EC Number   |
Protein Variants |
Reference |
|---|
    1.14.13.2 | A16T/S394P/D416A |
low ability to hydroxylate 3-aminophenol |
684919 |
| 1.14.13.2 | A400G |
transforms 3-aminophenol with efficiency almost like mutant A400G/K429R |
-, 684919 |
| 1.14.13.2 | A400G/K429R |
among mutants, highest enzymatic activity to hydroxylate 3-aminophenol |
684919 |
| 1.14.13.2 | D38A |
kcat/KM for 4-hydroxybenzoate is 16.8fold higher than wild-type value |
684641 |
| 1.14.13.2 | D38Y |
kcat/KM for 4-hydroxybenzoate is 11.8fold higher than wild-type value |
684641 |
| 1.14.13.2 | D38Y/T42R |
kcat/KM for 4-hydroxybenzoate is 32fold higher than wild-type value |
684641 |
| 1.14.13.2 | E49Q |
investigation of oxygen half-reaction |
658045 |
| 1.14.13.2 | E49Q |
mutant has lost the ability in the oxidized state to rapidly exchange the product, i.e., 3,4-dihydroxybenzoate, for the substrate, p-hydroxybenzoate |
658048 |
| 1.14.13.2 | E49Q |
mutation enhances the positive charge in the active site of PHBH, rate of hydroxylation is above that of wild-type, the rate of release of product is slower than the rate of return of the flavin to the oxidized state |
658045 |
| 1.14.13.2 | H135P |
alters the enzyme's substrate specificity |
-, 684919 |
