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Review
. 1999 Mar;181(5):1375-9.
doi: 10.1128/JB.181.5.1375-1379.1999.

The thioredoxin superfamily: redundancy, specificity, and gray-area genomics

F Aslund  1 , J Beckwith
Affiliations
Review

The thioredoxin superfamily: redundancy, specificity, and gray-area genomics

F Aslund et al. J Bacteriol. 1999 Mar.
No abstract available

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Figures

FIG. 1
FIG. 1
Members of the thioredoxin superfamily in E. coli. Members of the family are boxed. Reduction (black arrow), oxidation (broken arrow), and disulfide bond isomerization (two arrows) are indicated. Three members of this family (NrdH, DsbG, and DsbE) are not shown, as their roles in these pathways are not clear.
See this image and copyright information in PMC

References

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    1. Anfinsen C B, Haber E, Sela M, White F H., Jr The kinetics of formation of native ribonuclease during oxidation of the reduced polypeptide chain. Proc Natl Acad Sci USA. 1961;47:1309–1314. - PMC - PubMed
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    1. Åslund F, Ehn B, Miranda-Vizuete A, Pueyo C, Holmgren A. Two additional glutaredoxins exist in Escherichia coli: glutaredoxin 3 is a hydrogen donor for ribonucleotide reductase in a thioredoxin/glutaredoxin 1 double mutant. Proc Natl Acad Sci USA. 1994;91:9813–9817. - PMC - PubMed
    1. Bardwell J C A, Lee J-O, Jander G, Martin N, Belin D, Beckwith J. A pathway for disulfide bond formation in vivo. Proc Natl Acad Sci USA. 1993;90:1038–1042. - PMC - PubMed

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