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Article

Characterization of the PduS cobalamin reductase of Salmonella enterica and its role in the Pdu microcompartment.

Journal of bacteriology - 1 Oct 2010

Cheng Shouqiang, Bobik Thomas A

Abstract excerpt

Salmonella enterica degrades 1,2-propanediol (1,2-PD) in a coenzyme B12 (adenosylcobalamin, AdoCbl)-dependent fashion. Salmonella obtains AdoCbl by assimilation of complex precursors, such as vitamin B12 and hydroxocobalamin. Assimilation of these compounds requires reduction of their central cobalt atom from Co3+ to Co2+ to Co+, followed by adenosylation to AdoCbl. In this work, the His6-tagged PduS cobalamin...

Topics

Amino Acid Sequence
Bacterial Proteins
Blotting, Western
Cations, Divalent
Chromatography, Gel
Electrophoresis, Polyacrylamide Gel
Genetic Complementation Test
Hydrogen-Ion Concentration
Kinetics
Models, Biological

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Molecular Sequence Data

Phenotype

Protein Binding

Salmonella enterica

Sequence Homology, Amino Acid

Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization

Tandem Mass Spectrometry

Temperature

Source

Open in PubMed Open full text

Identifiers

PMID: 20656910
DOI: 10.1128/JB.00575-10
PMCID: PMC2944522

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Characterization of the PduS cobalamin reductase of Salmonella enterica and its role in the Pdu microcompartment.PMID 20656910Read ↗

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