EC Number   |
Protein Variants |
Reference |
|---|
    1.4.1.16 | T171S/R181F/H227V |
site-directed saturation mutagenesis, the mutant shows 14.6fold increased activity with phenylpyruvate compared to the wild-type enzyme |
724034 |
| 1.4.1.16 | T70S |
catalytic ability of T70S does not change much |
763313 |
| 1.4.1.16 | V14L |
mutation results in decrease of kcat/KM with meso-DAP and pyruvic acid |
763313 |
| 1.4.1.16 | V156D |
mutation results in decrease of kcat/KM with meso-DAP and pyruvic acid, almost complete loss of catalytic ability |
763313 |
| 1.4.1.16 | V68M |
mutation decreases the kcat/KM value with meso-DAP, the catalytic efficiency toward pyruvic acid does not change |
763313 |
| 1.4.1.16 | W121L |
mutant accepts substrates D-2-phenylglycine and D-homophenylalanine |
762879 |
| 1.4.1.16 | W121L/H227I |
mutant sow improved enzyme activities towards various 2-oxoacids including sterically bulky substrates. The substrate binding cavity of the mutant enzyme is reshaped to accommodate these bulky substrates, thus leading to higher enzyme activity |
762879 |
