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Information on EC 3.4.21.120 - oviductin and Organism(s) Xenopus laevis and UniProt Accession P79953

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EC Tree
     3 Hydrolases
         3.4 Acting on peptide bonds (peptidases)
             3.4.21 Serine endopeptidases
                3.4.21.120 oviductin
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This record set is specific for:
Xenopus laevis
UNIPROT: P79953 not found.
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Word Map
The taxonomic range for the selected organisms is: Xenopus laevis
The enzyme appears in selected viruses and cellular organisms
Reaction Schemes
preferential cleavage at Gly-Ser-Arg373-/- of glycoprotein gp43 in Xenopus laevis coelemic egg envelope to yield gp41
Synonyms
alpha-fetoprotein, oviductin, ovochymase, oviductin-1, ovochymase 2, oviductin-i, oviductal protease, gp43 processing protease, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
oviductal protease
-
Gp43 processing protease
-
-
oviductal protease
-
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
gp43 + H2O
gp41 + ?
show the reaction diagram
oviductin alone is the oviductal factor responsible for converting the egg envelope to a sperm-penetrable form, via an increase in sperm binding. gp43 processing is the only requirement for envelope conversion
-
-
?
gp43 + H2O
gp41 + ?
show the reaction diagram
Nalpha-tert-butoxycarbonyl-Leu-Ser-Thr-Arg-4-methylcoumarin-7-amide + H2O
Nalpha-tert-butoxycarbonyl-Leu-Ser-Thr-Arg + 7-amino-4-methylcoumarin
show the reaction diagram
-
14% of the activity with Nalpha-tert-butoxycarbonyl-Phe-Ser-Arg-4-methylcoumarin-7-amide
-
-
?
Nalpha-tert-butoxycarbonyl-Leu-Thr-Arg-4-methylcoumarin-7-amide + H2O
Nalpha-tert-butoxycarbonyl-Leu-Thr-Arg + 7-amino-4-methylcoumarin
show the reaction diagram
-
12% of the activity with Nalpha-tert-butoxycarbonyl-Phe-Ser-Arg-4-methylcoumarin-7-amide
-
-
?
Nalpha-tert-butoxycarbonyl-Phe-Ser-Arg-4-methylcoumarin-7-amide + H2O
Nalpha-tert-butoxycarbonyl-Phe-Ser-Arg + 7-amino-4-methylcoumarin
show the reaction diagram
-
-
-
-
?
Nalpha-tert-butoxycarbonylphenylalanylserylarginyl-7-amido-4-methylcoumarin + H2O
Nalpha-tert-butoxycarbonylphenylalanylserylarginine + 7-amino-4-methylcoumarin
show the reaction diagram
-
-
-
-
?
Pro-Phe-Arg-4-methylcoumarin-7-amide + H2O
Pro-Phe-Arg + 7-amino-4-methylcoumarin
show the reaction diagram
-
9% of the activity with Nalpha-tert-butoxycarbonyl-Phe-Ser-Arg-4-methylcoumarin-7-amide
-
-
?
Pyr-Gly-Arg-4-methylcoumarin-7-amide + H2O
Pyr-Gly-Arg + 7-amino-4-methylcoumarin
show the reaction diagram
-
9% of the activity with Nalpha-tert-butoxycarbonyl-Phe-Ser-Arg-4-methylcoumarin-7-amide
-
-
?
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
gp43 + H2O
gp41 + ?
show the reaction diagram
oviductin alone is the oviductal factor responsible for converting the egg envelope to a sperm-penetrable form, via an increase in sperm binding. gp43 processing is the only requirement for envelope conversion
-
-
?
gp43 + H2O
gp41 + ?
show the reaction diagram
-
preferential cleavage at Gly-Ser-Arg373-/-glycoprotein gp43 in Xenopus laevis coelemic egg envelope to yield gp41. Processing of gp43 causes physical changes in the egg envelope which occurs during egg transit through the oxiduct
-
-
?
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Ca2+
-
38% stimulation at 10 mM. 11% stimulation at 100 mM
KCl
-
maximal activity in 200-400 mM solution of monovalent salts is 200% of that in absence of added salt
LiCl
-
maximal activity in 200-400 mM solution of monovalent salts is 200% of that in absence of added salt
NaCl
-
maximal activity in 200-400 mM solution of monovalent salts is 200% of that in absence of added salt
NaF
-
maximal activity in 200-400 mM solution of monovalent salts is 200% of that in absence of added salt
NaNO3
-
maximal activity in 200-400 mM solution of monovalent salts is 200% of that in absence of added salt
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
antipain
-
0.05 mM, 35% inhibition
Aprotinin
-
0.05 mM, 97% inhibition
diisopropyl fluorophosphate
-
0.05 mM, 37% inhibition. Rapid and irreverible
EDTA
-
0.05 mM, 90% inhibition
EGTA
-
0.05 mM, 94% inhibition
guanidine hydrochloride
-
competitive
leupeptin
-
0.05 mM, 55% inhibition
p-aminobenzamidine
-
competitive
Soybean trypsin inhibitor
-
0.0025 mM, 84% inhibition
-
additional information
-
no inhibition by iodoacetamide, E-64, pepstatin or 1,10-phenanthroline
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.058
Nalpha-tert-butoxycarbonylphenylalanylserylarginyl-7-amido-4-methylcoumarin
-
-
-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
3.8
Nalpha-tert-butoxycarbonylphenylalanylserylarginyl-7-amido-4-methylcoumarin
-
-
-
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0075
guanidine hydrochloride
-
-
0.0041
p-aminobenzamidine
-
-
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
8
-
Nalpha-tert-butoxycarbonylphenylalanylserylarginyl-4-methylcoumarin-7-amide
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7.5 - 8.5
-
more than 90% of maximal activity at pH 7.5 and at pH 8.5, less than 30% of maximal activity below pH 6.5
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
Uniprot
Manually annotated by BRENDA team
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
-
secretory granules
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
OVCH2_XENLA
1004
0
110612
Swiss-Prot
Secretory Pathway (Reliability: 2)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
66000
-
x * 66000, SDS-PAGE under both nonreducing and reducing conditions
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
?
-
x * 66000, SDS-PAGE under both nonreducing and reducing conditions
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
proteolytic modification
protease is translated as the N terminus of an unusual mosaic protein. It is proposed that during post-translational proteolytic processing of the mosaic oviductin glycoprotein, the processed N-terminal protease domain is released coupled to two C-terminal CUB domains and constitutes the enzymatically active protease molecule
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
relatively stable to rapid freezing in the presence of 20% glycerol. 90% of the activity remains after each freeze-thaw cycle
-
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Hardy, D.M.; Hedrick, J.L.
Oviductin. Purification and properties of the oviductal protease that processes the molecular weight 43000 glycoprotein of the Xenopus laevis egg envelope
Biochemistry
31
4466-4472
1992
Xenopus laevis
Manually annotated by BRENDA team
Lindsay, L.L.; Wieduwilt, M.J.; Hedrick, J.L.
Oviductin, the Xenopus laevis oviductal protease that processes egg envelope glycoprotein gp43, increases sperm binding to envelopes, and is translated as part of an unusual mosaic protein composed of two protease and several CUB domains
Biol. Reprod.
60
989-995
1999
Xenopus laevis (P79953), Xenopus laevis
Manually annotated by BRENDA team