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2,3-epoxy-2,3-dihydro-2-methyl-3-phytyl-1,4-naphthoquinone + 1,4-dithiothreitol
2-hydroxy-2-methyl-3-phytyl-2,3-dihydronaphthoquinone + oxidized dithiothreitol
2,3-epoxy-2,3-dihydro-2-methyl-3-phytyl-1,4-naphthoquinone + 1,4-dithiothreitol + H2O
2-methyl-3-phytyl-1,4-naphthoquinone + oxidized dithiothreitol
2,3-epoxy-2-methyl-3-phytyl-2,3-dihydro-1,4-naphthoquinone + 1,4-dithiothreitol
vitamin K + oxidized dithiothreitol + H2O
-
-
-
?
2,3-epoxy-2-methyl-3-phytyl-2,3-dihydro-1,4-naphthoquinone + tris(3-hydroxypropyl)phosphine
?
by replacing dithiothreitol with tris(3-hydroxypropyl)phosphine and replacing imidazole with phosphate as pH buffer, all nonenzymatic side reactions are effectively eliminated and accurate measurement of enzymatic activity in vitro is possible
-
-
?
2,3-epoxyphylloquinone + 1,4-dithiothreitol
phylloquinone + oxidized dithiothreitol
2,3-epoxyphylloquinone + AH2
phylloquinone + A + ?
2,3-epoxyphylloquinone + reduced thioredoxin
phylloquinone + oxidized thioredoxin
-
-
-
-
?
2-hydroxymethyl-vitamin K 2,3-epoxide + dithiothreitol
2-hydroxymethyl-vitamin K + oxidized dithiothreitol
2-methyl-3-phytyl-1,4-naphthoquinone + dithiothreitol
vitamin K hydroquinone + oxidized dithiothreitol
-
i.e. vitamin K
-
-
?
2-methyl-3-phytyl-1,4-naphthoquinone + oxidized dithiothreitol
2,3-epoxy-2,3-dihydro-2-methyl-3-phytyl-1,4-naphthoquinone + 1,4-dithiothreitol
-
-
-
-
?
2-methyl-3-phytyl-1,4-naphthoquinone + oxidized dithiothreitol + H2O
2,3-epoxy-2,3-dihydro-2-methyl-3-phytyl-1,4-naphthoquinone + 1,4-dithiothreitol
allylbenzene 2',3'-oxide + 1,4-dithiothreitol
allylbenzene + oxidized dithiothreitol
-
-
-
?
styrene 1',2'-oxide + 1,4-dithiothreitol
styrene + oxidized dithiothreitol
-
-
-
?
vitamin K + 1,4-dithiothreitol
vitamin K hydroquinone + oxidized dithiothreitol + H2O
-
-
-
?
vitamin K 2,3-epoxide + dithiothreitol
vitamin K + oxidized dithiothreitol
vitamin K 2,3-epoxide + oxidized dithiothreitol
vitamin K + 1,4-dithiothreitol
-
-
-
-
ir
vitamin K 2,3-epoxide + reduced dithiothreitol
vitamin K quinone + oxidized dithiothreitol + H2O
vitamin K 2,3-epoxide analogs + dithiothreitol
?
vitamin K1 2,3-epoxide + dithiothreitol
vitamin K1 + oxidized dithiothreitol
additional information
?
-
2,3-epoxy-2,3-dihydro-2-methyl-3-phytyl-1,4-naphthoquinone + 1,4-dithiothreitol
2-hydroxy-2-methyl-3-phytyl-2,3-dihydronaphthoquinone + oxidized dithiothreitol
-
-
-
?
2,3-epoxy-2,3-dihydro-2-methyl-3-phytyl-1,4-naphthoquinone + 1,4-dithiothreitol
2-hydroxy-2-methyl-3-phytyl-2,3-dihydronaphthoquinone + oxidized dithiothreitol
-
i.e. vitamin K 2,3-epoxide
i.e. vitamin K
-
?
2,3-epoxy-2,3-dihydro-2-methyl-3-phytyl-1,4-naphthoquinone + 1,4-dithiothreitol
2-hydroxy-2-methyl-3-phytyl-2,3-dihydronaphthoquinone + oxidized dithiothreitol
-
i.e. vitamin K 2,3-epoxide
i.e. vitamin K, an important cofactor for the posttranslational gamma-carboxylation of several blood coagulation factors
-
?
2,3-epoxy-2,3-dihydro-2-methyl-3-phytyl-1,4-naphthoquinone + 1,4-dithiothreitol
2-hydroxy-2-methyl-3-phytyl-2,3-dihydronaphthoquinone + oxidized dithiothreitol
-
i.e. vitamin K 2,3-epoxide, the enzyme initiates the vitamin K catalytic cycle, overview
i.e. vitamin K
-
?
2,3-epoxy-2,3-dihydro-2-methyl-3-phytyl-1,4-naphthoquinone + 1,4-dithiothreitol
2-hydroxy-2-methyl-3-phytyl-2,3-dihydronaphthoquinone + oxidized dithiothreitol
-
i.e. vitamin K 2,3-epoxide, two dithiol-dependent steps
i.e. vitamin K
-
?
2,3-epoxy-2,3-dihydro-2-methyl-3-phytyl-1,4-naphthoquinone + 1,4-dithiothreitol
2-hydroxy-2-methyl-3-phytyl-2,3-dihydronaphthoquinone + oxidized dithiothreitol
-
i.e. vitamin K 2,3-epoxide
i.e. vitamin K
-
?
2,3-epoxy-2,3-dihydro-2-methyl-3-phytyl-1,4-naphthoquinone + 1,4-dithiothreitol
2-hydroxy-2-methyl-3-phytyl-2,3-dihydronaphthoquinone + oxidized dithiothreitol
-
i.e. vitamin K 2,3-epoxide
i.e. vitamin K
-
?
2,3-epoxy-2,3-dihydro-2-methyl-3-phytyl-1,4-naphthoquinone + 1,4-dithiothreitol
2-hydroxy-2-methyl-3-phytyl-2,3-dihydronaphthoquinone + oxidized dithiothreitol
-
-
-
?
2,3-epoxy-2,3-dihydro-2-methyl-3-phytyl-1,4-naphthoquinone + 1,4-dithiothreitol
2-hydroxy-2-methyl-3-phytyl-2,3-dihydronaphthoquinone + oxidized dithiothreitol
-
-
-
?
2,3-epoxy-2,3-dihydro-2-methyl-3-phytyl-1,4-naphthoquinone + 1,4-dithiothreitol
2-hydroxy-2-methyl-3-phytyl-2,3-dihydronaphthoquinone + oxidized dithiothreitol
-
-
-
?
2,3-epoxy-2,3-dihydro-2-methyl-3-phytyl-1,4-naphthoquinone + 1,4-dithiothreitol
2-hydroxy-2-methyl-3-phytyl-2,3-dihydronaphthoquinone + oxidized dithiothreitol
-
-
-
?
2,3-epoxy-2,3-dihydro-2-methyl-3-phytyl-1,4-naphthoquinone + 1,4-dithiothreitol
2-hydroxy-2-methyl-3-phytyl-2,3-dihydronaphthoquinone + oxidized dithiothreitol
-
-
-
?
2,3-epoxy-2,3-dihydro-2-methyl-3-phytyl-1,4-naphthoquinone + 1,4-dithiothreitol
2-hydroxy-2-methyl-3-phytyl-2,3-dihydronaphthoquinone + oxidized dithiothreitol
-
i.e. vitamin K 2,3-epoxide
i.e. 3-hydroxy-2,3-dihydro-vitamin K
?
2,3-epoxy-2,3-dihydro-2-methyl-3-phytyl-1,4-naphthoquinone + 1,4-dithiothreitol
2-hydroxy-2-methyl-3-phytyl-2,3-dihydronaphthoquinone + oxidized dithiothreitol
-
i.e. vitamin K 2,3-epoxide
i.e. 3-hydroxy-2,3-dihydro-vitamin K
?
2,3-epoxy-2,3-dihydro-2-methyl-3-phytyl-1,4-naphthoquinone + 1,4-dithiothreitol
2-hydroxy-2-methyl-3-phytyl-2,3-dihydronaphthoquinone + oxidized dithiothreitol
-
i.e. vitamin K 2,3-epoxide
i.e. 3-hydroxy-2,3-dihydro-vitamin K
?
2,3-epoxy-2,3-dihydro-2-methyl-3-phytyl-1,4-naphthoquinone + 1,4-dithiothreitol
2-hydroxy-2-methyl-3-phytyl-2,3-dihydronaphthoquinone + oxidized dithiothreitol
-
i.e. vitamin K 2,3-epoxide
i.e. vitamin K
-
?
2,3-epoxy-2,3-dihydro-2-methyl-3-phytyl-1,4-naphthoquinone + 1,4-dithiothreitol
2-hydroxy-2-methyl-3-phytyl-2,3-dihydronaphthoquinone + oxidized dithiothreitol
i.e. vitamin K 2,3-epoxide
i.e. vitamin K
-
?
2,3-epoxy-2,3-dihydro-2-methyl-3-phytyl-1,4-naphthoquinone + 1,4-dithiothreitol
2-hydroxy-2-methyl-3-phytyl-2,3-dihydronaphthoquinone + oxidized dithiothreitol
-
i.e. vitamin K 2,3-epoxide
i.e. vitamin K
-
?
2,3-epoxy-2,3-dihydro-2-methyl-3-phytyl-1,4-naphthoquinone + 1,4-dithiothreitol
2-hydroxy-2-methyl-3-phytyl-2,3-dihydronaphthoquinone + oxidized dithiothreitol
-
i.e. vitamin K 2,3-epoxide, the enzyme is supposed to catalyze the reduction of the epoxide to quinone and of the quinone to vitamin K hydroquinone
-
?
2,3-epoxy-2,3-dihydro-2-methyl-3-phytyl-1,4-naphthoquinone + 1,4-dithiothreitol
2-hydroxy-2-methyl-3-phytyl-2,3-dihydronaphthoquinone + oxidized dithiothreitol
-
-
-
?
