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Literature summary for 1.17.4.4 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
Search for more literature for 1.17.4.4

Protein Variants

Protein Variants Comment Organism
F55G site-directed mutagenesis, the nonconservative mutant is predicted to be inactive by molecular modeling analyses Homo sapiens
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
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
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

Inhibitors Comment Organism Structure
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

Localization Comment Organism GeneOntology No. Textmining
microsome
-
 Homo sapiens
-
-

Natural Substrates/ Products (Substrates)

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

Organism

Organism UniProt Comment Textmining
Homo sapiens Q9BQB6
-
-

Substrates and Products (Substrate)

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

Synonyms

Synonyms Comment Organism
vitamin K epoxide reductase
-
 Homo sapiens
VKORC1
-
 Homo sapiens

Temperature Optimum [°C]

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

pH Optimum

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

General Information

General Information Comment Organism
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
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