PMID:12107154

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Citation

Strych, U and Benedik, MJ (2002) Mutant analysis shows that alanine racemases from Pseudomonas aeruginosa and Escherichia coli are dimeric. J. Bacteriol. 184:4321-5

Abstract

Alanine racemases are ubiquitous prokaryotic enzymes providing the essential peptidoglycan precursor D-alanine. We present evidence that the enzymes from Pseudomonas aeruginosa and Escherichia coli function exclusively as homodimers. Moreover, we demonstrate that expression of a K35A Y235A double mutation of dadX in E. coli suppresses bacterial growth in a dominant negative fashion.

Links

PubMed PMC135199

Keywords

Alanine Racemase/chemistry; Alanine Racemase/genetics; Escherichia coli/enzymology; Escherichia coli/growth & development; Molecular Sequence Data; Mutation; Pseudomonas aeruginosa/enzymology

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