2,3-epoxy-2,3-dihydro-2-methyl-3-phytyl-1,4-naphthoquinone + 1,4-dithiothreitol
2-hydroxy-2-methyl-3-phytyl-2,3-dihydronaphthoquinone + oxidized dithiothreitol
-
i.e. vitamin K 2,3-epoxide
i.e. 3-hydroxy-2,3-dihydro-vitamin K
?
2,3-epoxy-2,3-dihydro-2-methyl-3-phytyl-1,4-naphthoquinone + 1,4-dithiothreitol
2-hydroxy-2-methyl-3-phytyl-2,3-dihydronaphthoquinone + oxidized dithiothreitol
-
-
-
?
2,3-epoxy-2,3-dihydro-2-methyl-3-phytyl-1,4-naphthoquinone + 1,4-dithiothreitol
2-hydroxy-2-methyl-3-phytyl-2,3-dihydronaphthoquinone + oxidized dithiothreitol
-
i.e. vitamin K 2,3-epoxide
i.e. 3-hydroxy-2,3-dihydro-vitamin K
?
2,3-epoxy-2,3-dihydro-2-methyl-3-phytyl-1,4-naphthoquinone + 1,4-dithiothreitol
2-hydroxy-2-methyl-3-phytyl-2,3-dihydronaphthoquinone + oxidized dithiothreitol
-
-
-
?
2,3-epoxy-2,3-dihydro-2-methyl-3-phytyl-1,4-naphthoquinone + 1,4-dithiothreitol
2-hydroxy-2-methyl-3-phytyl-2,3-dihydronaphthoquinone + oxidized dithiothreitol
-
i.e. vitamin K 2,3-epoxide
i.e. 3-hydroxy-2,3-dihydro-vitamin K
?
2,3-epoxy-2,3-dihydro-2-methyl-3-phytyl-1,4-naphthoquinone + 1,4-dithiothreitol
2-hydroxy-2-methyl-3-phytyl-2,3-dihydronaphthoquinone + oxidized dithiothreitol
-
-
-
?
2,3-epoxy-2,3-dihydro-2-methyl-3-phytyl-1,4-naphthoquinone + 1,4-dithiothreitol + H2O
2-methyl-3-phytyl-1,4-naphthoquinone + oxidized dithiothreitol
-
-
-
-
r
2,3-epoxy-2,3-dihydro-2-methyl-3-phytyl-1,4-naphthoquinone + 1,4-dithiothreitol + H2O
2-methyl-3-phytyl-1,4-naphthoquinone + oxidized dithiothreitol
-
-
-
-
r
2,3-epoxy-2,3-dihydro-2-methyl-3-phytyl-1,4-naphthoquinone + 1,4-dithiothreitol + H2O
2-methyl-3-phytyl-1,4-naphthoquinone + oxidized dithiothreitol
-
-
-
-
r
2,3-epoxy-2,3-dihydro-2-methyl-3-phytyl-1,4-naphthoquinone + 1,4-dithiothreitol + H2O
2-methyl-3-phytyl-1,4-naphthoquinone + oxidized dithiothreitol
-
-
-
-
r
2,3-epoxy-2,3-dihydro-2-methyl-3-phytyl-1,4-naphthoquinone + 1,4-dithiothreitol + H2O
2-methyl-3-phytyl-1,4-naphthoquinone + oxidized dithiothreitol
-
-
-
?, r
2,3-epoxy-2,3-dihydro-2-methyl-3-phytyl-1,4-naphthoquinone + 1,4-dithiothreitol + H2O
2-methyl-3-phytyl-1,4-naphthoquinone + oxidized dithiothreitol
-
-
-
-
r
2,3-epoxy-2,3-dihydro-2-methyl-3-phytyl-1,4-naphthoquinone + 1,4-dithiothreitol + H2O
2-methyl-3-phytyl-1,4-naphthoquinone + oxidized dithiothreitol
-
-
-
-
r
2,3-epoxy-2,3-dihydro-2-methyl-3-phytyl-1,4-naphthoquinone + 1,4-dithiothreitol + H2O
2-methyl-3-phytyl-1,4-naphthoquinone + oxidized dithiothreitol
-
-
-
-
r
2,3-epoxyphylloquinone + 1,4-dithiothreitol
phylloquinone + oxidized dithiothreitol
-
-
-
-
?
2,3-epoxyphylloquinone + 1,4-dithiothreitol
phylloquinone + oxidized dithiothreitol
-
-
-
?
2,3-epoxyphylloquinone + AH2
phylloquinone + A + ?
-
-
-
-
?
2,3-epoxyphylloquinone + AH2
phylloquinone + A + ?
-
VKOR reduces vitamin K using membrane-embedded thiols, Cys132 and Cys135, which become oxidized with concomitant VKOR inactivation. VKOR is subsequently reactivated by an unknown redox protein that might act directly on the Cys132-Cys135 residues
-
-
?
2,3-epoxyphylloquinone + AH2
phylloquinone + A + ?
the enzyme catalyzes the reduction of vitamin K 2,3-epoxide to vitamin K1, overview
-
-
?
2-hydroxymethyl-vitamin K 2,3-epoxide + dithiothreitol
2-hydroxymethyl-vitamin K + oxidized dithiothreitol
-
-
-
?
2-hydroxymethyl-vitamin K 2,3-epoxide + dithiothreitol
2-hydroxymethyl-vitamin K + oxidized dithiothreitol
-
-
-
?
2-methyl-3-phytyl-1,4-naphthoquinone + oxidized dithiothreitol + H2O
2,3-epoxy-2,3-dihydro-2-methyl-3-phytyl-1,4-naphthoquinone + 1,4-dithiothreitol
-
-
-
-
r
2-methyl-3-phytyl-1,4-naphthoquinone + oxidized dithiothreitol + H2O
2,3-epoxy-2,3-dihydro-2-methyl-3-phytyl-1,4-naphthoquinone + 1,4-dithiothreitol
-
-
-
-
r
2-methyl-3-phytyl-1,4-naphthoquinone + oxidized dithiothreitol + H2O
2,3-epoxy-2,3-dihydro-2-methyl-3-phytyl-1,4-naphthoquinone + 1,4-dithiothreitol
-
-
-
-
r
2-methyl-3-phytyl-1,4-naphthoquinone + oxidized dithiothreitol + H2O
2,3-epoxy-2,3-dihydro-2-methyl-3-phytyl-1,4-naphthoquinone + 1,4-dithiothreitol
-
-
-
-
r
2-methyl-3-phytyl-1,4-naphthoquinone + oxidized dithiothreitol + H2O
2,3-epoxy-2,3-dihydro-2-methyl-3-phytyl-1,4-naphthoquinone + 1,4-dithiothreitol
-
-
-
-
?
2-methyl-3-phytyl-1,4-naphthoquinone + oxidized dithiothreitol + H2O
2,3-epoxy-2,3-dihydro-2-methyl-3-phytyl-1,4-naphthoquinone + 1,4-dithiothreitol
-
-
-
-
r
2-methyl-3-phytyl-1,4-naphthoquinone + oxidized dithiothreitol + H2O
2,3-epoxy-2,3-dihydro-2-methyl-3-phytyl-1,4-naphthoquinone + 1,4-dithiothreitol
-
-
-
?
2-methyl-3-phytyl-1,4-naphthoquinone + oxidized dithiothreitol + H2O
2,3-epoxy-2,3-dihydro-2-methyl-3-phytyl-1,4-naphthoquinone + 1,4-dithiothreitol
-
-
-
?
2-methyl-3-phytyl-1,4-naphthoquinone + oxidized dithiothreitol + H2O
2,3-epoxy-2,3-dihydro-2-methyl-3-phytyl-1,4-naphthoquinone + 1,4-dithiothreitol
-
-
-
r
2-methyl-3-phytyl-1,4-naphthoquinone + oxidized dithiothreitol + H2O
2,3-epoxy-2,3-dihydro-2-methyl-3-phytyl-1,4-naphthoquinone + 1,4-dithiothreitol
-
crucial role of the Tyr-139 amino acid in this reaction mechanism, Tyr-139 residue appears to determine the second half-step of the catalytic mechanism
-
-
r
2-methyl-3-phytyl-1,4-naphthoquinone + oxidized dithiothreitol + H2O
2,3-epoxy-2,3-dihydro-2-methyl-3-phytyl-1,4-naphthoquinone + 1,4-dithiothreitol
-
-
-
-
?
2-methyl-3-phytyl-1,4-naphthoquinone + oxidized dithiothreitol + H2O
2,3-epoxy-2,3-dihydro-2-methyl-3-phytyl-1,4-naphthoquinone + 1,4-dithiothreitol
-
-
-
?
2-methyl-3-phytyl-1,4-naphthoquinone + oxidized dithiothreitol + H2O
2,3-epoxy-2,3-dihydro-2-methyl-3-phytyl-1,4-naphthoquinone + 1,4-dithiothreitol
-
-
-
-
r
2-methyl-3-phytyl-1,4-naphthoquinone + oxidized dithiothreitol + H2O
2,3-epoxy-2,3-dihydro-2-methyl-3-phytyl-1,4-naphthoquinone + 1,4-dithiothreitol
reduction of vitamin K 2,3-epoxide to vitamin K
-
-
?
