Protein Variants | Comment | Organism |
---|---|---|
D36V | naturally occuring mutation, warfarin resistant mutant | Homo sapiens |
L128R | naturally occuring mutation, warfarin resistant mutant | Homo sapiens |
R58G, | naturally occuring mutation, warfarin resistant mutant | Homo sapiens |
V29L | naturally occuring mutation, warfarin resistant mutant | Homo sapiens |
V45A | naturally occuring mutation, warfarin resistant mutant | Homo sapiens |
V66M | naturally occuring mutation, warfarin resistant mutant | Homo sapiens |
Inhibitors | Comment | Organism | Structure |
---|---|---|---|
warfarin | non-competitive inhibitor, displacement of the warfarin binding site away from the vitamin K binding site by at least one turn of the transmembrane helix. The fully extended phenyl group of S-warfarin may interact with the phenyl fragment of Tyr139 of VKOR in a stacking configuration. Binding of S-warfarin to VKOR in the presence of vitamin K could modify, i.e. reduce the rate of flip-flop of lipid membrane, ultimately leading to the decrease of the amount of the vitamin K hydroquinone form | Homo sapiens |
Localization | Comment | Organism | GeneOntology No. | Textmining |
---|---|---|---|---|
endoplasmic reticulum membrane | - |
Homo sapiens | 5789 | - |
membrane | transmembrane protein with 5 transmembrane helices, membrane topology, overview | Homo sapiens | 16020 | - |
Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
2-methyl-3-phytyl-1,4-naphthoquinone + oxidized dithiothreitol + H2O | Homo sapiens | - |
2,3-epoxy-2,3-dihydro-2-methyl-3-phytyl-1,4-naphthoquinone + 1,4-dithiothreitol | - |
? |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Homo sapiens | - |
- |
- |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
2-methyl-3-phytyl-1,4-naphthoquinone + oxidized dithiothreitol + H2O | - |
Homo sapiens | 2,3-epoxy-2,3-dihydro-2-methyl-3-phytyl-1,4-naphthoquinone + 1,4-dithiothreitol | - |
? |
Synonyms | Comment | Organism |
---|---|---|
vitamin K epoxide reductase | - |
Homo sapiens |
VKOR | - |
Homo sapiens |
VKORC1 | - |
Homo sapiens |
General Information | Comment | Organism |
---|---|---|
metabolism | 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 | Homo sapiens |
additional information | 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 | Homo sapiens |
physiological function | the enzyme is involved in the vitamin K cycle maintaining vitamin K levels and sustain the blood coagulation cascade | Homo sapiens |