{PDOC00714}
{PS00923; ASP_GLU_RACEMASE_1}
{PS00924; ASP_GLU_RACEMASE_2}
{BEGIN}
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* Aspartate and glutamate racemases signatures *
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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.

-Consensus pattern: [IVA]-[LIVM]-x-C-x(0,1)-N-[ST]-[MSA]-[STH]-[LIVFYSTANK]
                    [The C is an active site residue]
-Sequences known to belong to this class detected by the pattern: ALL.
-Other sequence(s) detected in Swiss-Prot: 5.

-Consensus pattern: [LIVM](2)-x-[AG]-C-T-[DEH]-[LIVMFY]-[PNGRS]-x-[LIVM]
                    [The C is an active site residue]
-Sequences known to belong to this class detected by the pattern: ALL.
-Other sequence(s) detected in Swiss-Prot: NONE.

-Last update: May 2004 / Text revised.

[ 1] Gallo K.A., Knowles J.R.
     "Purification, cloning, and cofactor independence of glutamate
     racemase from Lactobacillus."
     Biochemistry 32:3981-3990(1993).
     PubMed=8385993
{END}