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Article

DsbA-DsbB interaction through their active site cysteines. Evidence from an odd cysteine mutant of DsbA.

The Journal of biological chemistry - 21 Jul 1995

Kishigami S, Kanaya E, Kikuchi M, Ito K

Abstract excerpt

Formation of disulfide bonds in Escherichia coli envelope proteins is facilitated by the Dsb system, which is thought to consist of at least two components, a periplasmic soluble enzyme (DsbA) and a membrane-bound factor (DsbB). Although it is believed that DsbA directly oxidizes substrate cysteines and DsbB reoxidizes DsbA to allow multiple rounds of reactions, direct evidence for the DsbA-DsbB interaction has...

Topics

Amino Acid Sequence
Bacterial Proteins
Base Sequence
Binding Sites
Cysteine
Glutathione
Glutathione Disulfide
Isomerases
Membrane Proteins
Molecular Sequence Data
Mutation

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Protein Disulfide-Isomerases

Structure-Activity Relationship

Source

Identifiers

PMID: 7615498
DOI: 10.1074/jbc.270.29.17072

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 29 Aug 2026. Prepared record publication-7615498-2026-08-29.1. Manifest publication-graph-cohort-2026-08-29.1.

Source receipt: PubMed via Helena Literature Corpus, retrieved 29 Aug 2026.

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DsbA-DsbB interaction through their active site cysteines. Evidence from an odd cysteine mutant of DsbA.PMID 7615498Read ↗

Roles of cysteine residues of DsbB in its activity to reoxidize DsbA, the protein disulphide bond catalyst of Escherichia coli.Semantic proximity Read ↗

Respiratory chain strongly oxidizes the CXXC motif of DsbB in the Escherichia coli disulfide bond formation pathway.Semantic proximity Read ↗

Mutational analysis of the disulfide catalysts DsbA and DsbB.Semantic proximity Read ↗

Mutants in DsbB that appear to redirect oxidation through the disulfide isomerization pathway.Semantic proximity Read ↗

The disulphide isomerase DsbC cooperates with the oxidase DsbA in a DsbD-independent manner.Semantic proximity Read ↗

Roles of a conserved arginine residue of DsbB in linking protein disulfide-bond-formation pathway to the respiratory chain of Escherichia coli.Semantic proximity Read ↗

Paradoxical redox properties of DsbB and DsbA in the protein disulfide-introducing reaction cascade.Semantic proximity Read ↗

Identification of a segment of DsbB essential for its respiration-coupled oxidation.Semantic proximity Read ↗

Role of the cytosolic loop of DsbB in catalytic turnover of the ubiquinone-DsbB complex.Semantic proximity Read ↗

Reduction of the periplasmic disulfide bond isomerase, DsbC, occurs by passage of electrons from cytoplasmic thioredoxin.Semantic proximity Read ↗

Six conserved cysteines of the membrane protein DsbD are required for the transfer of electrons from the cytoplasm to the periplasm of Escherichia coli.Semantic proximity Read ↗

An in vivo pathway for disulfide bond isomerization in Escherichia coli.Semantic proximity Read ↗

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