v5.1.0.3
Glycine data from LIS
Type | Active_site |
Description | Aspartate racemase ( ) and glutamate racemase ( ) are two evolutionary related bacterial enzymes that do not seem to require a cofactor for their activity [ ]. Glutamate racemase, which interconverts L-glutamate into D-glutamate, is required for the biosynthesis of peptidoglycan and some peptide-based antibiotics such as gramicidin S.In addition to characterised aspartate and glutamate racemases, this family also includes a hypothetical protein from Erwinia carotovora and one from Escherichia coli (ygeA). Two conserved cysteines are present in the sequence of these enzymes. They are expected to play a role in catalytic activity by acting as bases in proton abstraction from the substrate. This entry represents a conserved region containing the first cysteine. |
Short Name | Asp/Glu_racemase_AS_1 |