EC Number   |
Protein Variants |
Reference |
|---|
    2.3.1.9 | C377A |
site-directed mutagenesis, almost inactive mutant |
-, 736252 |
| 2.3.1.9 | C378A |
site-directed mutagenesis, almost inactive mutant |
735609 |
| 2.3.1.9 | C378G |
mutation eliminates the ability of thiolase to catalyze proton abstraction from C2 of acetyl-CoA |
487683 |
| 2.3.1.9 | C89A |
no thiolytic activity towards acetoacetyl-CoA |
487701 |
| 2.3.1.9 | C89A |
site-directed mutagenesis, almost inactive mutant |
-, 736252 |
| 2.3.1.9 | C91A |
site-directed mutagenesis, almost inactive mutant |
-, 735609 |
| 2.3.1.9 | C92S |
kcat decreases to 0.2% of that for the recombinant thiolase |
486875 |
| 2.3.1.9 | E252del |
25% of wild-type activity at 37°C, 40% of wild-type activity at 30°C. Mutant is unstable compared to the wild-type protein at 37°C. KM-value for acetoacetyl-CoA is 2fold higher than wild-type value. Km-value for CoA is 1.8fold lower than wild-type value |
676035 |
| 2.3.1.9 | E252del |
no residual activity under any condition |
676035 |
| 2.3.1.9 | E252del |
relative protein amount and enzyme activity of 30% and 25% respectively, in comparison to the wild-type at 37°C. 2fold Km-elevation for substrates coenzyme A and acetoacetyl-CoA compared to wild-type values. Vmax is comparable to wild-type value |
676035 |
