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Article

Disruption of an ATP-dependent isomerization of the recA protein by mutation of histidine 163.

The Journal of biological chemistry - 15 Jan 1991

Muench K A, Bryant F R

Abstract excerpt

We have used site-directed mutagenesis to replace histidine 163 of the recA polypeptide with an alanine residue. The new [Ala-163]recA protein catalyzes single-stranded (ss) DNA-dependent ATP hydrolysis with a turnover number that is similar to that of the wild-type recA protein. Despite being proficient in ssDNA-dependent ATP hydrolysis, the [Ala-163]recA protein is unable to promote the ATP-dependent...

Topics

Adenosine Triphosphatases
Adenosine Triphosphate
Alanine
DNA, Bacterial
DNA, Single-Stranded
Electrophoresis, Polyacrylamide Gel
Escherichia coli
Histidine
Hydrogen-Ion Concentration
Hydrolysis
Isomerism

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Mutation

Rec A Recombinases

Source

Identifiers

PMID: 1824702

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 29 Aug 2026. Prepared record publication-1824702-2026-08-29.1. Manifest publication-graph-cohort-2026-08-29.1.

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

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Disruption of an ATP-dependent isomerization of the recA protein by mutation of histidine 163.PMID 1824702Read ↗

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