1887

Abstract

Many bacteria, including , have a unique gene that encodes glutamate racemase. This enzyme catalyses the formation of -glutamate, which is necessary for cell wall peptidoglycan synthesis. However, has two glutamate racemase genes, named and . Since appears to be indispensable for growth in rich medium, the role of in -amino acid synthesis is vague. Experiments with - and -knockout mutants confirmed that is essential for growth in rich medium but showed that this gene was dispensable for growth in minimal medium, where executes the anaplerotic role of . LacZ fusion assays demonstrated that was expressed in both types of media but was expressed only in minimal medium, which accounted for the absence of function in rich medium. Neither nor was required for cells to synthesize poly---glutamate (-PGA), a capsule polypeptide of - and -glutamate linked through a -carboxylamide bond. Wild-type cells degraded the capsule during the late stationary phase without accumulating the degradation products, -glutamate and -glutamate, in the medium. In contrast, or mutant cells accumulated significant amounts of - but not -glutamate. Exogenous -glutamate utilization was somewhat defective in the mutants and the double mutation of and severely impaired -amino acid utilization. Thus, both racemase genes appear necessary to complete the catabolism of exogenous -glutamate generated from -PGA.

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2004-09-01
2019-11-17
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