Mutant analysis shows that alanine racemases from Pseudomonas aeruginosa and Escherichia coli are dimeric.
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.
Strych
Ulrich
U
Department of Biology and Biochemistry, University of Houston, Houston, Texas 77204-5001, USA.
Benedik
Michael J
MJ
D000411:Alanine Racemase / Q000737:chemistry / Q000235:genetics*; D004926:Escherichia coli / Q000201:enzymology* / Q000254:growth & development; D008969:Molecular Sequence Data; D009154:Mutation; D011550:Pseudomonas aeruginosa / Q000201:enzymology*
D000411:Alanine Racemase