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Synonyms
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epoxidase, phylloquinone
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oxygenase, phylloquinone mono- (2,3-epoxidizing)
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phylloquinone epoxidase
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vitamin K 2,3-epoxidase
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vitamin K epoxidase
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phylloquinone + reduced acceptor + O2 = 2,3-epoxyphylloquinone + acceptor + H2O
phylloquinone + reduced acceptor + O2 = 2,3-epoxyphylloquinone + acceptor + H2O
enzyme has two distinct functions: vitamin K epoxidation and gamma-glutamyl carboxylation
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phylloquinone + reduced acceptor + O2 = 2,3-epoxyphylloquinone + acceptor + H2O
propeptide and glutamate-containing substrates bound to the vitamin K-dependent carboxylase convert its vitamin K epoxidase function from an inactive to an active state
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phylloquinone + reduced acceptor + O2 = 2,3-epoxyphylloquinone + acceptor + H2O
enzyme linked to the vitamin K dependent carboxylation system
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phylloquinone + reduced acceptor + O2 = 2,3-epoxyphylloquinone + acceptor + H2O
enzyme linked to the vitamin K dependent carboxylation system
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phylloquinone + reduced acceptor + O2 = 2,3-epoxyphylloquinone + acceptor + H2O
vitamin K-dependent carboxylase activity and vitamin K epoxidase activity are properties of the same protein
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phylloquinone + reduced acceptor + O2 = 2,3-epoxyphylloquinone + acceptor + H2O
K218 is the essential base that deprotonates AH2 to initiate he reaction
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phylloquinone + reduced acceptor + O2 = 2,3-epoxyphylloquinone + acceptor + H2O
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phylloquinone,hydrogen-donor:oxygen oxidoreductase (2,3-epoxidizing)
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Phe-Leu-Glu-Glu-Leu + reduced acceptor + O2
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Substrates: -
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phylloquinone + electron donor + O2
2,3-epoxyphylloquinone + oxidized electron + H2O
phylloquinone + electron donor + O2
2,3-epoxyphylloquinone + oxidized electron donor + H2O
additional information
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phylloquinone + electron donor + O2
2,3-epoxyphylloquinone + oxidized electron + H2O
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Substrates: -
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phylloquinone + electron donor + O2
2,3-epoxyphylloquinone + oxidized electron + H2O
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Substrates: -
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phylloquinone + electron donor + O2
2,3-epoxyphylloquinone + oxidized electron + H2O
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Substrates: -
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phylloquinone + electron donor + O2
2,3-epoxyphylloquinone + oxidized electron donor + H2O
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Substrates: -
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phylloquinone + electron donor + O2
2,3-epoxyphylloquinone + oxidized electron donor + H2O
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Substrates: -
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phylloquinone + electron donor + O2
2,3-epoxyphylloquinone + oxidized electron donor + H2O
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Substrates: -
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phylloquinone + electron donor + O2
2,3-epoxyphylloquinone + oxidized electron donor + H2O
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Substrates: vitamin K1, enzyme involved in vitamin K dependent prothrombin synthesis
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phylloquinone + electron donor + O2
2,3-epoxyphylloquinone + oxidized electron donor + H2O
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Substrates: -
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additional information
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Substrates: electron donor: NADH
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additional information
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Substrates: enzyme shows epoxidase, but no carboxylase activity. In the absence of glutamine, the enzyme shows unfettered epoxidation
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additional information
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Substrates: electron donor: NADH
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additional information
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Substrates: NADH or NADPH, if reduced pyridine nucleotides are provided, no cytosolic component is required
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additional information
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Substrates: NADH or NADPH, if reduced pyridine nucleotides are provided, no cytosolic component is required
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additional information
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Substrates: electron donor: NADPH
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additional information
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Substrates: electron donor: NADPH
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phylloquinone + electron donor + O2
2,3-epoxyphylloquinone + oxidized electron + H2O
phylloquinone + electron donor + O2
2,3-epoxyphylloquinone + oxidized electron + H2O
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Substrates: -
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phylloquinone + electron donor + O2
2,3-epoxyphylloquinone + oxidized electron + H2O
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Substrates: -
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phylloquinone + electron donor + O2
2,3-epoxyphylloquinone + oxidized electron + H2O
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Substrates: -
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NADH
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2-chloro-3-phytyl-1,4-naphthoquinone
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glutathione peroxidase
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competitive inhibitor
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Tetrachloro-4-pyridinol
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additional information
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CN- no inhibitor
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additional information
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no inhibitors: CO and CN-
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glutamate-containing substrates
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bound to the vitamin K-dependent carboxylase converts its vitamin K epoxidase function from an inactive to an active state
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Mn2+
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activating effect is limited to peptide substrate with vicinal glutamyl residues
propeptide
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bound to the vitamin K-dependent carboxylase converts its vitamin K epoxidase function from an inactive to an active state
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Cerebral Hemorrhage
In models of intracerebral hemorrhage, rivaroxaban is superior to warfarin to limit blood brain barrier disruption and hematoma expansion.
