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PROSITE documentation PDOC00714

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.

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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



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