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Article

Combinations of protein-disulfide isomerase domains show that there is little correlation between isomerase activity and wild-type growth.

The Journal of biological chemistry - 27 Jul 2001

Xiao R, Solovyov A, Gilbert H F, Holmgren A, Lundström-Ljung J

Abstract excerpt

Protein-disulfide isomerase (PDI) has five domains: a, b, b', a' and c, all of which except c have a thioredoxin fold. A single catalytic domain (a or a') is effective in catalyzing oxidation of a reduced protein but not isomerization of disulfides (Darby, N. J., and Creighton, T. E. (1995) Biochemistry 34, 11725-11735). To examine the structural basis for this oxidase and isomerase activity of PDI, shuffled...

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PMID: 11375405
DOI: 10.1074/jbc.M104203200

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 5 Sept 2026. Manifest publication-graph-cohort-2026-09-05.1.

Source receipt: pubmed, retrieved 5 Sept 2026.

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