EC Number   |
Protein Variants |
Reference |
|---|
   1.1.3.38 | D170S |
most active with branched-chain 4-alkylphenol, mutant enzyme favors the formation of alcohols |
655540 |
| 1.1.3.38 | D170S |
with vanilly alcohol, eugenol, and 4-(methoxymethyl)phenol the mutant enzyme is more than 1000fold less active than the wild-type enzyme |
654161 |
| 1.1.3.38 | D170S/T457E |
produces (S)-1-(4'-hydroxyphenyl)ethanol from 4-ethylphenol. The wild-type enzyme produces (R)-1-(4'-hydroxyphenyl)ethanol |
654161 |
| 1.1.3.38 | E502G |
the octamer/dimer ratio is 1:10. The catalytic efficiency of the mutant is significantly increased for ortho-substituted 4-methylphenols |
656232 |
| 1.1.3.38 | F424G |
mutant does not contain any flavin after purification |
763480 |
| 1.1.3.38 | F454Y |
as for wild-type enzyme the octamer/dimer ratio of the mutant enzyme is 1.5:1. The catalytic efficiency of the mutant is significantly increased for ortho-substituted 4-methylphenols |
656232 |
| 1.1.3.38 | H422A |
mutant enzyme retains activity, turnover rates decrease by 1 order of magnitude. Mutant enzyme is still able to form a stable binary complex of reduced enzyme and a quinone methide product intermediate, a crucial step during vanillyl-alcohol oxidase-mediated catalysis. Although mutation prevents covalent linkage of FAD, mutant enzyme contains tightly bound FAD |
655975 |
| 1.1.3.38 | H422C |
mutant enzyme retains activity, turnover rates decrease by 1 order of magnitude. Although mutation prevents covalent linkage of FAD, mutant enzyme contains tightly bound FAD |
655975 |
| 1.1.3.38 | H422T |
mutant enzyme retains activity, turnover rates decrease by 1 order of magnitude. Although mutation prevents covalent linkage of FAD, mutant enzyme contains tightly bound FAD |
655975 |
| 1.1.3.38 | H61T |
FAD-free apoenzyme H61T mainly exists as a dimeric species of 126000 Da. Binding of FAD to apoH61T rapidly restores enzyme activity and induces octamerization |
656076 |