2-methyl-3-phytyl-1,4-naphthoquinone + oxidized dithiothreitol + H2O
2,3-epoxy-2,3-dihydro-2-methyl-3-phytyl-1,4-naphthoquinone + 1,4-dithiothreitol
-
-
-
-
r
vitamin K 2,3-epoxide + dithiothreitol
vitamin K + oxidized dithiothreitol
-
-
-
?
vitamin K 2,3-epoxide + dithiothreitol
vitamin K + oxidized dithiothreitol
-
-
-
?
vitamin K 2,3-epoxide + dithiothreitol
vitamin K + oxidized dithiothreitol
-
-
-
?
vitamin K 2,3-epoxide + dithiothreitol
vitamin K + oxidized dithiothreitol
-
-
-
?
vitamin K 2,3-epoxide + dithiothreitol
vitamin K + oxidized dithiothreitol
-
-
-
?
vitamin K 2,3-epoxide + dithiothreitol
vitamin K + oxidized dithiothreitol
-
-
-
-
?
vitamin K 2,3-epoxide + dithiothreitol
vitamin K + oxidized dithiothreitol
-
-
-
-
?
vitamin K 2,3-epoxide + dithiothreitol
vitamin K + oxidized dithiothreitol
-
-
-
-
?
vitamin K 2,3-epoxide + dithiothreitol
vitamin K + oxidized dithiothreitol
-
-
-
?
vitamin K 2,3-epoxide + dithiothreitol
vitamin K + oxidized dithiothreitol
-
-
-
?
vitamin K 2,3-epoxide + dithiothreitol
vitamin K + oxidized dithiothreitol
-
-
-
?
vitamin K 2,3-epoxide + dithiothreitol
vitamin K + oxidized dithiothreitol
-
-
-
?
vitamin K 2,3-epoxide + dithiothreitol
vitamin K + oxidized dithiothreitol
-
-
-
?
vitamin K 2,3-epoxide + dithiothreitol
vitamin K + oxidized dithiothreitol
-
-
-
?
vitamin K 2,3-epoxide + dithiothreitol
vitamin K + oxidized dithiothreitol
-
-
-
?
vitamin K 2,3-epoxide + dithiothreitol
vitamin K + oxidized dithiothreitol
-
-
-
?
vitamin K 2,3-epoxide + dithiothreitol
vitamin K + oxidized dithiothreitol
-
-
-
?
vitamin K 2,3-epoxide + dithiothreitol
vitamin K + oxidized dithiothreitol
-
-
-
?
vitamin K 2,3-epoxide + dithiothreitol
vitamin K + oxidized dithiothreitol
-
-
-
-
?
vitamin K 2,3-epoxide + dithiothreitol
vitamin K + oxidized dithiothreitol
-
2-mercaptoethanol, reduced glutathione, cysteine and 1,6-hexanedithiol are inactive as acceptors
-
?
vitamin K 2,3-epoxide + dithiothreitol
vitamin K + oxidized dithiothreitol
-
substrate vitamin K 2,3-epoxide, in the presence of 0.0017 mM R,S-warfarin
-
?
vitamin K 2,3-epoxide + dithiothreitol
vitamin K + oxidized dithiothreitol
-
thioredoxin is the possible physiological electron acceptor
-
?
vitamin K 2,3-epoxide + dithiothreitol
vitamin K + oxidized dithiothreitol
-
reaction in metabolic pathway of vitamin K
-
?
vitamin K 2,3-epoxide + dithiothreitol
vitamin K + oxidized dithiothreitol
-
-
-
?
vitamin K 2,3-epoxide + dithiothreitol
vitamin K + oxidized dithiothreitol
-
-
-
?
vitamin K 2,3-epoxide + dithiothreitol
vitamin K + oxidized dithiothreitol
-
-
-
?
vitamin K 2,3-epoxide + dithiothreitol
vitamin K + oxidized dithiothreitol
-
-
-
?
vitamin K 2,3-epoxide + dithiothreitol
vitamin K + oxidized dithiothreitol
-
-
-
?
vitamin K 2,3-epoxide + dithiothreitol
vitamin K + oxidized dithiothreitol
-
2-mercaptoethanol, reduced glutathione, cysteine and 1,6-hexanedithiol are inactive as acceptors
-
?
vitamin K 2,3-epoxide + dithiothreitol
vitamin K + oxidized dithiothreitol
-
reaction in metabolic pathway of vitamin K
-
?
vitamin K 2,3-epoxide + dithiothreitol
vitamin K + oxidized dithiothreitol
-
-
-
?
vitamin K 2,3-epoxide + dithiothreitol
vitamin K + oxidized dithiothreitol
-
thioredoxin is the possible physiological electron acceptor
-
?
vitamin K 2,3-epoxide + reduced dithiothreitol
vitamin K quinone + oxidized dithiothreitol + H2O
-
-
-
-
r
vitamin K 2,3-epoxide + reduced dithiothreitol
vitamin K quinone + oxidized dithiothreitol + H2O
-
-
-
-
r
vitamin K 2,3-epoxide analogs + dithiothreitol
?
-
such as hydroxymethyl-, chloromethyl-, fluoromethyl-, difluoromethyl-, and formyl-analogs
-
-
?
vitamin K 2,3-epoxide analogs + dithiothreitol
?
-
such as hydroxymethyl-, chloromethyl-, fluoromethyl-, difluoromethyl-, and formyl-analogs
-
-
?
vitamin K1 2,3-epoxide + dithiothreitol
vitamin K1 + oxidized dithiothreitol
-
-
-
-
?
vitamin K1 2,3-epoxide + dithiothreitol
vitamin K1 + oxidized dithiothreitol
-
-
-
-
?
vitamin K1 2,3-epoxide + dithiothreitol
vitamin K1 + oxidized dithiothreitol
-
-
-
-
?
vitamin K1 2,3-epoxide + dithiothreitol
vitamin K1 + oxidized dithiothreitol
-
-
-
-
?
vitamin K1 2,3-epoxide + dithiothreitol
vitamin K1 + oxidized dithiothreitol
-
-
-
?
vitamin K1 2,3-epoxide + dithiothreitol
vitamin K1 + oxidized dithiothreitol
-
-
-
-
?
vitamin K1 2,3-epoxide + dithiothreitol
vitamin K1 + oxidized dithiothreitol
-
two patients suffering from combined deficiency of vitamin K-dependent clotting factors type 2 possess a R98W substitution at the presumed cytoplasmic end of TM alpha-helix 2. Because the residue is far-removed from the proposed active site its mutation is, therefore assumed to disrupt VKORC1 structure or VKOR complex assembly rather than catalysis
-
-
?
vitamin K1 2,3-epoxide + dithiothreitol
vitamin K1 + oxidized dithiothreitol
VKORC1 contains missense mutations in the two heritable human diseases: combined deficiency of vitamin-K-dependent clotting factors type 2 (VKCFD2, Online Mendelian Inheritance in Man 607473) and resistance to coumarin-type anticoagulant drugs (warfarin resistance, WR, Online Mendelian Inheritance in man 122700)
-
-
?
vitamin K1 2,3-epoxide + dithiothreitol
vitamin K1 + oxidized dithiothreitol
-
-
-
-
?
vitamin K1 2,3-epoxide + dithiothreitol
vitamin K1 + oxidized dithiothreitol
-
-
-
-
?
vitamin K1 2,3-epoxide + dithiothreitol
vitamin K1 + oxidized dithiothreitol
-
vitamin K is an essential cofactor for post-translational gamma-carboxylation of vitamin K-dependent coagulation factors. The modification is carried out by a system of integral proteins of the endoplasmic reticulum membrane where the warfarin sensitive vitamin K 2,3-epoxide reductase (VKOR) produces the reduced hydroquinone form of vitamin K needed by the gamma-carboxylase as the active cofactor. VKOR is the rate-limiting step in the system
-
-
?
vitamin K1 2,3-epoxide + dithiothreitol
vitamin K1 + oxidized dithiothreitol
-
-
-
-
?
additional information
?
-
-
VKOR is a part of the post-translational protein-modification system that produces gamma-carboxylated proteins. The vitamin K-dependent gamma-carboxylation system consists of the vitamin K-dependent gamma-carboxylase, which requires the reduced hydroquinone form of vitamin K1 as a cofactor and the warfarin-sensitive enzyme vitamin K1 2,3-epoxide reductase, VKOR. VKOR and gamma-carboxylase are close enough together in the membrane to operate as a supramolecular assembly of proteins, in which substrates and products are shuttled efficiently from one component to the next. Calumenin is likely to have a regulatory role in controlling the activity of the system
-
-
?
additional information
?
-
-
the enzyme is involved in angiogenesis
-
-
?
additional information
?
-
-
the enzyme is involved in coagulation factor activity
-
-
?
additional information
?
-
the enzyme is involved in coagulation factor activity
-
-
?
additional information
?
-
-
the enzyme is involved in reduction of vitamin K, which is required by the gamma-glutamyl carboxylase, GGCX, transforming glutamate to gamma carboxyl glutamic acid in a vitamin K-dependent manner, gamma carboxyl glutamic acid is required for activity of proteins involved in coagulation, overview
-
-
?
additional information
?
-
-
the enzyme is involved in regulation of response to oral anticoagulants of European-American warfarin patients
-
-
?
additional information
?
-
-
the VKCFD2 disease, a vitamin K-dependent clotting factor deficiency, is caused by enzyme mutations, VKORC1 is the key component of the vitamin K reductase activity targeted by coumarin-derived drugs in prophylaxis and therapy of thrombosis
-
-
?
additional information
?
-
vitamin K epoxide reductase is the enzyme responsible for the recycling of vitamin K 2,3-epoxide to vitamin K hydroquinone, a cofactor that is essential for the synthesis of several blood coagulation factors
-
-
?
additional information
?
-
-
VKORC1 is the key gene of the vitamin K cycle encoding the molecular target of coumarin-type anticoagulants vitaminK epoxide reductase, VKORC1 recycles vitamin K 2,3-epoxide to vitamin K hydroquinone, which functions as the essential cofactor for gamma-carboxylation of gamma-carboxyl-glutamic acid-domain proteins such as coagulation factors II, VII, IX, and X, proteins C, S, and Z, osteocalcin, matrix Gla protein MGP, and Gas6, gamma-glutamyl carboxylase, GGCX, is the enzyme that accomplishes the carboxylation reaction, VKORC1 represents the rate-limiting step in the reaction
-
-
?
additional information
?
-
-
Purified vitamin K epoxide reductase alone is sufficient for conversion of vitamin K epoxide to vitamin K and vitamin K to vitamin KH2
-
-
?
additional information
?
-
-
the enzyme, driven by the reducing agent DTT, reduces both vitamin K 2,3-epoxide and vitamin K to the activated hydroquinone form
-
-
?
additional information
?
-
-
advantages and caveats of using the DTT-driven VKOR assay, overview
-
-
?
additional information
?
-
-
no synthesis of 3-hydroxyvitamin K1 by the wild-type enzyme, but by mutants Y139C, Y139F, and Y139S
-
-
?
additional information
?
