Active Site

Asp/Glu racemase, active site (IPR018187)

Short name: Asp/Glu_racemase_AS

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.

GO terms

Biological Process

No terms assigned in this category.

Molecular Function

GO:0016855 racemase and epimerase activity, acting on amino acids and derivatives

Cellular Component

No terms assigned in this category.

Contributing signatures

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