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Literature summary for 5.1.1.3 extracted from

  • Tanner, M.E.; Gallo, K.A.; Knowles, J.R.
    Isotope effects and the identification of catalytic residues in the reaction catalyzed by glutamate racemase (1993), Biochemistry, 32, 3998-4006.
    View publication on PubMed

Protein Variants

Protein Variants Comment Organism
C184A mutant C73A and C184A enzymes are inactive as racemases. However they are capable of catalyzing the elimination of HCl from opposite enantiomers of threo-3-chloroglutamic acid, a process that presumably requires only one enzymic base. It appears that Cys73 is responsible for the abstraction of the C-2 hydrogen from R-Glu and Cys184 abstracts the proton from S-glutamate in the racemization reaction of the wild type enzyme Lactobacillus sp.
C73A mutant C73A and C184A enzymes are inactive as racemases. However they are capable of catalyzing the elimination of HCl from opposite enantiomers of threo-3-chloroglutamic acid, a process that presumably requires only one enzymic base. It appears that Cys73 is responsible for the abstraction of the C-2 hydrogen from R-Glu and Cys184 abstracts the proton from S-glutamate in the racemization reaction of the wild type enzyme Lactobacillus sp.

Organism

Organism UniProt Comment Textmining
Lactobacillus sp.
-
-
-

Reaction

Reaction Comment Organism Reaction ID
L-glutamate = D-glutamate deprotonation/protonation mechanism for racemization in which the breaking of the carbon-hydrogen bond at C-2 is partially rate-determining Lactobacillus sp.

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
D-Glu
-
Lactobacillus sp. L-Glu
-
?