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Literature summary extracted from

  • Chatron, N.; Abi Khalil, R.; Benoit, E.; Lattard, V.
    Structural investigation of the vitamin K epoxide reductase (VKORC1) binding site with vitamin K (2020), Biochemistry, 59, 1351-1360.
    View publication on PubMed

Protein Variants

EC Number Protein Variants Comment Organism
1.17.4.4 F55G site-directed mutagenesis, the nonconservative mutant is predicted to be inactive by molecular modeling analyses Homo sapiens
1.17.4.4 F55Y site-directed mutagenesis, the conservative mutant is expected to be active by molecular modeling analyses, molecular docking of vitK1E to the F55G mutant Homo sapiens
1.17.4.4 F83G site-directed mutagenesis, the nonconservative mutant is predicted to be inactive by molecular modeling analyses, a loss of hydrogen bonds to S52 and S81 induced by the F83G mutation leads to a rotation of vitK1E away from the active site, also facing TM2 Homo sapiens
1.17.4.4 N80G site-directed mutagenesis, the nonconservative mutant is predicted to be inactive by molecular modeling analyses, molecular docking of vitK1E to the N80G mutant. The N80G mutation induces a loss of hydrogen bonds to S52 and S81, leading vitK1E to rotate away from C135 Homo sapiens

Inhibitors

EC Number Inhibitors Comment Organism Structure
1.17.4.4 warfarin molecular docking and dynamics of VKORC1-vitamin epoxide K and VKORC1-warfarin complexes, overview. Activity assay data are fitted by nonlinear regression to the noncompetitive inhibition model Homo sapiens

Localization

EC Number Localization Comment Organism GeneOntology No. Textmining
1.17.4.4 microsome
-
 Homo sapiens
-
-

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
1.17.4.4 2,3-epoxyphylloquinone + a protein with reduced L-cysteine residues Homo sapiens
-
 phylloquinone + a protein with a disulfide bond + H2O
-
 ?
1.17.4.4 phylloquinone + a protein with reduced L-cysteine residues Homo sapiens
-
 phylloquinol + a protein with a disulfide bond
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
1.17.4.4 Homo sapiens Q9BQB6
-
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.17.4.4 2,3-epoxyphylloquinone + a protein with reduced L-cysteine residues
-
 Homo sapiens phylloquinone + a protein with a disulfide bond + H2O
-
 ?
1.17.4.4 phylloquinone + a protein with reduced L-cysteine residues
-
 Homo sapiens phylloquinol + a protein with a disulfide bond
-
 ?
1.17.4.4 vitamin K1 + MK4 epoxide + DTT
-
 Homo sapiens ?
-
 ?

Synonyms

EC Number Synonyms Comment Organism
1.17.4.4 vitamin K epoxide reductase
-
 Homo sapiens
1.17.4.4 VKORC1
-
 Homo sapiens

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
1.17.4.4 37
-
 assay at Homo sapiens

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
1.17.4.4 7.4
-
 assay at Homo sapiens

General Information

EC Number General Information Comment Organism
1.17.4.4 additional information VKORC1 enzymatic site structure and function analysis, molecular modeling. Residues F55, N80, and F83 are crucial for vitamin K epoxide binding. Residues F55, N80, and F83 appear to act in a concerted manner to keep vitamin K epoxide close to the C135 catalytic residue. Residues F55 and N80 prevent naphthoquinone head rotation away from the active site, assisted by residue F83 that prevents vitamin K from sliding outside the enzymatic pocket, through hydrophobic tail stabilization. Molecular docking and dynamics of VKORC1-vitamin epoxide K and VKORC1-warfarin complexes, molecular simulations, overview. Substrate binding structure analysis Homo sapiens
1.17.4.4 physiological function the vitamin K epoxide reductase (VKORC1) enzyme is of primary importance in many physiological processes, i.e. blood coagulation, energy metabolism, and arterial calcification prevention, due to its role in the vitamin K cycle. VKORC1 catalyzes reduction of vitamin K epoxide to quinone and then to hydroquinone Homo sapiens