|PROSITE documentation PDOC00714 [for PROSITE entry PS00923]|
Aspartate racemase (EC 220.127.116.11) and glutamate racemase (EC 18.104.22.168) 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 characterized 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. We developed signature patterns for both cysteines.Last update:
May 2004 / Text revised.
PROSITE methods (with tools and information) covered by this documentation:
|1||Authors||Gallo K.A. Knowles J.R.|
|Title||Purification, cloning, and cofactor independence of glutamate racemase from Lactobacillus.|