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Literature summary for 1.17.4.4 extracted from

  • Van Horn, W.D.
    Structural and functional insights into human vitamin K epoxide reductase and vitamin K epoxide reductase-like1 (2013), Crit. Rev. Biochem. Mol. Biol., 48, 357-372.
    View publication on PubMed
Search for more literature for 1.17.4.4

Cloned(Commentary)

Cloned (Comment) Organism
gene Vkor, sequence comparisons Homo sapiens

Protein Variants

Protein Variants Comment Organism
C43A naturally occuring mutant, active in presence of DTT, which helps to bypass C43 Homo sapiens
C51A naturally occuring mutant, active in presence of DTT, which helps to bypass C43 Homo sapiens
I123N naturally occuring mutant Homo sapiens
R58G naturally occuring mutant Homo sapiens
W59R/W59C/W59L naturally occuring mutant Homo sapiens

Inhibitors

Inhibitors Comment Organism Structure
warfarin hVKOR is directly and irreversibly inhibited by warfarin, hVKOR is the target of a common anticoagulant, warfarin. Tyr139 in hVKOR is part of the warfarin binding site Homo sapiens
warfarin
-
 Mycobacterium tuberculosis

Localization

Localization Comment Organism GeneOntology No. Textmining
endoplasmic reticulum membrane integral membrane protein, topology, overview Homo sapiens 5789
-

Natural Substrates/ Products (Substrates)

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
-
 ?
2-methyl-3-phytyl-1,4-naphthoquinone + oxidized dithiothreitol + H2O Mycobacterium tuberculosis
-
 2,3-epoxy-2,3-dihydro-2-methyl-3-phytyl-1,4-naphthoquinone + 1,4-dithiothreitol
-
 ?
additional information Homo sapiens the enzyme, driven by the reducing agent DTT, reduces both vitamin K 2,3-epoxide and vitamin K to the activated hydroquinone form ?
-
 ?

Organism

Organism UniProt Comment Textmining
Homo sapiens
-
-
-
Mycobacterium tuberculosis
-
-
-

Source Tissue

Source Tissue Comment Organism Textmining
liver high expression level Homo sapiens
-

Substrates and Products (Substrate)

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
-
 ?
2-methyl-3-phytyl-1,4-naphthoquinone + oxidized dithiothreitol + H2O
-
 Mycobacterium tuberculosis 2,3-epoxy-2,3-dihydro-2-methyl-3-phytyl-1,4-naphthoquinone + 1,4-dithiothreitol
-
 ?
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 Homo sapiens ?
-
 ?

Synonyms

Synonyms Comment Organism
vitamin K epoxide reductase
-
 Homo sapiens
vitamin K epoxide reductase
-
 Mycobacterium tuberculosis
VKOR
-
 Homo sapiens
VKOR
-
 Mycobacterium tuberculosis
VKOR complex
-
 Homo sapiens
VKOR complex
-
 Mycobacterium tuberculosis
VKORC1
-
 Homo sapiens

General Information

General Information Comment Organism
evolution 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 Homo sapiens
malfunction 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 Homo sapiens
metabolism vitamin K cycle, overview Homo sapiens
additional information 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 Homo sapiens
physiological function 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 Homo sapiens