Home  |  Contact
PROSITE documentation PDOC00714 [for PROSITE entry PS00923]

Aspartate and glutamate racemases signatures





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 [1]. 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.

Technical section

PROSITE methods (with tools and information) covered by this documentation:

ASP_GLU_RACEMASE_1, PS00923; Aspartate and glutamate racemases signature 1  (PATTERN)

ASP_GLU_RACEMASE_2, PS00924; Aspartate and glutamate racemases signature 2  (PATTERN)


Reference

1AuthorsGallo K.A. Knowles J.R.
TitlePurification, cloning, and cofactor independence of glutamate racemase from Lactobacillus.
SourceBiochemistry 32:3981-3990(1993).
PubMed ID8385993



PROSITE is copyright. It is produced by the SIB Swiss Institute Bioinformatics. There are no restrictions on its use by non-profit institutions as long as its content is in no way modified. Usage by and for commercial entities requires a license agreement. For information about the licensing scheme send an email to
Prosite License or see: prosite_license.html.

Miscellaneous

View entry in original PROSITE document format
View entry in raw text format (no links)