
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?
Pro-oxytocin/neurophysin(1-20) + H2O
Pro-oxytocin/neurophysin(1-12) + pro-oxytocin/neurophysin(13-20)
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strictly selective for basic amino acid doublet Lys11-Arg12, cleavage site: Arg12-Ala13
i.e. peptide II (i.e. oxytocinGly10Lys11Arg12 and peptide III)
?
Pro-oxytocin/neurophysin(1-20) + H2O
Pro-oxytocin/neurophysin(1-12) + pro-oxytocin/neurophysin(13-20)
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strictly selective for basic amino acid doublet Lys11-Arg12, cleavage site: Arg12-Ala13
i.e. peptide II (i.e. oxytocinGly10Lys11Arg12 and peptide III)
?
Pro-oxytocin/neurophysin(1-20) + H2O
Pro-oxytocin/neurophysin(1-12) + pro-oxytocin/neurophysin(13-20)
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i.e. model substrate peptide I
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?
Pro-oxytocin/neurophysin(1-20) + H2O
Pro-oxytocin/neurophysin(1-12) + pro-oxytocin/neurophysin(13-20)
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i.e. model substrate peptide I
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?
Pro-oxytocin/neurophysin(1-20) + H2O
Pro-oxytocin/neurophysin(1-12) + pro-oxytocin/neurophysin(13-20)
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i.e. model substrate peptide I
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-
?
Pro-oxytocin/neurophysin(1-20) + H2O
Pro-oxytocin/neurophysin(1-12) + pro-oxytocin/neurophysin(13-20)
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i.e. model substrate peptide I
i.e. peptide II (i.e. oxytocinGly10Lys11Arg12 and peptide III)
?
Pro-oxytocin/neurophysin(1-20) + H2O
Pro-oxytocin/neurophysin(1-12) + pro-oxytocin/neurophysin(13-20)
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i.e. model substrate peptide I
i.e. peptide II (i.e. oxytocinGly10Lys11Arg12 and peptide III)
?
Pro-oxytocin/neurophysin(1-20) + H2O
Pro-oxytocin/neurophysin(1-12) + pro-oxytocin/neurophysin(13-20)
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strictly selective for basic amino acid doublet Lys11-Arg12, cleavage site: Arg12-Ala13
i.e. peptide II (i.e. oxytocinGly10Lys11Arg12 and peptide III)
?
[Ala10]-Pro-oxytocin/neurophysin(1-20) + H2O
?
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i.e. peptide XI, hydrolysis at the same rate as pro-oxytocin/neurophysin(1-20)
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?
additional information
?
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relationship between structure and enzyme action
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?
additional information
?
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relationship between structure and enzyme action
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?
additional information
?
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specificity depends on the organization of a beta-turn-alpha-helix of nine or more residues containing the basic amino acid doublet near the centre
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?
additional information
?
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structural requirements of the substrate peptides (pro-OT/Np-model)
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?
additional information
?
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No substrates are pro-oxytocin/neurophysin peptides (i.e. pro-OT/Np(1-20)) with D-Arg12
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?
additional information
?
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No substrates are pro-oxytocin/neurophysin peptides (i.e. pro-OT/Np(1-20)) with D-Arg12
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?
additional information
?
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No substrates are pro-oxytocin/neurophysin peptides (i.e. pro-OT/Np(1-20)) with D-Arg12
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?
additional information
?
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peptides bearing Nle or D-Arg at subsite P1 or containing Nle or D-Lys at subsite P2 remain uncleaved, substrate bearing the Lys-Arg doublet is hydrolyzed with best efficiency, a minimal length of eight residues is necessary to allow for substrate binding
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-
?
additional information
?
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peptides bearing Nle or D-Arg at subsite P1 or containing Nle or D-Lys at subsite P2 remain uncleaved, substrate bearing the Lys-Arg doublet is hydrolyzed with best efficiency, a minimal length of eight residues is necessary to allow for substrate binding
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-
?
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
Pro-oxytocin/neurophysin + H2O
?
-
involved in post-translational processing
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-
?
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
-
[D-Lys11]-pro-oxytocin/neurophysin(1-20), Gly-Gly-Lys-D-Arg-Ala-Val, Cys-Pro-Leu-Gly-Gly-Lys-D-Arg-Ala-Val; no inhibition by PMSF, pepstatin
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
additional information
-
pI: 4.9 or 6.9 (corpus luteum, different enzyme preparations)
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
additional information
-
secretory granule from neurohypophysis hypothalamus
brenda
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
55000 - 65000
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
monomer
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
affinity chromatography
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Cohen, P.; Clamagirand, C.; Gluschankof, P.; Gomez, S.; Creminon, C.; Plevrakis, I.; Clavreul, C.; Fahy, C.; Boussetta, H.; et al.
Somatostatin-28 and pro-ocytocin/neurophysin convertases: basic pair selective endoproteases involved in pro-hormone processing in the rat brain cortex and bovine corpus luteum
Biochimie
70
17-23
1988
Bos taurus
brenda
Clamagirand, C.; Creminon, C.; Fahy, C.; Boussetta, H.; Cohen, P.
Partial purification and functional properties of an endoprotease from bovine neurosecretory granules cleaving proocytocin/neurophysin peptides at the basic amino acid doublet
Biochemistry
26
6018-6023
1987
Bos taurus
brenda
Clamagirand, C.; Camier, M.; Fahy, C.; Clavreul, C.; Creminon, C.; Cohen, P.
C-terminally extended ocytocin and pro-ocytocin: neurophysin peptide converting enzyme in bovine corpus luteum [published erratum appears in Biochem Biophys Res Commun 1987 May 14;144(3):1349]
Biochem. Biophys. Res. Commun.
143
789-796
1987
Bos taurus
brenda
Creminon, C.; Rholam, M.; Boussetta, H.; Marrakchi, N.; Cohen, P.
Synthetic peptide substrates as models to study a pro-ocytocin/neurophysin converting enzyme
J. Chromatogr.
440
439-448
1988
Bos taurus
brenda
Brakch, N.; Boussetta, H.; Rholam, M.; Cohen, P.
Processing endoprotease recognizes a structural feature at the cleavage site of peptide prohormones. The pro-ocytocin/neurophysin model
J. Biol. Chem.
264
15912-15916
1989
Bos taurus
brenda
Plevrakis, I.; Clamagirand, C.; Creminon, C.; Brakch, N.; Rholam, M.; Cohen, P.
Proocytocin/neurophysin convertase from bovine neurohypophysis and corpus luteum secretory granules: complete purification, structure-function relationships, and competitive inhibitor
Biochemistry
28
2705-2710
1989
Bos taurus
brenda
Guillou, M.D.; Camier, M.; Clamagirand, C.
Evidence for the presence of pro-oxytocin/neurophysin-converting enzyme in the human ovary
J. Endocrinol.
142
345-352
1994
Homo sapiens
brenda
Rholam, M.; Clamagirand, C.; Cohen, P.
Magnolysin
Handbook Of Proteolytic Enzymes(Barrett,A. J. ,Rawlings,N. D. ,Woessner,J. F. ,Eds. )Academic Press
1
1039-1042
2004
Bos taurus, Homo sapiens
-
brenda
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