EC Number   |
Protein Variants |
Reference |
|---|
    4.1.1.48 | D184A |
no alteration of native structure, very little difference in Km, turnover rate compared to wild type, but less thermal stability |
652796 |
| 4.1.1.48 | D61C |
kcat/Km for 1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate is about 1.5fold lower than the wild-type value |
-, 721686 |
| 4.1.1.48 | E168A |
site directed mutagenesis |
-, 692324 |
| 4.1.1.48 | E210Q |
kcat/Km for 1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate is 6fold lower than wild-type value |
-, 725533 |
| 4.1.1.48 | E51Q |
kcat/Km for 1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate is 28fold lower than wild-type value |
-, 725533 |
| 4.1.1.48 | F246S |
about 2fold increase in turnover-number, 8fold increase in KM-value, decrease in kcat/Km |
724261 |
| 4.1.1.48 | F246S |
mutation at C-terminus, increases flexibility |
747143 |
| 4.1.1.48 | F89A |
approximately 24fold increase in the KM-value, eleven-fold decrease in the maximum turnover rate |
726453 |
| 4.1.1.48 | G212E |
about 2fold increase in turnover-number, 100fold increase Km-value, decrease in kcat/Km. Mutant enzyme is about as thermostable as wild-type enzyme |
724261 |
| 4.1.1.48 | G212E |
mutation interferes with phosphate binding |
747143 |
