Cloning, characterization, and expression in Escherichia coli of a gene encoding Listeria seeligeri catalase, a bacterial enzyme highly homologous to mammalian catalases.

doi:10.1128/jb.173.16.5159-5167.1991

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Article

Cloning, characterization, and expression in Escherichia coli of a gene encoding Listeria seeligeri catalase, a bacterial enzyme highly homologous to mammalian catalases.

Journal of bacteriology - 1 Aug 1991

Haas A, Brehm K, Kreft J, Goebel W

Abstract excerpt

A gene coding for catalase (hydrogen-peroxide:hydrogen-peroxide oxidoreductase; EC 1.11.1.6) of the gram-positive bacterium Listeria seeligeri was cloned from a plasmid library of EcoRI-digested chromosomal DNA, with Escherichia coli DH5 alpha as a host. The recombinant catalase was expressed in E. coli to an enzymatic activity approximately 50 times that of the combined E. coli catalases. The nucleotide sequence...

Topics

Amino Acid Sequence
Animals
Base Sequence
Blotting, Southern
Catalase
Chromosome Deletion
Cloning, Molecular
Escherichia coli
Humans
Listeria
Mammals

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Molecular Sequence Data

Mutation

Plants

Recombinant Proteins

Repetitive Sequences, Nucleic Acid

Sequence Homology, Nucleic Acid

Yeasts

Source

Open in PubMed Open full text

Identifiers

PMID: 1860824
DOI: 10.1128/jb.173.16.5159-5167.1991
PMCID: PMC208208

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 29 Aug 2026. Prepared record publication-1860824-2026-08-29.1. Manifest publication-graph-cohort-2026-08-29.1.

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

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