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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.

SUBMITTER: Strych U 

PROVIDER: S-EPMC135199 | biostudies-literature | 2002 Aug

REPOSITORIES: biostudies-literature

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

Strych Ulrich U   Benedik Michael J MJ  

Journal of bacteriology 20020801 15


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. ...[more]

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