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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.

SUBMITTER: Pucci MJ 

PROVIDER: S-EPMC205080 | biostudies-other | 1994 Jan

REPOSITORIES: biostudies-other

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The Escherichia coli Dga (MurI) protein shares biological activity and structural domains with the Pediococcus pentosaceus glutamate racemase.

Pucci M J MJ   Novotny J J   Discotto L F LF   Dougherty T J TJ  

Journal of bacteriology 19940101 2


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. ...[more]

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