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Article

Eukaryotic protein disulfide isomerase complements Escherichia coli dsbA mutants and increases the yield of a heterologous secreted protein with disulfide bonds.

The Journal of biological chemistry - 3 May 1996

Ostermeier M, De Sutter K, Georgiou G

Abstract excerpt

Eukaryotic protein disulfide isomerase (PDI) is a 55-kDa enzyme with cysteine oxidoreductase, chaperone, and antichaperone activities that catalyzes disulfide formation and rearrangement in the eukaryotic endoplasmic reticulum. In Gram-negative bacteria, the formation of disulfide bonds in the pe...

Topics

Animals
Aprotinin
Catalysis
Disulfides
Escherichia coli
Genetic Complementation Test
Isomerases
Mutation
Oxidoreductases
Phenotype
Protein Disulfide-Isomerases
Protein Folding

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Identifiers

PMID: 8631865
DOI: 10.1074/jbc.271.18.10616

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 30 Aug 2026. Prepared record publication-8631865-2026-08-30.1. Manifest publication-graph-cohort-2026-08-30.1.

Source receipt: PubMed via Helena Literature Corpus, retrieved 30 Aug 2026.

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