Molecular characterization of katA from Campylobacter jejuni and generation of a catalase-deficient mutant of Campylobacter coli by interspecific allelic exchange.

doi:10.1099/13500872-141-6-1369

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Article

Molecular characterization of katA from Campylobacter jejuni and generation of a catalase-deficient mutant of Campylobacter coli by interspecific allelic exchange.

Microbiology (Reading, England) - 1 Jun 1995

Grant Kathleen A, Park Simon F

Abstract excerpt

A gene encoding catalase (hydrogen-peroxide:hydrogen-peroxide oxidoreductase; EC 1.11.1.6) from Campylobacter jejuni was cloned by functional complementation of a catalase-deficient mutant of Escherichia coli. The catalase structural gene, designated katA, was assigned by subcloning and its nucleotide sequence determined. The deduced protein product of 508 amino acids, which had a calculated molecular mass of...

Topics

Alleles
Amino Acid Sequence
Bacterial Proteins
Base Sequence
Campylobacter coli
Campylobacter jejuni
Catalase
Drug Resistance, Microbial
Enzyme Induction
Escherichia coli
Gene Expression Regulation, Bacterial

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Genes, Bacterial

Genetic Complementation Test

Hydrogen Peroxide

Molecular Sequence Data

Molecular Weight

Sequence Alignment

Sequence Homology, Amino Acid

Source

Open in PubMed

Identifiers

PMID: 7670638
DOI: 10.1099/13500872-141-6-1369

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 29 Aug 2026. Prepared record publication-7670638-2026-08-29.1. Manifest publication-graph-cohort-2026-08-29.1.

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

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