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Article

Functional analysis of paralogous thiol-disulfide oxidoreductases in Bacillus subtilis.

The Journal of biological chemistry - 27 Aug 1999

Bolhuis A, Venema G, Quax W J, Bron S, van Dijl J M

Abstract excerpt

The in vivo formation of disulfide bonds, which is critical for the stability and/or activity of many proteins, is catalyzed by thiol-disulfide oxidoreductases. In the present studies, we show that the Gram-positive eubacterium Bacillus subtilis contains three genes, denoted bdbA, bdbB, and bdbC, for thiol-disulfide oxidoreductases. Escherichia coli alkaline phosphatase, containing two disulfide bonds, was...

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PMID: 10455116
DOI: 10.1074/jbc.274.35.24531

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

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