Crystallization (Comment) | Organism |
---|---|
crystal structure analysis, overview | Helicobacter pylori |
Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
L-glutamate | Helicobacter pylori | - |
D-glutamate | - |
r |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Helicobacter pylori | - |
- |
- |
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 | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
L-glutamate | - |
Helicobacter pylori | D-glutamate | - |
r |
Synonyms | Comment | Organism |
---|---|---|
HpMurI | - |
Helicobacter pylori |
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 |