-
-
VKOR is a part of the post-translational protein-modification system that produces gamma-carboxylated proteins. The vitamin K-dependent gamma-carboxylation system consists of the vitamin K-dependent gamma-carboxylase, which requires the reduced hydroquinone form of vitamin K1 as a cofactor and the warfarin-sensitive enzyme vitamin K1 2,3-epoxide reductase, VKOR. VKOR and gamma-carboxylase are close enough together in the membrane to operate as a supramolecular assembly of proteins, in which substrates and products are shuttled efficiently from one component to the next. Calumenin is likely to have a regulatory role in controlling the activity of the system
-
-
?
additional information
?
-
-
the reduction is linked to dithiol-dependent oxidative folding of proteins in the ER by protein disulfide isomerase, PDI, oxidative folding of reduced RNase triggers the reduction of vitamin K epoxid and the gamma-carboxylation of the synthetic gamma-carboxylase peptide substrate FLEEL, overview
-
-
?
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2,3-epoxy-2,3-dihydro-2-methyl-3-phytyl-1,4-naphthoquinone + 1,4-dithiothreitol
2-hydroxy-2-methyl-3-phytyl-2,3-dihydronaphthoquinone + oxidized dithiothreitol
2,3-epoxy-2,3-dihydro-2-methyl-3-phytyl-1,4-naphthoquinone + 1,4-dithiothreitol + H2O
2-methyl-3-phytyl-1,4-naphthoquinone + oxidized dithiothreitol
2,3-epoxyphylloquinone + AH2
phylloquinone + A + ?
2-methyl-3-phytyl-1,4-naphthoquinone + oxidized dithiothreitol
2,3-epoxy-2,3-dihydro-2-methyl-3-phytyl-1,4-naphthoquinone + 1,4-dithiothreitol
-
-
-
-
?
2-methyl-3-phytyl-1,4-naphthoquinone + oxidized dithiothreitol + H2O
2,3-epoxy-2,3-dihydro-2-methyl-3-phytyl-1,4-naphthoquinone + 1,4-dithiothreitol
vitamin K 2,3-epoxide + dithiothreitol
vitamin K + oxidized dithiothreitol
vitamin K1 2,3-epoxide + dithiothreitol
vitamin K1 + oxidized dithiothreitol
additional information
?
-
2,3-epoxy-2,3-dihydro-2-methyl-3-phytyl-1,4-naphthoquinone + 1,4-dithiothreitol
2-hydroxy-2-methyl-3-phytyl-2,3-dihydronaphthoquinone + oxidized dithiothreitol
-
-
-
?
2,3-epoxy-2,3-dihydro-2-methyl-3-phytyl-1,4-naphthoquinone + 1,4-dithiothreitol
2-hydroxy-2-methyl-3-phytyl-2,3-dihydronaphthoquinone + oxidized dithiothreitol
-
i.e. vitamin K 2,3-epoxide
i.e. vitamin K
-
?
2,3-epoxy-2,3-dihydro-2-methyl-3-phytyl-1,4-naphthoquinone + 1,4-dithiothreitol
2-hydroxy-2-methyl-3-phytyl-2,3-dihydronaphthoquinone + oxidized dithiothreitol
-
i.e. vitamin K 2,3-epoxide
i.e. vitamin K, an important cofactor for the posttranslational gamma-carboxylation of several blood coagulation factors
-
?
2,3-epoxy-2,3-dihydro-2-methyl-3-phytyl-1,4-naphthoquinone + 1,4-dithiothreitol
2-hydroxy-2-methyl-3-phytyl-2,3-dihydronaphthoquinone + oxidized dithiothreitol
-
i.e. vitamin K 2,3-epoxide, the enzyme initiates the vitamin K catalytic cycle, overview
i.e. vitamin K
-
?
2,3-epoxy-2,3-dihydro-2-methyl-3-phytyl-1,4-naphthoquinone + 1,4-dithiothreitol
2-hydroxy-2-methyl-3-phytyl-2,3-dihydronaphthoquinone + oxidized dithiothreitol
-
i.e. vitamin K 2,3-epoxide
i.e. vitamin K
-
?
2,3-epoxy-2,3-dihydro-2-methyl-3-phytyl-1,4-naphthoquinone + 1,4-dithiothreitol
2-hydroxy-2-methyl-3-phytyl-2,3-dihydronaphthoquinone + oxidized dithiothreitol
-
i.e. vitamin K 2,3-epoxide
i.e. vitamin K
-
?
2,3-epoxy-2,3-dihydro-2-methyl-3-phytyl-1,4-naphthoquinone + 1,4-dithiothreitol
2-hydroxy-2-methyl-3-phytyl-2,3-dihydronaphthoquinone + oxidized dithiothreitol
-
-
-
?
2,3-epoxy-2,3-dihydro-2-methyl-3-phytyl-1,4-naphthoquinone + 1,4-dithiothreitol
2-hydroxy-2-methyl-3-phytyl-2,3-dihydronaphthoquinone + oxidized dithiothreitol
-
-
-
?
2,3-epoxy-2,3-dihydro-2-methyl-3-phytyl-1,4-naphthoquinone + 1,4-dithiothreitol
2-hydroxy-2-methyl-3-phytyl-2,3-dihydronaphthoquinone + oxidized dithiothreitol
-
-
-
?
2,3-epoxy-2,3-dihydro-2-methyl-3-phytyl-1,4-naphthoquinone + 1,4-dithiothreitol
2-hydroxy-2-methyl-3-phytyl-2,3-dihydronaphthoquinone + oxidized dithiothreitol
-
-
-
?
2,3-epoxy-2,3-dihydro-2-methyl-3-phytyl-1,4-naphthoquinone + 1,4-dithiothreitol
2-hydroxy-2-methyl-3-phytyl-2,3-dihydronaphthoquinone + oxidized dithiothreitol
-
-
-
?
2,3-epoxy-2,3-dihydro-2-methyl-3-phytyl-1,4-naphthoquinone + 1,4-dithiothreitol
2-hydroxy-2-methyl-3-phytyl-2,3-dihydronaphthoquinone + oxidized dithiothreitol
-
i.e. vitamin K 2,3-epoxide
i.e. vitamin K
-
?
2,3-epoxy-2,3-dihydro-2-methyl-3-phytyl-1,4-naphthoquinone + 1,4-dithiothreitol
2-hydroxy-2-methyl-3-phytyl-2,3-dihydronaphthoquinone + oxidized dithiothreitol
i.e. vitamin K 2,3-epoxide
i.e. vitamin K
-
?
2,3-epoxy-2,3-dihydro-2-methyl-3-phytyl-1,4-naphthoquinone + 1,4-dithiothreitol
2-hydroxy-2-methyl-3-phytyl-2,3-dihydronaphthoquinone + oxidized dithiothreitol
-
i.e. vitamin K 2,3-epoxide
i.e. vitamin K
-
?
2,3-epoxy-2,3-dihydro-2-methyl-3-phytyl-1,4-naphthoquinone + 1,4-dithiothreitol
2-hydroxy-2-methyl-3-phytyl-2,3-dihydronaphthoquinone + oxidized dithiothreitol
-
i.e. vitamin K 2,3-epoxide, the enzyme is supposed to catalyze the reduction of the epoxide to quinone and of the quinone to vitamin K hydroquinone
-
?
2,3-epoxy-2,3-dihydro-2-methyl-3-phytyl-1,4-naphthoquinone + 1,4-dithiothreitol
2-hydroxy-2-methyl-3-phytyl-2,3-dihydronaphthoquinone + oxidized dithiothreitol
-
-
-
?
2,3-epoxy-2,3-dihydro-2-methyl-3-phytyl-1,4-naphthoquinone + 1,4-dithiothreitol
2-hydroxy-2-methyl-3-phytyl-2,3-dihydronaphthoquinone + oxidized dithiothreitol
-
-
-
?
2,3-epoxy-2,3-dihydro-2-methyl-3-phytyl-1,4-naphthoquinone + 1,4-dithiothreitol
2-hydroxy-2-methyl-3-phytyl-2,3-dihydronaphthoquinone + oxidized dithiothreitol
-
-
-
?
2,3-epoxy-2,3-dihydro-2-methyl-3-phytyl-1,4-naphthoquinone + 1,4-dithiothreitol
2-hydroxy-2-methyl-3-phytyl-2,3-dihydronaphthoquinone + oxidized dithiothreitol
-
-
-
?
2,3-epoxy-2,3-dihydro-2-methyl-3-phytyl-1,4-naphthoquinone + 1,4-dithiothreitol + H2O
2-methyl-3-phytyl-1,4-naphthoquinone + oxidized dithiothreitol
-
-
-
-
r
2,3-epoxy-2,3-dihydro-2-methyl-3-phytyl-1,4-naphthoquinone + 1,4-dithiothreitol + H2O
2-methyl-3-phytyl-1,4-naphthoquinone + oxidized dithiothreitol
-
-
-
-
r
2,3-epoxy-2,3-dihydro-2-methyl-3-phytyl-1,4-naphthoquinone + 1,4-dithiothreitol + H2O
2-methyl-3-phytyl-1,4-naphthoquinone + oxidized dithiothreitol
-
-
-
-
r
2,3-epoxy-2,3-dihydro-2-methyl-3-phytyl-1,4-naphthoquinone + 1,4-dithiothreitol + H2O
2-methyl-3-phytyl-1,4-naphthoquinone + oxidized dithiothreitol
-
-
-
-
r
2,3-epoxy-2,3-dihydro-2-methyl-3-phytyl-1,4-naphthoquinone + 1,4-dithiothreitol + H2O
2-methyl-3-phytyl-1,4-naphthoquinone + oxidized dithiothreitol
-
-
-
?, r
2,3-epoxy-2,3-dihydro-2-methyl-3-phytyl-1,4-naphthoquinone + 1,4-dithiothreitol + H2O
2-methyl-3-phytyl-1,4-naphthoquinone + oxidized dithiothreitol
-
-
-
-
r
2,3-epoxy-2,3-dihydro-2-methyl-3-phytyl-1,4-naphthoquinone + 1,4-dithiothreitol + H2O
2-methyl-3-phytyl-1,4-naphthoquinone + oxidized dithiothreitol
-
-
-
-
r
2,3-epoxy-2,3-dihydro-2-methyl-3-phytyl-1,4-naphthoquinone + 1,4-dithiothreitol + H2O
2-methyl-3-phytyl-1,4-naphthoquinone + oxidized dithiothreitol
-
-
-
-
r
2,3-epoxyphylloquinone + AH2
phylloquinone + A + ?
