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Literature summary extracted from

  • Gardill, S.L.; Suttie, J.W.
    Vitamin K epoxide and quinone reductase activities. Evidence for reduction by a common enzyme (1990), Biochem. Pharmacol., 40, 1055-1061.
    View publication on PubMed

Inhibitors

EC Number Inhibitors Comment Organism Structure
1.17.4.4 Chloromenaquinone-2
-
 Rattus norvegicus
1.17.4.4 coumarin anticoagulants
-
 Rattus norvegicus

Localization

EC Number Localization Comment Organism GeneOntology No. Textmining
1.17.4.4 microsome
-
 Rattus norvegicus
-
-

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-epoxy-2,3-dihydro-2-methyl-3-phytyl-1,4-naphthoquinone + 1,4-dithiothreitol Rattus norvegicus i.e. vitamin K 2,3-epoxide, the enzyme is supposed to catalyze the reduction of the epoxide to quinone and of the quinone to vitamin K hydroquinone 2-hydroxy-2-methyl-3-phytyl-2,3-dihydronaphthoquinone + oxidized dithiothreitol
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
1.17.4.4 Rattus norvegicus
-
-
-

Source Tissue

EC Number Source Tissue Comment Organism Textmining
1.17.4.4 liver
-
 Rattus norvegicus
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.17.4.4 2,3-epoxy-2,3-dihydro-2-methyl-3-phytyl-1,4-naphthoquinone + 1,4-dithiothreitol i.e. vitamin K 2,3-epoxide, the enzyme is supposed to catalyze the reduction of the epoxide to quinone and of the quinone to vitamin K hydroquinone Rattus norvegicus 2-hydroxy-2-methyl-3-phytyl-2,3-dihydronaphthoquinone + oxidized dithiothreitol
-
 ?

Cofactor

EC Number Cofactor Comment Organism Structure
1.17.4.4 thioredoxin probable physiological cofactor Rattus norvegicus