EC Number   |
Protein Variants |
Reference  |
|---|
    2.5.1.30 | more |
the hybrid-type combination of component I (Bacillus subtilis) and component II (Bacillus stearothermophilus) gives distinct prenyltransferase activity. The hybrid-type enzyme catalyzes the synthesis of heptaprenyl diphosphate and shows moderate heat stability, which is between those of the natural enzymes from Bacillus subtilis and Bacillus stearothermophilus. There is no possibility of forming a hybrid between the heptaprenyl and hexaprenyl diphosphate synthases |
637628 |
| 2.5.1.30 | D73A |
mutant shows similar Km-value for farnesyl diphosphate and Vmax-value compared to the wild-type |
637629 |
| 2.5.1.30 | D97A |
reaction products have marked differences in chain length distribution from the wild-type enzyme. D97A produces larger amounts of shorter chain prenyl diphosphates |
637629 |
| 2.5.1.30 | E128V |
mutant shows similar Km-value for farnesyl diphosphate and Vmax-value compared to the wild-type |
637629 |
| 2.5.1.30 | K130I |
mutant shows similar Km-value for farnesyl diphosphate and Vmax-value compared to the wild-type |
637629 |
| 2.5.1.30 | L94S |
9fold lower Vmax values and 7fold higher Km-values for the allylic substrate farnesyl diphosphate compared to wild-type enzyme |
637629 |
| 2.5.1.30 | N127A |
mutant shows similar Km-value for farnesyl diphosphate and Vmax-value compared to the wild-type |
637629 |
| 2.5.1.30 | T76V |
mutant shows similar Km-value for farnesyl diphosphate and Vmax-value compared to the wild-type |
637629 |
| 2.5.1.30 | V93G |
16fold lower Vmax values and 10fold higher Km-values for the allylic substrate farnesyl diphosphate compared to wild-type enzyme |
637629 |
| 2.5.1.30 | Y103S |
reaction products have marked differences in chain length distribution from the wild-type enzyme. Y103S gives octaprenyl diphosphate (C40) as the final product |
637629 |