-
-
-
-
?
2,3-epoxyphylloquinone + AH2
phylloquinone + A + ?
-
VKOR reduces vitamin K using membrane-embedded thiols, Cys132 and Cys135, which become oxidized with concomitant VKOR inactivation. VKOR is subsequently reactivated by an unknown redox protein that might act directly on the Cys132-Cys135 residues
-
-
?
2,3-epoxyphylloquinone + AH2
phylloquinone + A + ?
the enzyme catalyzes the reduction of vitamin K 2,3-epoxide to vitamin K1, overview
-
-
?
2-methyl-3-phytyl-1,4-naphthoquinone + oxidized dithiothreitol + H2O
2,3-epoxy-2,3-dihydro-2-methyl-3-phytyl-1,4-naphthoquinone + 1,4-dithiothreitol
-
-
-
-
r
2-methyl-3-phytyl-1,4-naphthoquinone + oxidized dithiothreitol + H2O
2,3-epoxy-2,3-dihydro-2-methyl-3-phytyl-1,4-naphthoquinone + 1,4-dithiothreitol
-
-
-
-
r
2-methyl-3-phytyl-1,4-naphthoquinone + oxidized dithiothreitol + H2O
2,3-epoxy-2,3-dihydro-2-methyl-3-phytyl-1,4-naphthoquinone + 1,4-dithiothreitol
-
-
-
-
r
2-methyl-3-phytyl-1,4-naphthoquinone + oxidized dithiothreitol + H2O
2,3-epoxy-2,3-dihydro-2-methyl-3-phytyl-1,4-naphthoquinone + 1,4-dithiothreitol
-
-
-
-
r
2-methyl-3-phytyl-1,4-naphthoquinone + oxidized dithiothreitol + H2O
2,3-epoxy-2,3-dihydro-2-methyl-3-phytyl-1,4-naphthoquinone + 1,4-dithiothreitol
-
-
-
-
?
2-methyl-3-phytyl-1,4-naphthoquinone + oxidized dithiothreitol + H2O
2,3-epoxy-2,3-dihydro-2-methyl-3-phytyl-1,4-naphthoquinone + 1,4-dithiothreitol
-
-
-
-
r
2-methyl-3-phytyl-1,4-naphthoquinone + oxidized dithiothreitol + H2O
2,3-epoxy-2,3-dihydro-2-methyl-3-phytyl-1,4-naphthoquinone + 1,4-dithiothreitol
-
-
-
?
2-methyl-3-phytyl-1,4-naphthoquinone + oxidized dithiothreitol + H2O
2,3-epoxy-2,3-dihydro-2-methyl-3-phytyl-1,4-naphthoquinone + 1,4-dithiothreitol
-
-
-
?
2-methyl-3-phytyl-1,4-naphthoquinone + oxidized dithiothreitol + H2O
2,3-epoxy-2,3-dihydro-2-methyl-3-phytyl-1,4-naphthoquinone + 1,4-dithiothreitol
-
-
-
r
2-methyl-3-phytyl-1,4-naphthoquinone + oxidized dithiothreitol + H2O
2,3-epoxy-2,3-dihydro-2-methyl-3-phytyl-1,4-naphthoquinone + 1,4-dithiothreitol
-
-
-
-
?
2-methyl-3-phytyl-1,4-naphthoquinone + oxidized dithiothreitol + H2O
2,3-epoxy-2,3-dihydro-2-methyl-3-phytyl-1,4-naphthoquinone + 1,4-dithiothreitol
-
-
-
-
r
2-methyl-3-phytyl-1,4-naphthoquinone + oxidized dithiothreitol + H2O
2,3-epoxy-2,3-dihydro-2-methyl-3-phytyl-1,4-naphthoquinone + 1,4-dithiothreitol
reduction of vitamin K 2,3-epoxide to vitamin K
-
-
?
2-methyl-3-phytyl-1,4-naphthoquinone + oxidized dithiothreitol + H2O
2,3-epoxy-2,3-dihydro-2-methyl-3-phytyl-1,4-naphthoquinone + 1,4-dithiothreitol
-
-
-
-
r
vitamin K 2,3-epoxide + dithiothreitol
vitamin K + oxidized dithiothreitol
-
-
-
?
vitamin K 2,3-epoxide + dithiothreitol
vitamin K + oxidized dithiothreitol
-
-
-
-
?
vitamin K 2,3-epoxide + dithiothreitol
vitamin K + oxidized dithiothreitol
-
thioredoxin is the possible physiological electron acceptor
-
?
vitamin K 2,3-epoxide + dithiothreitol
vitamin K + oxidized dithiothreitol
-
reaction in metabolic pathway of vitamin K
-
?
vitamin K 2,3-epoxide + dithiothreitol
vitamin K + oxidized dithiothreitol
-
reaction in metabolic pathway of vitamin K
-
?
vitamin K 2,3-epoxide + dithiothreitol
vitamin K + oxidized dithiothreitol
-
thioredoxin is the possible physiological electron acceptor
-
?
vitamin K1 2,3-epoxide + dithiothreitol
vitamin K1 + oxidized dithiothreitol
-
two patients suffering from combined deficiency of vitamin K-dependent clotting factors type 2 possess a R98W substitution at the presumed cytoplasmic end of TM alpha-helix 2. Because the residue is far-removed from the proposed active site its mutation is, therefore assumed to disrupt VKORC1 structure or VKOR complex assembly rather than catalysis
-
-
?
vitamin K1 2,3-epoxide + dithiothreitol
vitamin K1 + oxidized dithiothreitol
VKORC1 contains missense mutations in the two heritable human diseases: combined deficiency of vitamin-K-dependent clotting factors type 2 (VKCFD2, Online Mendelian Inheritance in Man 607473) and resistance to coumarin-type anticoagulant drugs (warfarin resistance, WR, Online Mendelian Inheritance in man 122700)
-
-
?
vitamin K1 2,3-epoxide + dithiothreitol
vitamin K1 + oxidized dithiothreitol
-
vitamin K is an essential cofactor for post-translational gamma-carboxylation of vitamin K-dependent coagulation factors. The modification is carried out by a system of integral proteins of the endoplasmic reticulum membrane where the warfarin sensitive vitamin K 2,3-epoxide reductase (VKOR) produces the reduced hydroquinone form of vitamin K needed by the gamma-carboxylase as the active cofactor. VKOR is the rate-limiting step in the system
-
-
?
additional information
?
-
-
VKOR is a part of the post-translational protein-modification system that produces gamma-carboxylated proteins. The vitamin K-dependent gamma-carboxylation system consists of the vitamin K-dependent gamma-carboxylase, which requires the reduced hydroquinone form of vitamin K1 as a cofactor and the warfarin-sensitive enzyme vitamin K1 2,3-epoxide reductase, VKOR. VKOR and gamma-carboxylase are close enough together in the membrane to operate as a supramolecular assembly of proteins, in which substrates and products are shuttled efficiently from one component to the next. Calumenin is likely to have a regulatory role in controlling the activity of the system
-
-
?
additional information
?
-
-
the enzyme is involved in angiogenesis
-
-
?
additional information
?
-
-
the enzyme is involved in coagulation factor activity
-
-
?
additional information
?
-
the enzyme is involved in coagulation factor activity
-
-
?
additional information
?
-
-
the enzyme is involved in reduction of vitamin K, which is required by the gamma-glutamyl carboxylase, GGCX, transforming glutamate to gamma carboxyl glutamic acid in a vitamin K-dependent manner, gamma carboxyl glutamic acid is required for activity of proteins involved in coagulation, overview
-
-
?
additional information
?
-
-
the enzyme is involved in regulation of response to oral anticoagulants of European-American warfarin patients
-
-
?
additional information
?
-
-
the VKCFD2 disease, a vitamin K-dependent clotting factor deficiency, is caused by enzyme mutations, VKORC1 is the key component of the vitamin K reductase activity targeted by coumarin-derived drugs in prophylaxis and therapy of thrombosis
-
-
?
additional information
?
-
vitamin K epoxide reductase is the enzyme responsible for the recycling of vitamin K 2,3-epoxide to vitamin K hydroquinone, a cofactor that is essential for the synthesis of several blood coagulation factors
-
-
?
additional information
?
