PMID:3288628
| Citation |
Russel, M and Model, P (1988) Sequence of thioredoxin reductase from Escherichia coli. Relationship to other flavoprotein disulfide oxidoreductases. J. Biol. Chem. 263:9015-9 |
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| Abstract |
The DNA sequence of the Escherichia coli gene encoding thioredoxin reductase has been determined. The predicted protein sequence agrees with an earlier determination of the 17 amino-terminal amino acids and with a fragment of the protein containing the redox-active half-cystines. Similarity between E. coli thioredoxin reductase and other flavoprotein disulfide oxidoreductases is quite limited, but three short segments, two of which are probably involved in FAD and NADPH binding, are highly conserved between thioredoxin reductase, glutathione reductase, dihydrolipoamide dehydrogenase, and mercuric reductase. |
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| Keywords |
Amino Acid Sequence; Base Sequence; Binding Sites; DNA, Bacterial/genetics; Disulfides/metabolism; Escherichia coli/enzymology; Flavoproteins/metabolism; Genes; Genes, Bacterial; Molecular Sequence Data; NADH, NADPH Oxidoreductases/genetics; Sequence Homology, Nucleic Acid; Thioredoxin-Disulfide Reductase/genetics |
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