EC Number |
Natural Substrates |
---|
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 | more |
the enzyme is an endogenous DNA gyrase inhibitor |
5.1.1.3 | more |
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 |