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| | Physiological functions of thioredoxin and thioredoxin reductase -- Arnér and Holmgren 267 (20): 6102 -- FEBS ... (Site not responding. Last check: 2007-10-09) |
 | | The sequences in the N-terminal FAD domain encompassing the active site disulfide motif identical to that of glutathione reductase, and the C-terminal elongation with selenocysteine and its neighbouring cysteine residue, are shown by one-letter amino-acid abbreviations with U identifying the selenocysteine [49,57]. |
 | | Kumar, S., Björnstedt, M. and Holmgren, A. (1992) Selenite is a substrate for calf thymus thioredoxin reductase and thioredoxin and elicits a large non-stoichiometric oxidation of NADPH in the presence of oxygen. |
 | | Arscott, L.D., Gromer, S., Schirmer, R.H., Becker, K. and Williams, C.H. Jr (1997) The mechanism of thioredoxin reductase from human placenta is similar to the mechanisms of lipoamide dehydrogenase and glutathione reductase and is distinct from the mechanism of thioredoxin reductase from Escherichia coli. |
| content.febsjournal.org /cgi/content/full/267/20/6102 (5516 words) |
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