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0.00667
Phe-Leu-Glu-Glu-Leu
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additional information
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additional information
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additional information
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additional information
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high value in the early prenatal perod of 10-30 gestational weeks
additional information
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maximum enzyme activity requires both the microsomal and the soluble fraction
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brenda
fetus, neonate, 1-18 years
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brenda
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brenda
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250-300 g
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7- to 10-day old rats
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Holtzman strain, male rats
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brenda
homozygous warfarin-resistent rats
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brenda
rats of a Sprague-Dawley-derived strain, 8-10 weeks old male and female rats
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brenda
Sprague-Dawley strain, fasted male rats, 250 - 350 g
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brenda
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brenda
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obtained at autopsy
brenda
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brenda
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brenda
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microsomal recombinant protein preparation from chinese hamster ovary cells
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brenda
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solubilized microsomal recombinant protein preparation from baculovirus-infected Spodoptera frugiperda cells
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brenda
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brenda
Highest Expressing Human Cell Lines
Filter by:
Cell Line Links
Gene Links
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77000
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x * 77000, SDS-PAGE
94000
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x * 94000, SDS-PAGE, wild type enzyme
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x * 77000, SDS-PAGE
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x * 94000, SDS-PAGE, wild type enzyme
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H160A
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94% of wild-type activity
H287A
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163% of wild-type activity
H381A
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142% of wild-type activity
K218A
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no residual activity, but exogenous amines restore activity and its degree depends on the basicity of the amine
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preincubation for 15 min at 37°C results in an almost complete inhibition of the epoxidation
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stable for several days when left on ice, freezing and thawing destroys the activity
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-20°C, lyophilized, stable for up to 1 month
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-80°C, soluble enzyme preparation, at least 5% glycerol, stable to multiple freeze and thaw cycles
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partially
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expressed in chinese hamster ovary cells CHO-Dukx-B11
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wild-type and mutants of bovine enzyme species expressed in baculovirus-infected Spodoptera frugiperda cells
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wild-type and mutants of bovine enzyme species expressed in chinese hamster ovary cells CHO-Dukx-B11
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Willingham, A.K.; Matschiner, J.T.
Changes in phylloquinone epoxidase activity related to prothrombin synthesis and microsomal clotting activity in the rat
Biochem. J.
140
435-441
1974
Rattus norvegicus
brenda
Suttie, J.W.; Geweke, L.O.; Martin, S.L.; Willingham, A.K.
Vitamin K epoxidase: dependence of epoxidase activity on substrates of the vitamin K-dependent carboxylation reaction
FEBS Lett.
109
267-270
1980
Rattus norvegicus
brenda
DeMetz, M.; Soute, B.A.M.; Hemker, H.C.; Vermeer, C.
The inhibition of vitamin K-dependent carboxylase by cyanide
FEBS Lett.
137
253-256
1982
Bos taurus
brenda
Larson, A.E.; Suttie, J.W.
Vitamin K-dependent carboxylase: evidence for a hydroperoxide intermediate in the reaction
Proc. Natl. Acad. Sci. USA
75
5413-5416
1978
Rattus norvegicus
brenda
Sadowski, J.A.; Schnoes, H.K.; Suttie, J.W.
Vitamin K epoxidase: properties and relationship to prothrombin synthesis
Biochemistry
16
3856-3863
1977
Rattus norvegicus
brenda
Wallin, R.; Suttie, J.W.
Vitamin K-dependent carboxylase: evidence for cofractionation of carboxylase and epoxidase activities, and for carboxylation of a high-molecular-weight microsomal protein
Arch. Biochem. Biophys.
214
155-163
1982
Rattus norvegicus
brenda
McTigue, J.J.; Suttie, J.W.
Oxygen dependence of vitamin K-dependent carboxylase and vitamin K epoxidase
FEBS Lett.
200
71-75
1986
Rattus norvegicus
brenda
Hubbard, B.R.; Ulrich, M.M.W.; Jacobs, M.; Vermeer, C.; Walsh, C.; Furie, B.; Furie, B.C.
Vitamin K-dependent carboxylase: affinity purification from bovine liver by using a synthetic propeptide containing the gamma-carboxylation recognition site
Proc. Natl. Acad. Sci. USA
86
6893-6897
1989
Bos taurus
brenda
Roth, D.A.; Whirl, M.L.; Velazquez-Estades, L.J.; Walsh, C.T.; Furie, B.; Furie, B.C.
Mutagenesis of vitamin K-dependent carboxylase demonstrates a carboxyl terminus-mediated interaction with vitamin K hydroquinone
J. Biol. Chem.
270
5305-5311
1995
Bos taurus
brenda
Sugiura, I.; Furie, B.; Walsh, C.T.; Furie, B.C.
Profactor IX propeptide and glutamate substrate binding sites on the vitamin K-dependent carboxylase identified by site-directed mutagenesis
J. Biol. Chem.
271
17837-17844
1996
Bos taurus
brenda
Sugiura, I.; Furie, B.; Walsh, C.T.; Furie, B.C.
Propeptide and glutamate-containing substrates bound to the vitamin K-dependent carboxylase convert its vitamin K epoxidase function from an inactive to an active state
Proc. Natl. Acad. Sci. USA
94
9069-9074
1997
Bos taurus
brenda
Itoh, S.; Onishi, S.
Developmental changes of vitamin K epoxidase and reductase activities involved in the vitamin K cycle in human liver
Early Hum. Dev.
57
15-23
2000
Homo sapiens
brenda
Rishavy, M.A.; Hallgren, K.W.; Yakubenko, A.V.; Shtofman, R.L.; Runge, K.W.; Berkner, K.L.
Bronsted analysis reveals Lys218 as the carboxylase active site base that deprotonates vitamin K hydroquinone to initiate vitamin K-dependent protein carboxylation
Biochemistry
45
13239-13248
2006
Leptospira interrogans
brenda
Rishavy, M.A.; Hallgren, K.W.; Yakubenko, A.V.; Zuerner, R.L.; Runge, K.W.; Berkner, K.L.
The vitamin K-dependent carboxylase has been acquired by Leptospira pathogens and shows altered activity that suggests a role other than protein carboxylation
J. Biol. Chem.
280
34870-34877
2005
Leptospira interrogans
brenda
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