Is thioredoxin the physiological vitamin K epoxide reducing agent?

scientific article published on July 6, 1992

Is thioredoxin the physiological vitamin K epoxide reducing agent? is …
instance of (P31):
scholarly articleQ13442814

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P356DOI10.1016/0014-5793(92)80681-6
P698PubMed publication ID1299627
P5875ResearchGate publication ID21855331

P2093author name stringP. C. Preusch
P2860cites workStimulation of the dithiol-dependent reductases in the vitamin K cycle by the thioredoxin system. Strong synergistic effects with protein disulphide-isomeraseQ42792635
Inhibition of thioredoxin reductase (E.C. 1.6.4.5.) by antitumor quinonesQ43939248
Solubilization and characterization of vitamin K epoxide reductase from normal and warfarin-resistant rat liver microsomes.Q54479905
Vitamin K1 2,3-epoxide and quinone reduction: mechanism and inhibitionQ67298046
Enzymatic reduction-oxidation of protein disulfides by thioredoxinQ70397478
Reduced thioredoxin: a possible physiological cofactor for vitamin K epoxide reductase. Further support for an active site disulfideQ70407705
Warfarin inhibition of vitamin K 2,3-epoxide reductase in rat liver microsomesQ71138461
Indirect inhibition of vitamin K epoxide reduction by salicylateQ72590969
Vitamin K dependent carboxylase: subcellular location of the carboxylase and enzymes involved in Vitamin K metabolism in rat liverQ72848541
Identification of a warfarin-sensitive protein component in a 200S rat liver microsomal fraction catalyzing vitamin K and vitamin K 2,3-epoxide reductionQ93669761
Enzymatic reduction of alloxan by thioredoxin and NADPH-thioredoxin reductaseQ36405226
Protein disulfide isomerase: multiple roles in the modification of nascent secretory proteinsQ38274381
Tissue distribution and subcellular localization of bovine thioredoxin determined by radioimmunoassayQ39627376
Vitamin K epoxide and quinone reductase activities. Evidence for reduction by a common enzymeQ41238980
P433issue3
P407language of work or nameEnglishQ1860
P921main subjectvitamin KQ182338
(E)-phytonadioneQ186093
P304page(s)257-259
P577publication date1992-07-01
1992-07-06
P1433published inFEBS LettersQ1388051
P1476titleIs thioredoxin the physiological vitamin K epoxide reducing agent?
P478volume305

Reverse relations

cites work (P2860)
Q28568888Characterization and purification of the vitamin K1 2,3 epoxide reductases system from rat liver
Q24337424Conserved loop cysteines of vitamin K epoxide reductase complex subunit 1-like 1 (VKORC1L1) are involved in its active site regeneration
Q40204873Disulfide-dependent protein folding is linked to operation of the vitamin K cycle in the endoplasmic reticulum. A protein disulfide isomerase-VKORC1 redox enzyme complex appears to be responsible for vitamin K1 2,3-epoxide reduction
Q39074534Functional Study of the Vitamin K Cycle Enzymes in Live Cells
Q36298281Human vitamin K epoxide reductase and its bacterial homologue have different membrane topologies and reaction mechanisms
Q52655392Membrane topology mapping of vitamin K epoxide reductase by in vitro translation/cotranslocation.
Q41862955Microsomal lipoamide reductase provides vitamin K epoxide reductase with reducing equivalents
Q33871717News and views on thioredoxin reductases
Q73788000Purification of warfarin-sensitive vitamin K epoxide reductase
Q37122098Structure and function of vitamin K epoxide reductase
Q34274107The thioredoxin system—From science to clinic
Q28274345The vitamin K cycle
Q37122109VKORC1: a warfarin-sensitive enzyme in vitamin K metabolism and biosynthesis of vitamin K-dependent blood coagulation factors
Q28583201Vitamin K 2,3-epoxide reductase and the vitamin K-dependent gamma-carboxylation system
Q41168727Warfarin traps human vitamin K epoxide reductase in an intermediate state during electron transfer.

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