EC Number |
Protein Variants |
Reference |
---|
1.13.11.8 | A18W |
site-directed mutagenesis, mutation in the betaa-subunit, residue Ala18b is located opening of the putative allosteric pocket, the mutant displays reduced activity and altered rate enhancement by vanillin compared to the wild-type enzyme |
741768 |
1.13.11.8 | F103H |
site-directed mutagenesis, mutation in the alpha-subunit, residue Phe103a is located in the putative allosteric pocket, the mutant displays reduced activity and altered rate enhancement by vanillin compared to the wild-type enzyme |
741768 |
1.13.11.8 | F103L |
site-directed mutagenesis, mutation in the alpha-subunit, residue Phe103a is located in the putative allosteric pocket, the mutant displays reduced activity and altered rate enhancement by vanillin compared to the wild-type enzyme |
741768 |
1.13.11.8 | F103T |
site-directed mutagenesis, mutation in the alpha-subunit, residue Phe103a is located in the putative allosteric pocket, the mutant displays reduced activity and altered rate enhancement by vanillin compared to the wild-type enzyme |
741768 |
1.13.11.8 | F103T |
site-directed mutagenesis, mutation in the alpha-subunit, the mutant shows enhanced utilization of substrates gallate and 3-O-methylgallate, but not of protocatechuate, compared to the wild-type enzyme |
743708 |
1.13.11.8 | F103V |
site-directed mutagenesis, mutation in the alpha-subunit, residue Phe103a is located in the putative allosteric pocket, the mutant displays reduced activity and altered rate enhancement by vanillin compared to the wild-type enzyme |
741768 |
1.13.11.8 | F103V |
site-directed mutagenesis, mutation in the alpha-subunit, the mutant shows enhanced utilization of substrates gallate and 3-O-methylgallate, but not of protocatechuate, compared to the wild-type enzyme |
743708 |
1.13.11.8 | more |
in silico docking of substrates to the enzyme mutants, and impact of Phe103alpha mutations on allosteric activation of alternate substrate dioxygenation, overview |
743708 |