The Escherichia coli Dga (MurI) protein shares biological activity and structural domains with the Pediococcus pentosaceus glutamate racemase.
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.
Pucci
M J
MJ
Department of Microbiology, Bristol-Myers Squibb Research Institute, Wallingford, Connecticut 06492-7660.
Novotny
J
J
Discotto
L F
LF
Dougherty
T J
TJ
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
D005971:Glutamates; D018698:Glutamic Acid; D000591:Amino Acid Isomerases; C062292:glutamate racemase