Active Site

Asp/Glu racemase, active site 1 (IPR018187)

Short name: Asp/Glu_racemase_AS_1

Description

Aspartate racemase (EC:5.1.1.13) and glutamate racemase (EC:5.1.1.3) are two evolutionary related bacterial enzymes that do not seem to require a cofactor for their activity [PMID: 8385993]. 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.

Contributing signatures

Signatures from InterPro member databases are used to construct an entry.
PROSITE patterns