Mutant analysis shows that alanine racemases from Pseudomonas aeruginosa and Escherichia coli are dimeric.

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.

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Cite this paper

@article{Strych2002MutantAS, title={Mutant analysis shows that alanine racemases from Pseudomonas aeruginosa and Escherichia coli are dimeric.}, author={Ulrich Strych and Michael J. Benedik}, journal={Journal of bacteriology}, year={2002}, volume={184 15}, pages={4321-5} }