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VKORC1 is the key gene of the vitamin K cycle encoding the molecular target of coumarin-type anticoagulants vitaminK epoxide reductase, VKORC1 recycles vitamin K 2,3-epoxide to vitamin K hydroquinone, which functions as the essential cofactor for gamma-carboxylation of gamma-carboxyl-glutamic acid-domain proteins such as coagulation factors II, VII, IX, and X, proteins C, S, and Z, osteocalcin, matrix Gla protein MGP, and Gas6, gamma-glutamyl carboxylase, GGCX, is the enzyme that accomplishes the carboxylation reaction, VKORC1 represents the rate-limiting step in the reaction
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additional information
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the enzyme, driven by the reducing agent DTT, reduces both vitamin K 2,3-epoxide and vitamin K to the activated hydroquinone form
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additional information
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VKOR is a part of the post-translational protein-modification system that produces gamma-carboxylated proteins. The vitamin K-dependent gamma-carboxylation system consists of the vitamin K-dependent gamma-carboxylase, which requires the reduced hydroquinone form of vitamin K1 as a cofactor and the warfarin-sensitive enzyme vitamin K1 2,3-epoxide reductase, VKOR. VKOR and gamma-carboxylase are close enough together in the membrane to operate as a supramolecular assembly of proteins, in which substrates and products are shuttled efficiently from one component to the next. Calumenin is likely to have a regulatory role in controlling the activity of the system
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additional information
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the reduction is linked to dithiol-dependent oxidative folding of proteins in the ER by protein disulfide isomerase, PDI, oxidative folding of reduced RNase triggers the reduction of vitamin K epoxid and the gamma-carboxylation of the synthetic gamma-carboxylase peptide substrate FLEEL, overview
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evolution
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clear difference in VKOR activity and Ki for warfarin among bird species
evolution
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clear difference in VKOR activity and Ki for warfarin among bird species
evolution
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clear difference in VKOR activity and Ki for warfarin among bird species
evolution
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clear difference in VKOR activity and Ki for warfarin among bird species
evolution
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clear difference in VKOR activity and Ki for warfarin among bird species
evolution
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the enzyme belongs to the thiol-disulfide oxidoreductases. VKORL1, EC 1.1.4.2, is more highly conserved among vertebrates than its evolutionary relative VKOR, EC 1.1.4.1. The human paralogous proteins are 42% identical with 60% similarity
malfunction
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depletion of the protein disulfide formation activity of the enzyme in the endoplasmic reticulum results in cell death. Knockdown of the enzyme results in no detectable increase in expression of the ER Hsp70 chaperone BiP nor evidence of Xbp-1 splicing when measured on the final day of knockdown, indicating that an unfolded protein response is not being induced
malfunction
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warfarin interfers with the vitamin K cycle by inhibiting VKOR thus limiting the available activated hydroquinone cofactor and functionally impeding various blood clotting proteins that are dependent on gamma-carboxyglutamate residues
malfunction
some naturally occuring mutations of the enzyme, e.g. at residues mutations at Leu120, Leu128 and Tyr139, confer resistance against anti-coagulants, sodium warfarin, difenacoum and brodifacoum, to rats
metabolism
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vitamin K carboxylase converts vitamin K, in the vitamin K cycle, to an alkoxide-epoxide form which then reacts with CO2 and glutamate to generate gamma-carboxyglutamic acid. Subsequently, vitamin K epoxide reductase converts the alkoxide-epoxide to a hydroquinone form. By recycling vitamin K, the two integral-membrane proteins maintain vitamin K levels and sustain the blood coagulation cascade. Heterodimeric form of vitamin K carboxylase and vitamin K epoxide reductase may explain the efficient oxidation and reduction of vitamin K during the vitamin K cycle
metabolism
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vitamin K cycle, overview
metabolism
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VKOR contributes to an oxidizing endoplasmic reticulum environment under conditions of endoplasmic reticulum oxidoreductin and peroxiredoxin IV deficiency
metabolism
a key enzyme in the vitamin K cycle
metabolism
a key enzyme in the vitamin K cycle
metabolism
in vivo VKORC1L1 reduces vitamin K epoxide to support vitamin K-dependent carboxylation as efficiently as does VKORC1
metabolism
one of the key enzymes in the vitamin K cycle, which is essential for posttranslational modification of vitamin K-dependent proteins. Essential enzyme for vitamin K-dependent carboxylation
metabolism
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posttranslocational protein folding in the Gram-positive biofilm-forming actinobacterium Actinomyces oris is mediated by a membrane-bound thiol-disulfide oxidoreductase named MdbA, which catalyzes oxidative folding of nascent polypeptides transported by the Sec translocon. Reoxidation of MdbA involves a bacterial vitamin K epoxide reductase (VKOR)-like protein
metabolism
the enzyme plays important roles in redox regulation. The enzyme is involved in resistance to salt or drought stress. Down- and up-regulation of the enzyme in vivo changes the activities of antioxidant enzymes and results in differential accumulation of reactive oxygen species
metabolism
vitamin K 2,3-epoxide reductase family enzymes are the gatekeepers between nutritionally acquired K vitamins and the vitamin K cycle responsible for posttranslational modifications that confer biological activity upon vitamin K-dependent proteins with crucial roles in hemostasis, bone development and homeostasis, hormonal carbohydrate regulation and fertility
metabolism
VKORC1 is the key enzyme of the classical vitamin K cycle by which vitamin K-dependent proteins are gamma-carboxylated by the hepatic gamma-glutamyl carboxylase
metabolism
VKORC1L1 is chiefly responsible for antioxidative function by reduction of vitamin K to prevent damage by intracellular reactive oxygen species
physiological function
function of VKORC1 is to regenerate vitamin K and vitamin K hydroquinone from vitamin K 2,3-epoxide, a byproduct of the vitamin K-dependent gamma carboxylation reaction
physiological function
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human herpesvirus 8 viral interleukin-6 interacts with splice variant 2 of vitamin K epoxide reductase complex subunit 1, VKORC1v2, via the C-terminal residues 31-39 of the enzyme in the endoplasmic reticulum lumen, interaction analysis, VKORC1v2 to intracellular retention of endogenously expressed vIL-6, detailed overview
physiological function
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the enzyme is involved in the vitamin K cycle maintaining vitamin K levels and sustain the blood coagulation cascade
physiological function
the enzyme is regulated by microRNA miR-133a, which may have potential importance for anticoagulant therapy or aortic calcification. miR-133a levels correlate inversely with VKORC1 mRNA levels in 23 liver samples from healthy subjects
physiological function
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vitamin K 2,3-epoxide reductase complex subunit 1 is an essential enzyme for proper function of blood coagulation
physiological function
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vitamin K dependent oxidative protection is independent of VKOR inhibition by warfarin and GGCX inhibition by 2-chloro-vitamin K1, which indicated that vitamin K plays potential physiological roles outside of the realm of carboxylation. The hVKORL1, EC 11.4.2, turnover rate for vitamin K 2,3-epoxide reductase activity is significantly slower than for hVKOR
physiological function
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vitamin K epoxide reductase contributes to protein disulfide formation and redox homeostasis within the endoplasmic reticulum,depletion of the activity results in cell death, both peroxiredoxin IV and VKOR support cell growth and viability in the face of endoplasmic reticulum oxidoreductin depletion
physiological function
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vitamin K epoxide reductase is essential for the production of reduced vitamin K that is required for modification of vitamin K-dependent proteins
physiological function
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the vitamin K oxidoreductase reduces vitamin K to support the carboxylation and consequent activation of vitamin K-dependent proteins
physiological function
VKORC1 is an essential element involved in the correct gamma-carboxylation of vitamin K-dependent proteins such as Gas6, matrix-GLA protein and osteocalcin, as well as hemostatic proteins C, S and Z and coagulation factors II, VII, IX and X. vitamin K 2,3-epoxide reductase complex subunit 1, VKORC1, is a key protein in the vitamin K cycle, it is regulated by microRNA miR-133a, overview. Vitamin K 2,3-epoxide reductase complex subunit 1 is a relevant molecule for cardiovascular diseases, since it plays a role in soft tissue calcification
additional information
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conserved loop cysteines in VKOR are not required for active site regeneration after each cycle of oxidation
additional information
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membrane topology models for human VKOR, overview
additional information
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possible heterodimeric form of vitamin K carboxylase and vitamin K epoxide reductase during the vitamin K cycle and co-localization on the lumenal side of endoplasmic reticulum membrane, molecular dynamics simulations and modeling, overview
additional information
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structure-function relationship, the CXXC redox center active site (hVKOR Cys132 and Cys135) is located in the final transmembrane helix near the endoplasmic reticulum lumen/periplasmic side of the membrane, overview
additional information
VKORC1 function is measured in vitro using a dithiothreitol-driven vitamin K 2,3-epoxide reductase assay. Warfarin inhibits wild-type VKORC1 function by the DTT-VKOR assay. However, VKORC1 variants with warfarin resistance-associated missense mutations often show low VKOR activities and warfarin sensitivity instead of resistance. Development and evaluation of a cell culture-based, indirect VKOR assay accurately reports warfarin sensitivity or resistance for wild-type and variant VKORC1 proteins
additional information
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VKORC1 function is measured in vitro using a dithiothreitol-driven vitamin K 2,3-epoxide reductase assay. Warfarin inhibits wild-type VKORC1 function by the DTT-VKOR assay. However, VKORC1 variants with warfarin resistance-associated missense mutations often show low VKOR activities and warfarin sensitivity instead of resistance. Development and evaluation of a cell culture-based, indirect VKOR assay accurately reports warfarin sensitivity or resistance for wild-type and variant VKORC1 proteins
additional information
VKORC1 function is measured in vitro using a dithiothreitol-driven vitamin K 2,3-epoxide reductase assay. Warfarin inhibits wild-type VKORC1 function by the DTTVKOR assay. However, VKORC1 variants with warfarin resistance-associated missense mutations often show low VKOR activities and warfarin sensitivity instead of resistance. Development and evaluation of a cell culture-based, indirect VKOR assay accurately reports warfarin sensitivity or resistance for wild-type and variant VKORC1 proteins
additional information
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VKORC1 function is measured in vitro using a dithiothreitol-driven vitamin K 2,3-epoxide reductase assay. Warfarin inhibits wild-type VKORC1 function by the DTTVKOR assay. However, VKORC1 variants with warfarin resistance-associated missense mutations often show low VKOR activities and warfarin sensitivity instead of resistance. Development and evaluation of a cell culture-based, indirect VKOR assay accurately reports warfarin sensitivity or resistance for wild-type and variant VKORC1 proteins
additional information
