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Article

Conversion of a catalytic into a structural disulfide bond by circular permutation.

Biochemistry - 15 Dec 1998

Hennecke J, Glockshuber R

Abstract excerpt

The thiol-disulfide oxidoreductase DsbA from Escherichia coli is the strongest oxidant of the enzyme family and required for disulfide bond formation in the bacterial periplasm. The catalytic domain of this 189-residue protein has a thioredoxin-like fold and contains a catalytic disulfide bridge that is located within the sequence Cys30-Pro31-His32-Cys33 at the N-terminus of an alpha-helix. The Cys30-Cys33...

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Source

Identifiers

PMID: 9860875
DOI: 10.1021/bi981888v

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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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