EC Number |
Protein Variants |
Reference |
---|
1.14.13.24 | A308G |
site-directed mutagenesis, the mutant shows reduced activity compared to wild-type enzyme, comparison of FAD contents |
764754 |
1.14.13.24 | H213A |
inactive, but the strength of substrate binding is not affected by the mutation |
727958 |
1.14.13.24 | H213A |
the mutant enzyme cannot catalyze hydroxylation |
742501 |
1.14.13.24 | H213D |
the mutant enzyme can bind to 3-hydroxybenzoate with similar affinity as the wild-type enzyme and form C4a-hydroperoxy intermediate. It produces 2,5-dihydroxybenzoate with yields of 52% |
742501 |
1.14.13.24 | H213E |
the mutant enzyme can bind to 3-hydroxybenzoate with similar affinity as the wild-type enzyme and form C4a-hydroperoxy intermediate. It produces 2,5-dihydroxybenzoate with yields of 92%. The hydroxylation rate constant of the mutant enzyme (35/s) is similar to that of wild-type enzyme (36/s) and this variant has an efficiency of hydroxylation (92%) similar to the wild-type enzyme (86%) |
742501 |
1.14.13.24 | H213S |
inactive |
727958 |
1.14.13.24 | H213S |
the mutant enzyme can bind to 3-hydroxybenzoate with similar affinity as the wild-type enzyme and form C4a-hydroperoxy intermediate. It produces 2,5-dihydroxybenzoate with yields of 28% |
742501 |
1.14.13.24 | more |
construction of a nagX knockout mutant of strain CJ2 defective in nagX, the mutant fails to grow on 3-hydroxybenzoate but grows normally on naphthalene |
684560 |
1.14.13.24 | more |
construction of a P25X xlnD knockout mutant strain G50, no induction after growth on lactate and 3-hydroxy-4-methylbenzoate in contrast to the wild-type enzyme, slightly reduced activity with 3-hydroxybenzoate and gentisate |
-, 674255 |
1.14.13.24 | Q301E |
inactive |
727958 |