EC Number   |
Protein Variants |
Reference |
|---|
    5.3.2.6 | betaP1A |
site-directed mutagenesis, the mutant shows highly reduced catalytic efficiency compared to the wild-type hh4-OT |
-, 718874 |
| 5.3.2.6 | betaR11A |
site-directed mutagenesis, the mutant shows increased catalytic efficiency compared to the wild-type hh4-OT |
-, 718874 |
| 5.3.2.6 | alphaR40A |
site-directed mutagenesis, the mutant shows reduced catalytic efficiency compared to the wild-type hh4-OT |
-, 718874 |
| 5.3.2.6 | betaR39A |
site-directed mutagenesis, the mutant shows reduced catalytic efficiency compared to the wild-type hh4-OT |
-, 718874 |
| 5.3.2.6 | R39A |
site-directed mutagenesis, with 2-hydroxymuconate the R39A mutant shows decreased kcat by 125fold and increased Km by 1.5fold |
-, 718830 |
| 5.3.2.6 | R39Q |
site-directed mutagenesis, with 2-hydroxymuconate the R39Q mutant shows decreased kcat by 389fold and increased Km by 2.6fold, only the tight binding sites function catalytically in the R39Q mutant, structural changes in the R39Q mutant were mainly in the beta-hairpin from residues 50 to 57 which covers the active site |
-, 718830 |
| 5.3.2.6 | M45Y/F50A |
the mutant enzyme displays low Michael-type addition activity compared to the wild type enzyme |
748742 |
| 5.3.2.6 | H6M |
the mutant has about 3fold increased specific activity compared with that of wild type enzyme |
748742 |
| 5.3.2.6 | A33D |
the mutant shows highest enantioselectivity for the Michael-type addition of acetaldehyde to trans-beta nitrostyrene producing 4-nitro-3-phenylbutanal, compared to the wild type enzyme |
748742 |
| 5.3.2.6 | R39E |
the mutant shows highest enantioselectivity for the Michael-type addition of butanal to trans-beta nitrostyrene, producing 2-ethyl-4-nitro-3-phenylbutanal, compared to the wild type enzyme |
748742 |