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compounds target blood coagulation by inhibiting the vitamin K epoxide reductase (VKORC1), which catalyzes the reduction of vitamin K 2,3-epoxide to vitamin K
additional information
compounds target blood coagulation by inhibiting the vitamin K epoxide reductase (VKORC1), which catalyzes the reduction of vitamin K 2,3-epoxide to vitamin K
additional information
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role for Cys43 and Cys51 in catalysis with a relay mechanism in which a redox protein transfers electrons to these loop residues, which in turn reduce the membrane-embedded Cys132-Cys135 disulfide bond to activate VKOR
additional information
identification of the functional states of human Vitamin K epoxide reductase from molecular dynamics simulations
additional information
phylogenetic characterization of VKOR family proteins. A chronology for the evolution of the five extant VKOR clades is suggested
additional information
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phylogenetic characterization of VKOR family proteins. A chronology for the evolution of the five extant VKOR clades is suggested
additional information
the conserved loop cysteines of VKORC1L1, but not VKORC1, are involved in active site regeneration through an intra-molecular pathway. The different structures and reaction mechanisms of VKORC1L1 and VKORC1 may imply that these two enzymes have different physiological functions
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C101A
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formation of of a high-molecular-weight complex that is positive for thiol-disulfide oxidoreductase MdbA and vitamin K epoxide reductase
A26P
the IC50 ratio of wild-type to mutant enzyme is 49.6
A26T
the IC50 ratio of wild-type to mutant enzyme is 3.0
C6009T
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naturally occuring single nucleotide polymorphism
C6484T
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naturally occuring single nucleotide polymorphism
D36G
the IC50 ratio of wild-type to mutant enzyme is 3.2
D36V
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naturally occuring mutation, warfarin resistant mutant
D36Y
the IC50 ratio of wild-type to mutant enzyme is 3.8
G2653C
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naturally occuring single nucleotide polymorphism
G3673A
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naturally occuring single nucleotide polymorphism
G6853C
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naturally occuring single nucleotide polymorphism
G6R
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site-directed mutagenesis, the mutant shows altered membrane topology compared to the wild-type enzyme
G71A
the IC50 ratio of wild-type to mutant enzyme is 5.1
G9041A
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naturally occuring single nucleotide polymorphism
G9R
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site-directed mutagenesis, the mutant shows altered membrane topology compared to the wild-type enzyme
H28Q
the IC50 ratio of wild-type to mutant enzyme is 2.9
I86P
mutation has only a minor effect on the activity of wild-type enzyme, but it has a dramatic effect on the activity of the VKOR-CM mutant (a mutant with mutations in the charged residues flanking transmembrane domain 1), decreasing its activity to about 10%
K30L
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site-directed mutagenesis, the mutation close to the transmembrane domain 1 leads to altered membrane topology compared to the wild-type enzyme
L120Q
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naturally occuring mutation, the mutant is resistant to warfarin, but not to difenacoum, no synthesis of no 2-OH-vitamin K1 or 3-OH-vitamin K1
L128Q
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naturally occuring mutation, no synthesis of no 2-OH-vitamin K1 or 3-OH-vitamin K1
L27V
the IC50 ratio of wild-type to mutant enzyme is 2.5
N77S
the IC50 ratio of wild-type to mutant enzyme is 5.3
N77Y
the IC50 ratio of wild-type to mutant enzyme is 3.9
R33G
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site-directed mutagenesis, the mutation close to the transmembrane domain 1 leads to altered membrane topology compared to the wild-type enzyme
R35G
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site-directed mutagenesis, the mutation close to the transmembrane domain 1 leads to altered membrane topology compared to the wild-type enzyme
R37G
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site-directed mutagenesis, the mutation close to the transmembrane domain 1 leads to altered membrane topology compared to the wild-type enzyme
R58G,
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naturally occuring mutation, warfarin resistant mutant
S52L
the IC50 ratio of wild-type to mutant enzyme is 7.4
S53W
the IC50 ratio of wild-type to mutant enzyme is 5.7
S56F
the IC50 ratio of wild-type to mutant enzyme is 6.8
S57A
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the mutation eliminates VKOR activity
S7R
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site-directed mutagenesis, the mutant shows altered membrane topology compared to the wild-type enzyme
T5808G
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naturally occuring single nucleotide polymorphism
V54L
the IC50 ratio of wild-type to mutant enzyme is 4.5
V66G
the IC50 ratio of wild-type to mutant enzyme is 2.8
W57A
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the mutation eliminates VKOR activity
W59C
the IC50 ratio of wild-type to mutant enzyme is 7.6
W59L
the IC50 ratio of wild-type to mutant enzyme is 75.2
W59R
the IC50 ratio of wild-type to mutant enzyme is 17.5
W59R/W59C/W59L
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naturally occuring mutant
A26S
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mutant shows about 70% relative VKOR activity as compared to the wild type enzyme
A48T
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mutant shows about 120% relative VKOR activity as compared to the wild type enzyme
E37G
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mutant shows about 75% relative VKOR activity as compared to the wild type enzyme
L128S
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mutant shows about 20% relative VKOR activity as compared to the wild type enzyme
R12W
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mutant shows about 35% relative VKOR activity as compared to the wild type enzyme
R58G
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mutant shows about 40% relative VKOR activity as compared to the wild type enzyme
R61L
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mutant shows about 50% relative VKOR activity as compared to the wild type enzyme
Y139C
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mutant shows about 30% relative VKOR activity as compared to the wild type enzyme
W59G
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the single nucleotide polymorphism T175G in gene VKORC1 causes 4-hydroxycoumarin derivative-resistance
A143V
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mutant shows about 140% relative VKOR activity as compared to the wild type enzyme
E67K
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the mutant shows a reduced vitamin K epoxide turnover of about 33% compared to the wild type protein, and has no effect on warfarin sensitivity in vitro
F63C
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the mutation reduces the VKOR activity to about 30% of normal
I141V
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mutant shows about 45% relative VKOR activity as compared to the wild type enzyme
I90L
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mutant shows about 90% relative VKOR activity as compared to the wild type enzyme
L120Q/L128Q/Y139C/Y139F/Y139S
site-directed mutagenesis
R33P
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VKOR activity of the Arg33Pro variant is reduced to 42% of wild type activity
W59R
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mutant shows 16% residual VKOR activity
Y39N
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mutant shows about 30% relative VKOR activity as compared to the wild type enzyme
Y139F
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the mutation mediates resistance towards chlorophacinone and bromadiolone
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C1173T
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a single nucleotide polymorphism, SNP, for haplotypes associated with a lower oral anticoagulant dose requirement
C1173T
natural genetic polymorphism of the enzyme in a Chinese and a Caucasian population, genotyping, the exchange for T at position 1173 in asian patients results in a phenotype with higher sensitivity to oral anticoagulants, overview
C132A
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no catalytic activity, part of CXXC motif
C132A
mutation eliminates enzymatic activity in conversion of vitamin K to vitamin K hydroquinone
C135A
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no catalytic activity, part of CXXC motif
C135A
impairs warfarin binding
C135A
mutation eliminates enzymatic activity in conversion of vitamin K to vitamin K hydroquinone
C16A
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40% of wild-type activity
C16A
about 85% of wild-type activity in conversion of vitamin K to vitamin K hydroquinone. Mutant enzyme retains 40% of the wild-type activityin conversion of vitamin K to vitamin K hydroquinone
C43A
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35% of wild-type activity. C43 can form a disulfide bond with C51
C43A
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naturally occuring mutant, active in presence of DTT, which helps to bypass C43
C43A
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site-directed mutagenesis, the mutant shows vitamin K epoxide reduction activity similar to the wild-type enzyme, but only with the membrane-permeant reductant DTT, no mutant activity with thioredoxin as reductant
C43A
about 75% of wild-type activity in conversion of vitamin K to vitamin K hydroquinone. Mutant enzyme retains 25% of the wild-type activityin conversion of vitamin K to vitamin K hydroquinone
C43A/C51A
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112% of wild-type activity
C43A/C51A
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site-directed mutagenesis, the mutation has a minor effect on VKOR activity, the mutant of the altered four-transmembrane domain form of VKOR is more active than the wild-type three-transmembrane domain enzyme
C43A/C51A
about 50% of wild-type activity in conversion of vitamin K to vitamin K hydroquinone. The deletion mutant enzyme retains 85% of the wild-type activity in the conversion of vitamin K 2,3-epoxide to vitamin K
C51A
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95% of wild-type activity. C43 can form a disulfide bond with C51
C51A
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naturally occuring mutant, active in presence of DTT, which helps to bypass C43
C51A
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site-directed mutagenesis, the mutation has a minor effect on VKOR activity, the mutant of the altered four-transmembrane domain form of VKOR is more active than the wild-type three-transmembrane domain enzyme
C51A
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site-directed mutagenesis, the mutant shows vitamin K epoxide reduction activity similar to the wild-type enzyme, but only with the membrane-permeant reductant DTT, no mutant activity with thioredoxin as reductant
C51A
mutant enzyme retains essentially wild-type activity in conversion of vitamin K to vitamin K hydroquinone
C85A
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100% of wild-type activity
C85A
about 55% of wild-type activity in conversion of vitamin K to vitamin K hydroquinone. Mutant enzyme retains 105% of the wild-type activityin conversion of vitamin K to vitamin K hydroquinone
C96A
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45% of wild-type activity
C96A
about 50% of wild-type activity in conversion of vitamin K to vitamin K hydroquinone. Mutant enzyme retains 40% of the wild-type activityin conversion of vitamin K to vitamin K hydroquinone
DELTAC43-C51
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85% of wild-type activity
DELTAC43-C51
about 50% of wild-type activity in conversion of vitamin K to vitamin K hydroquinone. The deletion mutant enzyme retains 112% of the wild-type activity in the conversion of vitamin K 2,3-epoxide to vitamin K
I123N
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naturally occuring mutant
I123N
the IC50 ratio of wild-type to mutant enzyme is 8.5
L128R
VKOR activity is reduced to 5.2% of the activity of the wild-type enzyme
L128R
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naturally occuring mutation, warfarin resistant mutant
