Literature summary for 5.1.1.3 extracted from

Puig, E.; Garcia-Viloca, M.; Gonzalez-Lafont, A.; Lluch, J.M.; Field, M.J.
New insights into the reaction mechanism catalyzed by the glutamate racemase enzyme: pH titration curves and classical molecular dynamics simulations (2007), J. Phys. Chem. B, 111, 2385-2397.

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Organism

Organism	UniProt	Comment	Textmining
Aquifex pyrophilus	P56868	-	-

Reaction

Reaction	Comment	Organism	Reaction ID
L-glutamate = D-glutamate	glutamate racemase faces the difficult task of deprotonating a relatively low acidicity proton, the amino acids R-hydrogen, with a relatively poor base, a cysteine. The titration curves and the pK1/2 values of all of the ionizable residues for different structures leading from reactants to products are analyzed. From these results a concerted mechanism is proposed in which the Cys70 residue deprotonates the R-hydrogen of the substrate while, at the same time, being deprotonated by the Asp7 residue	Aquifex pyrophilus	a

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
L-glutamate	-	Aquifex pyrophilus	D-glutamate	-	?

Synonyms

Synonyms	Comment	Organism
glutamate racemase	-	Aquifex pyrophilus
MurI	-	Aquifex pyrophilus

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Release 2023.1 (January 2023)