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Literature summary for 5.1.1.3 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.
    View publication on PubMed

Crystallization (Commentary)

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

Natural Substrates/ Products (Substrates)

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

Organism

Organism UniProt Comment Textmining
Helicobacter pylori
-
-
-

Reaction

Reaction Comment Organism Reaction ID
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

Substrates and Products (Substrate)

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

Synonyms

Synonyms Comment Organism
HpMurI
-
Helicobacter pylori

General Information

General Information Comment Organism
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