title: The Escherichia coli Dga (MurI) protein shares biological activity and structural domains with the Pediococcus pentosaceus glutamate racemase.
abstract: The Pediococcus pentosaceus glutamate racemase gene product complemented the D-glutamate auxotrophy of Escherichia coli WM335. Amino acid sequence analysis of the two proteins revealed 28% identity, primarily in six clusters scattered throughout the sequence. Further analyses indicated secondary structure similarities between the two proteins. These data support a recent report that the dga (murI) gene product is a glutamate racemase.
authors.affiliation: Department of Microbiology, Bristol-Myers Squibb Research Institute, Wallingford, Connecticut 06492-7660.
authors.forename: M J
authors.initials: MJ
authors.lastname: Pucci
authors.forename: J
authors.initials: J
authors.lastname: Novotny
authors.forename: L F
authors.initials: LF
authors.lastname: Discotto
authors.forename: T J
authors.initials: TJ
authors.lastname: Dougherty
mesh_terms: D000591:Amino Acid Isomerases / Q000235:genetics*; D000595:Amino Acid Sequence; D004926:Escherichia coli / Q000201:enzymology / Q000235:genetics*; D005816:Genetic Complementation Test; D005971:Glutamates / Q000378:metabolism; D018698:Glutamic Acid; D008969:Molecular Sequence Data; D010376:Pediococcus / Q000201:enzymology / Q000235:genetics*; D017433:Protein Structure, Secondary; D017386:Sequence Homology, Amino Acid
chemical_list: D005971:Glutamates; D018698:Glutamic Acid; D000591:Amino Acid Isomerases; C062292:glutamate racemase