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Literature summary extracted from
- Inhibition studies of the enantiomers of beta-chloroalanine on purified alanine racemase from Bacillus subtilis (1976), Biochem. Biophys. Res. Commun., 68, 793-798.
Inhibitors
| EC Number | Inhibitors | Comment | Organism | Structure |
|---|---|---|---|---|
| 5.1.1.1 | D-Chloroalanine | Ki: 0.005 mM, competitive | Bacillus subtilis |  |
| 5.1.1.1 | L-chloroalanine | Ki: 1.71 mM, noncompetitive | Bacillus subtilis | |
Organism
| EC Number | Organism | UniProt | Comment | Textmining |
|---|---|---|---|---|
| 5.1.1.1 | Bacillus subtilis | - |
- |
- |
Reaction
| EC Number | Reaction | Comment | Organism | Reaction ID |
|---|---|---|---|---|
| 5.1.1.1 | L-alanine = D-alanine | the active site of the alanine racemase reacts asymmetrically with the enantiomers of the substrate and has a conformation which greatly favors the D-enantiomer | Bacillus subtilis |
Substrates and Products (Substrate)
| EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|---|
| 5.1.1.1 | L-Ala | - |
Bacillus subtilis | D-Ala | - |
? | |
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