L128R
site-directed mutagenesis, the mutant is resistant to warfarin and oral anti-coagulants
L128R
the IC50 ratio of wild-type to mutant enzyme is 49.7
R58G
VKOR activity is reduced to 20.6% of the activity of the wild-type enzyme
R58G
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naturally occuring mutant
R58G
the IC50 ratio of wild-type to mutant enzyme is 3.4
R98W
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two patients suffering from combined deficiency of vitamin K-dependent clotting factors type 2 possess a R98W substitution at the presumed cytoplasmic end of TM alpha-helix 2 of vitamin-K-epoxide reductase. Because the residue is far-removed from the proposed active site its mutation is, therefore assumed to disrupt VKORC1 structure or VKOR complex assembly rather than catalysis
R98W
VKOR activity is reduced to 8.9% of the activity of the wild-tyoe enzyme
V29L
VKOR activity is reduced to 96.6% of the activity of the wild-type enzyme.Above 0.02 mM warfarin the mutant enzyme retains higher VKOR activity than the wild-type enzyme
V29L
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naturally occuring mutation, warfarin resistant mutant
V29L
site-directed mutagenesis, the mutant is resistant to warfarin and oral anti-coagulants
V29L
the IC50 ratio of wild-type to mutant enzyme is 5.5
V45A
VKOR activity is reduced to 23% of the activity of the wild-type enzyme
V45A
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naturally occuring mutation, warfarin resistant mutant
V45A
site-directed mutagenesis, the mutant is resistant to warfarin and oral anti-coagulants
V45A
the IC50 ratio of wild-type to mutant enzyme is 6.2
V66M
mutation is responsible for warfarin resistance phenotype
V66M
naturally occuring VKORC1 mutant showing warfarin-resistance, patients with this mutation need a very high dosage of anticoagulants in therapy, overview
V66M
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naturally occuring mutation, warfarin resistant mutant
V66M
the IC50 ratio of wild-type to mutant enzyme is 5.4
Y139C
VKOR activity is reduced to 48% of the activity of the wild-type enzyme. Above 0.02 mM warfarin the mutant enzyme retains higher VKOR activity than the wild-type enzyme
Y139C
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naturally occuring mutation, the mutant is resistant to warfarin, but not to difenacoum, additional synthesis of 3-hydroxyvitamin K1
Y139C
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site-directed mutagenesis, the mutation dramatically affects the vitamin K epoxide reductase activity
Y139F
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naturally occuring mutation, the mutant is resistant to warfarin, but not to difenacoum, additional synthesis of 3-hydroxyvitamin K1
Y139F
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the mutant is warfarin insensitive and shows altered membrane topology compared to the wild-type enzyme
Y139S
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naturally occuring mutation, the mutant is resistant to warfarin, but not to difenacoum, additional synthesis of 3-hydroxyvitamin K1
Y139S
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site-directed mutagenesis, the mutation dramatically affects the vitamin K epoxide reductase activity, additional production of 3-hydroxyvitamin K1 in the mutant
A26T
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mutant shows about 60% relative VKOR activity as compared to the wild type enzyme
A26T
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the mutation has only a moderate effect on VKOR activity with a reduction to approximately 56% of wild type activity
L120Q
naturally occuring mutant, resitant to warfarin and other anticoagulants
L120Q
naturally occuring mutant, the mutant rat is resistant to some anticoagulants
L128Q
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mutant shows moderately reduced VKOR activity (about 60% compared to wild type protein) and is resistant to warfarin inhibition to a variable degree
L128Q
naturally occuring mutant, resitant to warfarin and other anticoagulants
L128Q
naturally occuring mutant, the mutant rat is resistant to some anticoagulants
Y139C
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mutant shows moderately reduced VKOR activity (about 60% compared to wild type protein) and is resistant to warfarin inhibition to a variable degree
Y139C
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warfarin-resistant mutant
Y139C
naturally occuring mutant, resitant to warfarin and other anticoagulants
Y139C
naturally occuring mutant, the mutant rat is resistant to some anticoagulants
Y139F
the natural occuring mutation confers resistance to enzyme inhibitor warfarin, the mutant rats do not show vitamin K deficiency
Y139F
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highly resistant to warfarin and increased resistance to further anticoagulants
Y139F
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the mutation mediates resistance towards chlorophacinone and bromadiolone
Y139F
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warfarin-resistant mutant
Y139F
naturally occuring mutant, resitant to warfarin and other anticoagulants
Y139F
naturally occuring mutant, the mutant rat is resistant to some anticoagulants
Y139S
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mutant shows moderately reduced VKOR activity and is resistant to warfarin inhibition to a variable degree
Y139S
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warfarin-resistant mutant
Y139S
naturally occuring mutant, resitant to warfarin and other anticoagulants
Y139S
naturally occuring mutant, the mutant rat is resistant to some anticoagulants
additional information
VKORC1 contains missense mutations in the two heritable human diseases: combined deficiency of vitamin-K-dependent clotting factors type 2 (VKCFD2, Online Mendelian Inheritance in Man 607473) and resistance to coumarin-type anticoagulant drugs (warfarin resistance, WR, Online Mendelian Inheritance in man 122700)
additional information
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VKORC1 contains missense mutations in the two heritable human diseases: combined deficiency of vitamin-K-dependent clotting factors type 2 (VKCFD2, Online Mendelian Inheritance in Man 607473) and resistance to coumarin-type anticoagulant drugs (warfarin resistance, WR, Online Mendelian Inheritance in man 122700)
additional information
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deficient enzyme mutants cause VKCFD2 disease phenotype
additional information
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enzyme overexpression stimulates cell proliferation, while inhibition of enzyme expression by antisense constructs reduces it, overview
additional information
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expression of the enzyme in HEK-293 cells significantly improves carboxylation in a HEK-293 cell line overexpressing factor X
additional information
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mutations in VKORC1 cause 2 distinctive phenotypes: a homozygous missense mutation in the VKORC1 gene leads to combined deficiency of vitamin Kdependent coagulation factors type 2, VKCFD2, and heterozygous missense mutations are responsible for hereditary warfarin resistance, expression of the enzyme in HEK-293 cells significantly improves carboxylation in a HEK-293 cell line overexpressing factor X
additional information
in vitro expression of VKORC1 gene constructs, including coding region and promoter, fails to reveal any genotype effect on transcription and mRNA processing
additional information
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in vitro expression of VKORC1 gene constructs, including coding region and promoter, fails to reveal any genotype effect on transcription and mRNA processing
additional information
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patient with warfarin resistance due to a 383T>G transition in exon 2 of the VKORC1 gene, patient is heterozygous for the mutation
additional information
genetic variation in the vitamin K epoxide reductase gene is associated with variation in plasma phylloquinone concentrations
additional information
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genetic variation in the vitamin K epoxide reductase gene is associated with variation in plasma phylloquinone concentrations
additional information
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VKORC1 gene polymorphisms are associated with warfarin dose requirements in Turkish patients
additional information
construction of warfarin-resistant VKORC1 variants following naturally occuring mutations in patients
additional information
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construction of warfarin-resistant VKORC1 variants following naturally occuring mutations in patients
additional information
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knockout of endogenous VKOR activity, i.e. VKOR and VKORC1L1 enzymes, in HEK-293 cells by transcription activator-like effector nucleases (TALENs)-mediated genome editing, overview. VKOR knockout cells regained KO reductase activity through VKORC1L1 after culturing for several generations (Figure 3A). In addition, this activity is sensitive to warfarin inhibition as the wild-type cells
additional information
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allelic mutations in the orthologous gene of VKORC1 can cause warfarin resistance
additional information
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allelic mutations in the orthologous gene can cause warfarin resistance
additional information
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siRNA silencing of VKOR complex subunit PDI
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Homo sapiens (Q9BQB6), Homo sapiens
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Luong, T.T.; Reardon-Robinson, M.E.; Siegel, S.D.; Ton-That, H.
Reoxidation of the thiol-disulfide oxidoreductase MdbA by a bacterial vitamin K epoxide reductase in the biofilm-forming actinobacterium actinomyces oris
J. Bacteriol.
199
e00817-16
2017
Actinomyces oris, Mycobacterium tuberculosis
brenda
Tie, J.K.; Jin, D.Y.; Stafford, D.W.
Conserved loop cysteines of vitamin K epoxide reductase complex subunit 1-like 1 (VKORC1L1) are involved in its active site regeneration
J. Biol. Chem.
289
9396-9407
2014
Homo sapiens (Q8N0U8)
brenda
Liu, S.; Cheng, W.; Fowle Grider, R.; Shen, G.; Li, W.
Structures of an intramembrane vitamin K epoxide reductase homolog reveal control mechanisms for electron transfer
Nat. Commun.
5
3110
2014
Synechococcus sp. JA-2-3B'a(2-13) (Q2JJF6)
brenda
Shen, G.; Cui, W.; Zhang, H.; Zhou, F.; Huang, W.; Liu, Q.; Yang, Y.; Li, S.; Bowman, G.R.; Sadler, J.E.; Gross, M.L.; Li, W.
Warfarin traps human vitamin K epoxide reductase in an intermediate state during electron transfer
Nat. Struct. Mol. Biol.
24
69-76
2017
Homo sapiens (Q9BQB6), Homo sapiens
brenda
Bevans, C.G.; Krettler, C.; Reinhart, C.; Watzka, M.; Oldenburg, J.
Phylogeny of the vitamin K 2,3-epoxide reductase (VKOR) family and evolutionary relationship to the disulfide bond formation protein B (DsbB) family
Nutrients
7
6224-6249
2015
Homo sapiens (Q9BQB6), Homo sapiens
brenda
Tew, B.Y.; Hong, T.B.; Otto-Duessel, M.; Elix, C.; Castro, E.; He, M.; Wu, X.; Pal, S.K.; Kalkum, M.; Jones, J.O.
Vitamin K epoxide reductase regulation of androgen receptor activity
Oncotarget
8
13818-13831
2017
Homo sapiens (Q9BQB6), Mus musculus (Q9CRC0), Mus musculus
brenda
Yu, Z.B.; Yang, X.J.; Du, J.J.; Wan, C.M.; Xu, J.N.; Wang, W.J.; Feng, Y.G.; Wang, X.Y.
A homologue of vitamin K epoxide reductase in Solanum lycopersicum is involved in resistance to osmotic stress
Physiol. Plant.
156
311-322
2016
Solanum lycopersicum (K4BAJ5), Solanum lycopersicum
brenda
Hatahet, F.; Blazyk, J.L.; Martineau, E.; Mandela, E.; Zhao, Y.; Campbell, R.E.; Beckwith, J.; Boyd, D.
Altered Escherichia coli membrane protein assembly machinery allows proper membrane assembly of eukaryotic protein vitamin K epoxide reductase
Proc. Natl. Acad. Sci. USA
112
15184-15189
2015
Rattus norvegicus (Q6TEK4)
brenda
Chatron, N.; Chalmond, B.; Trouve, A.; Benoit, E.; Caruel, H.; Lattard, V.; Tchertanov, L.
Identification of the functional states of human Vitamin K epoxide reductase from molecular dynamics simulations
RSC Adv.
7
52071-52090
2017
Homo sapiens (Q9BQB6)
-
brenda
Sinhadri, B.C.S.; Jin, D.Y.; Stafford, D.W.; Tie, J.K.
Vitamin K epoxide reductase and its paralogous enzyme have different structures and functions
Sci. Rep.
7
17632
2017
Homo sapiens (Q9BQB6)
brenda
Caspers, M.; Czogalla, K.J.; Liphardt, K.; Mueller, J.; Westhofen, P.; Watzka, M.; Oldenburg, J.
Two enzymes catalyze vitamin K 2,3-epoxide reductase activity in mouse VKORC1 is highly expressed in exocrine tissues while VKORC1L1 is highly expressed in brain
Thromb. Res.
135
977-983
2015
Mus musculus (Q6TEK5), Mus musculus (Q9CRC0), Mus musculus
brenda