EC Number   |
Natural Substrates |
|---|
    5.1.1.3 | L-2-aminoadipic acid |
- |
| 5.1.1.3 | L-glutamate |
- |
| 5.1.1.3 | D-glutamate |
catalytic action of glutamate racemase is driven by its own substrate, D-glutamate |
| 5.1.1.3 | more |
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 | 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-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 |
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 | L-Glu |
glutamate racemase is mainly concerned in D-Glu synthesis for poly-gamma-glutamate production |
| 5.1.1.3 | more |
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 | L-Glu |
the biosynthesis of D-Glu, one of the essential components of bacterial cell-wall peptidoglycan, is catalyzed by glutamate racemase |
