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Literature summary extracted from
- The inhibition of glutamate racemase by D-N-hydroxyglutamate (1997), Bioorg. Med. Chem. Lett., 7, 2265-2270.
No PubMed abstract available
Inhibitors
| EC Number | Inhibitors | Comment | Organism | Structure |
|---|---|---|---|---|
| 5.1.1.3 | D-N-Hydroxyglutamate | the compound acts as alternate substrate and is converted into 2-oxoglutarate and NH4+. Km: 0.057 mM, turnover number: 1080 min-1. An imine intermediate is likely the species causing the inhibition | Limosilactobacillus fermentum |  |
| 5.1.1.3 | L-N-Hydroxyglutamate | weak | Limosilactobacillus fermentum | |
Organism
| EC Number | Organism | UniProt | Comment | Textmining |
|---|---|---|---|---|
| 5.1.1.3 | Limosilactobacillus fermentum | - |
- |
- |
Reaction
| EC Number | Reaction | Comment | Organism | Reaction ID |
|---|---|---|---|---|
| 5.1.1.3 | L-glutamate = D-glutamate | the enzyme uses a two-base mechanism in which two Cys thiolates serve as the general base/acid catalysts. An initial deprotonation event produces a resonance-stabilized carbanionic intermediate that is subsequently protonated on the opposite face to generate the enantiomeric product | Limosilactobacillus fermentum |
Substrates and Products (Substrate)
| EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|---|
| 5.1.1.3 | D-Glu | - |
Limosilactobacillus fermentum | L-Glu | - |
? | |
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