EC Number   |
Protein Variants |
Reference |
|---|
   1.14.13.44 | G255F |
the variant exhibits 7% compared to the specific activity of the wild-type enzyme on NADH and 2,3-dihydroxybiphenyl, suggesting inhibition of substrate entrance into the active site by the large aromatic residue |
744407 |
| 1.14.13.44 | I244V |
mutant enzyme has a 30% higher specific activity with 2-sec-butylphenol, guaiacol, and 2-hydroxybiphenyl. The Km-value for guaiacol decreases with this mutant, but the Km-value for 2-hydroxybiphenyl increase |
-, 438847 |
| 1.14.13.44 | M223A |
site-directed saturation mutagenesis, the mutant shows reduced activity compared to wild-type enzyme |
764475 |
| 1.14.13.44 | M223E |
site-directed saturation mutagenesis, the mutant shows reduced activity compared to wild-type enzyme |
764475 |
| 1.14.13.44 | M223I |
site-directed saturation mutagenesis, the mutant shows reduced activity compared to wild-type enzyme |
764475 |
| 1.14.13.44 | M223K |
site-directed saturation mutagenesis, the mutant shows reduced activity compared to wild-type enzyme |
764475 |
| 1.14.13.44 | M223Q |
site-directed saturation mutagenesis, the mutant shows reduced activity compared to wild-type enzyme |
764475 |
| 1.14.13.44 | M321A |
site-directed saturation mutagenesis, the mutant variant demonstrates altered regioselectivity by oxidizing 3-hydroxybiphenyl, and thus enabling the production of a distinct antioxidant, 3,4-dihydroxybiphenyl, with similar ferric reducing capacity to the well-studied piceatannol. Mutant enzyme crystal structure analysis and comparison to the wild-type enzyme structure |
764475 |
| 1.14.13.44 | M321F |
site-directed saturation mutagenesis, wild-type HbpA possess pro-S enantioselectivity towards the production of several chiral sulfoxides, whereas the mutant M321F exhibits improved enantioselectivity and increased activity compared to wild-type |
764475 |
| 1.14.13.44 | M321L |
site-directed saturation mutagenesis, the mutant shows reduced activity compared to wild-type enzyme |
764475 |
