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Article

Functional properties of the two redox-active sites in yeast protein disulphide isomerase in vitro and in vivo.

Journal of molecular biology - 5 Mar 1999

Westphal V, Darby N J, Winther J R

Abstract excerpt

Protein folding catalysed by protein disulphide isomerase (PDI) has been studied both in vivo and in vitro using different assays. PDI contains a CGHC active site in each of its two catalytic domains (a and a'). The relative importance of each active site in PDI from Saccharomyces cerevisiae (yPDI) has been analysed by exchanging the active-site cysteine residues for serine residues. The activity of the mutant...

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Identifiers

PMID: 10047493
DOI: 10.1006/jmbi.1999.2560

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-07.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

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