The penultimate selenocysteine residue at the C-terminus of mammalian thioredoxin reductase plays an obligatory role in the NADPH-disulfide oxidoreductase catalytic mechanism.
Gorlatov
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Laboratory of Biochemistry, National Heart, Lung and Blood Institute, National Institutes of Health, Bethesda, MD 20892, USA.
Stadtman
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TC
D000818:Animals; D001665:Binding Sites; D002384:Catalysis; D004220:Disulfides / Q000378:metabolism*; D006801:Humans; D009247:NADH, NADPH Oxidoreductases / Q000378:metabolism*; D017279:Selenocysteine / Q000378:metabolism*; D013329:Structure-Activity Relationship; D013880:Thioredoxin-Disulfide Reductase / Q000737:chemistry* / Q000378:metabolism*
D004220:Disulfides; D017279:Selenocysteine; D009247:NADH, NADPH Oxidoreductases; D013880:Thioredoxin-Disulfide Reductase