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Is thioredoxin the physiological vitamin K epoxide reducing agent?
Author(s) -
Preusch Peter C.
Publication year - 1992
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(92)80681-6
Subject(s) - dithiothreitol , thioredoxin , microsome , biochemistry , thioredoxin reductase , chemistry , enzyme , reducing agent , vitamin k epoxide reductase , reductase , ferredoxin thioredoxin reductase , cytosol , cytochrome p450 , cyp2c9 , organic chemistry
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 cylosolic 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.