title: 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.
authors.affiliation: Department of Biology and Biochemistry, University of Houston, Houston, Texas 77204-5001, USA.
authors.forename: Ulrich
authors.initials: U
authors.lastname: Strych
authors.forename: Michael J
authors.initials: MJ
authors.lastname: Benedik
mesh_terms: 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*
chemical_list: D000411:Alanine Racemase