5.1.1.3	D-glutamate	catalytic action of glutamate racemase is driven by its own substrate, D-glutamate	
5.1.1.3	D-glutamate	enzyme catalyzes the formation of D-glutamate from L-glutamate through a 1,1-proton transfer mechanism which reversibly inverts the stereochemistry at the alpha-carbon of glutamate	
5.1.1.3	L-2-aminoadipic acid	-	
5.1.1.3	L-Glu	glutamate racemase is mainly concerned in D-Glu synthesis for poly-gamma-glutamate production	
5.1.1.3	L-Glu	the biosynthesis of D-Glu, one of the essential components of bacterial cell-wall peptidoglycan, is catalyzed by glutamate racemase	
5.1.1.3	L-glutamate	-	
5.1.1.3	L-glutamate	the enzyme is responsible for the synthesis of D-glutamate, an essential building block of the peptidoglycan layer in bacterial cell walls	
5.1.1.3	L-glutamate	enzyme catalyzes the formation of D-glutamate from L-glutamate through a 1,1-proton transfer mechanism which reversibly inverts the stereochemistry at the alpha-carbon of glutamate	
5.1.1.3	additional information	the enzyme is an endogenous DNA gyrase inhibitor	
5.1.1.3	additional information	enzyme exhibits both racemization activity and DNA gyrase inhibition. The two activities are unlinked and independent of each other. Enzyme-DNA gyrase interaction influences gyrase activity but has no effect on the racemization activity	
5.1.1.3	additional information	in addition to racemization activity, enzyme exhibits DNA gyrase activity by preventing DNA binding of gyrase. Sequestration of gyrase results in inhibition of all reactions catalyzed by DNA gyrase. Overexpression additiionally provides protection against ciprofloxacin	
5.1.1.3	additional information	Chlamydia trachomatis dapF encodes a bifunctional enzyme capable of both D-glutamate racemase and diaminopimelate epimerase, EC 5.1.1.7, activities. Diaminopimelate and glutamate appear to be competitive substrates, indicating that they share an active site despite the racemase reaction requiring the PLP cofactor	
5.1.1.3	additional information	the enzyme is a physiologically bifunctional alanine/glutamate racemase (EC 5.1.1.1/EC 5.1.1.3), it is not highly active, but it is clearly sufficient. The metC encoded L-alanine/L-glutamate racemase is a multifunctional CBL/ALR. CBL (EC 4.4.1.13) activity is no longer required in these bacteria