Activating Compound | Comment | Organism | Structure |
---|---|---|---|
DTT | activation in intact and Cys-mutated membranes | Homo sapiens | |
thioredoxin | activation only in intact membranes | Homo sapiens |
Cloned (Comment) | Organism |
---|---|
expression in Spodoptera frugiperda Sf21 cell microsomes using baculovirus containing wild-type or mutant VKORs transfection method, in vitro transcription and translation of the human enzyme using r-VKORC1/ZEM229 as the template | Homo sapiens |
Protein Variants | Comment | Organism |
---|---|---|
C43A | 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 | Homo sapiens |
C51A | 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 | Homo sapiens |
Localization | Comment | Organism | GeneOntology No. | Textmining |
---|---|---|---|---|
membrane | VKOR is an integral membrane protein | Homo sapiens | 16020 | - |
Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
2,3-epoxyphylloquinone + AH2 | Homo sapiens | 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 | phylloquinone + A + ? | - |
? |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Homo sapiens | - |
- |
- |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
2,3-epoxyphylloquinone + 1,4-dithiothreitol | - |
Homo sapiens | phylloquinone + oxidized dithiothreitol | - |
? | |
2,3-epoxyphylloquinone + AH2 | 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 | Homo sapiens | phylloquinone + A + ? | - |
? | |
2,3-epoxyphylloquinone + reduced thioredoxin | - |
Homo sapiens | phylloquinone + oxidized thioredoxin | - |
? |
Synonyms | Comment | Organism |
---|---|---|
vitamin K oxidoreductase | - |
Homo sapiens |
VKOR | - |
Homo sapiens |
Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
---|---|---|---|
21 | - |
assay at | Homo sapiens |
pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|
7.4 | - |
assay at | Homo sapiens |
General Information | Comment | Organism |
---|---|---|
additional information | 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 | Homo sapiens |
physiological function | the vitamin K oxidoreductase reduces vitamin K to support the carboxylation and consequent activation of vitamin K-dependent proteins | Homo sapiens |