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InterPro: IPR018187 Asp/Glu racemase, active site

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2424 proteins

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Accession

IPR018187 Asp/Glu_racemase_AS

Type

Active_site

Signatures Help

Database	ID	Name	Proteins
PROSITE pattern	PS00923	ASP_GLU_RACEMASE_1	1880
PROSITE pattern	PS00924	ASP_GLU_RACEMASE_2	1952
Signatures in BioMart

InterPro Relationships Help

Found in

IPR001920 Asp/Glu racemase
IPR004380 Aspartate racemase
IPR004391 Glutamate racemase
IPR015942 Asp/Glu/hydantoin racemase

GO Term annotation Help

Function

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

InterPro annotation

Entry Details in BioMart

Abstract

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 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.

Structural links Help

PDB - click here

SCOP: c.78.2.1

CATH: 3.40.50.1860

Database links Help

Enzyme: EC:5.1.1.3

Taxonomic coverage Help

Overlapping InterPro entries Help

IPR018187

Numbers of overlapping proteins

Average numbers of overlapping amino acids

Example proteins Help

B0JGW5 Glutamate racemase

P22634 Glutamate racemase

P73737 Glutamate racemase

More proteins

Example Proteins Key

InterPro entry accession number/name and structure databases		Colour code
IPR001920	Asp/Glu racemase
IPR018187	Asp/Glu racemase, active site
IPR004391	Glutamate racemase
IPR015942	Asp/Glu/hydantoin racemase
	SWISS-MODEL
	PDB Chain
	ModBase

Publications Open in usermanual
1.	Gallo KA, Knowles JR. Purification, cloning, and cofactor independence of glutamate racemase from Lactobacillus. Biochemistry 32 3981-90 1993 [PubMed: 8385993] http://dx.doi.org/10.1021/bi00066a019

Additional Reading Open in usermanual
	May M, Mehboob S, Mulhearn DC, Wang Z, Yu H, Thatcher GR, Santarsiero BD, Johnson ME, Mesecar AD. Structural and functional analysis of two glutamate racemase isozymes from Bacillus anthracis and implications for inhibitor design. J. Mol. Biol. 371 2007 1219-37 [PubMed: 17610893] http://dx.doi.org/10.1016/j.jmb.2007.05.093
	Ruzheinikov SN, Taal MA, Sedelnikova SE, Baker PJ, Rice DW. Substrate-induced conformational changes in Bacillus subtilis glutamate racemase and their implications for drug discovery. Structure 13 2005 1707-13 [PubMed: 16271894] http://dx.doi.org/10.1016/j.str.2005.07.024
	Ohtaki A, Nakano Y, Iizuka R, Arakawa T, Yamada K, Odaka M, Yohda M. Structure of aspartate racemase complexed with a dual substrate analogue, citric acid, and implications for the reaction mechanism. Proteins 70 2008 1167-74 [PubMed: 17847084] http://dx.doi.org/10.1002/prot.21528
	Kim KH, Bong YJ, Park JK, Shin KJ, Hwang KY, Kim EE. Structural basis for glutamate racemase inhibition. J. Mol. Biol. 372 2007 434-43 [PubMed: 17658548] http://dx.doi.org/10.1016/j.jmb.2007.05.003
	Lundqvist T, Fisher SL, Kern G, Folmer RH, Xue Y, Newton DT, Keating TA, Alm RA, de Jonge BL. Exploitation of structural and regulatory diversity in glutamate racemases. Nature 447 2007 817-22 [PubMed: 17568739] http://dx.doi.org/10.1038/nature05689

InterPro 23.1