Is thioredoxin the physiological vitamin K epoxide reducing agent?
E. coli thioredoxin plus thioredoxin reductase have previously been shown to replace dithiothreitol as the electron donor for mammalian liver microsomal vitamin K epoxide reduction in vitro. Such activity is dependent on detergent disruption of the microsomal membrane integrity. A previously characterized salicylate-inhibitable pathway for electron transfer from endogenous cytosolic reducing agents to the microsomal epoxide reducing warfarin-inhibitable enzyme is not inhibited by known alternate substrates and inhibitors of the thioredoxin system nor by antibodies against thioredoxin.
Preusch
P C
PC
Department of Chemistry, University of Akron, OH 44325.
D000818:Animals; D003600:Cytosol / Q000378:metabolism; D006041:Goats; D007106:Immune Sera; D066298:In Vitro Techniques; D008862:Microsomes, Liver / Q000378:metabolism; D006899:Mixed Function Oxygenases / Q000378:metabolism; D010084:Oxidation-Reduction; D051381:Rats; D013880:Thioredoxin-Disulfide Reductase / Q000378:metabolism; D013879:Thioredoxins / Q000276:immunology / Q000378:metabolism*; D010837:Vitamin K 1 / Q000031:analogs & derivatives* / Q000378:metabolism; D064417:Vitamin K Epoxide Reductases
D007106:Immune Sera; C016186:vitamin K1 oxide; D013879:Thioredoxins; D010837:Vitamin K 1; D006899:Mixed Function Oxygenases; D064417:Vitamin K Epoxide Reductases; D013880:Thioredoxin-Disulfide Reductase