Literature summary extracted from

Mixcoha, E.; Garcia-Viloca, M.; Lluch, J.M.; Gonzalez-Lafont, A.
Theoretical analysis of the catalytic mechanism of Helicobacter pylori glutamate racemase (2012), J. Phys. Chem. B, 116, 12406-12414.

Crystallization (Commentary)

EC Number	Crystallization (Comment)	Organism
5.1.1.3	crystal structure analysis, overview	Helicobacter pylori

Natural Substrates/ Products (Substrates)

EC Number	Natural Substrates	Organism	Comment (Nat. Sub.)	Natural Products	Comment (Nat. Pro.)	Rev.	Reac.
5.1.1.3	L-glutamate	Helicobacter pylori	-	D-glutamate	-	r

Organism

EC Number	Organism	UniProt	Comment	Textmining
5.1.1.3	Helicobacter pylori	-	-	-

Reaction

EC Number	Reaction	Comment	Organism	Reaction ID
5.1.1.3	L-glutamate = D-glutamate	the molecular mechanism involves deprotonation of the glutamate alpha-proton, followed by substrate reprotonation on the opposite stereochemical face	Helicobacter pylori	a

Substrates and Products (Substrate)

EC Number	Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
5.1.1.3	L-glutamate	-	Helicobacter pylori	D-glutamate	-	r

Synonyms

EC Number	Synonyms	Comment	Organism
5.1.1.3	HpMurI	-	Helicobacter pylori

General Information

EC Number	General Information	Comment	Organism
5.1.1.3	additional information	mechanism of Helicobacter pylori glutamate racemase to generate the thermodynamically unfavorable reverse protonation state of the catalytic residue cysteine required for the proton abstraction from the alpha-carbon of glutamate, molecular dynamics simulations with a molecular mechanics force field along with QM/MM calculations starting from the crystal structure and from different MD snapshot, structural fluctuations of the enzyme-substrate complex, structural analysis of the four transition state structures,overview	Helicobacter pylori

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Release 2023.1 (January 2023)