Purification and initial characterization of the ATP:corrinoid adenosyltransferase encoded by the cobA gene of Salmonella typhimurium.

doi:10.1128/jb.177.4.921-925.1995

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Article

Purification and initial characterization of the ATP:corrinoid adenosyltransferase encoded by the cobA gene of Salmonella typhimurium.

Journal of bacteriology - 1 Feb 1995

Suh S, Escalante-Semerena J C

Abstract excerpt

The cobA gene of Salmonella typhimurium and its product were overexpressed to approximately 20% of the total cell protein. CobA was purified to 98% homogeneity; N-terminal sequence analysis (21 residues) of homogeneous protein confirmed the predicted amino acid sequence. ATP:corrinoid adenosyltransferase activity was demonstrated in vitro to be associated with CobA. This activity was optimal at pH 8 and 37...

Topics

Alkyl and Aryl Transferases
Amino Acid Sequence
Bacterial Proteins
Base Sequence
Cations, Divalent
Cobamides
Genes, Bacterial
Hot Temperature
Hydrogen-Ion Concentration
Kinetics
Molecular Sequence Data

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Mutation

Phenotype

Recombinant Proteins

Salmonella typhimurium

Sequence Analysis

Substrate Specificity

Transferases

Source

Open in PubMed Open full text

Identifiers

PMID: 7860601
DOI: 10.1128/jb.177.4.921-925.1995
PMCID: PMC176684

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 29 Aug 2026. Prepared record publication-7860601-2026-08-29.1. Manifest publication-graph-cohort-2026-08-29.1.

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

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Purification and initial characterization of the ATP:corrinoid adenosyltransferase encoded by the cobA gene of Salmonella typhimurium.PMID 7860601Read ↗

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