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Substrate specificity of alliinase from E. adhaerens FERM P-19486
| Substrate | Kinetic constants | ||
|---|---|---|---|
|
Vmaxa (units/mg) |
Km (mM) |
Vmax/Km | |
| (±)-Alliin | 90.0 | 2.3 | 39.1 |
| (+)-Alliin | 18.5 | 5.7 | 3.2 |
| S-Allyl-L-cysteine | 66.1 | 10.6 | 6.2 |
| S-Methyl-L-cysteine | 15.3 | -b | - |
| (±)-S-Methyl-L-cysteine sulfoxide | 53.6 | - | - |
| S-Ethyl-L-cysteine | 29.7 | - | - |
| L-Cysteine | 1.6 | - | - |
a The Vmax value was obtained by the rate of pyruvic acid production in the standard reaction mixture containing each substrate at 40 mM.
b Not tested.
