EC Number |
Protein Variants |
Reference |
---|
2.8.2.1 | A146D |
sulfation activity of the mutant is strongly decreased for the substrates 4-nitrophenol and dopamine, enzyme form SULT1D1 |
660962 |
2.8.2.1 | A146E |
P-PST mutant by site-directed mutagenesis, highly reduced activity with dopamine, highly increased activity wih 4-nitrophenol |
645674 |
2.8.2.1 | A146Q |
sulfation activity of the mutant is strongly decreased for the substrates 4-nitrophenol and dopamine, enzyme form SULT1D1 |
660962 |
2.8.2.1 | A86D/I89E |
P-PST mutant by site-directed mutagenesis, highly reduced activity with dopamine, highly increased activity wih 4-nitrophenol |
645674 |
2.8.2.1 | A86D/I89E/A146E |
P-PST mutant by site-directed mutagenesis, no activity |
645674 |
2.8.2.1 | C70S |
mutation has no effect on enzymic activity, but the mutant is more thermosensitive than the wild-type |
645660 |
2.8.2.1 | D247L |
21fold better sulfation of 4-nitrophenol (120fold decrease in KM-value) and 54fold less efficient in sulfation of dopamine (8fold increase in KM-value) compared to wild-type enzyme. Preference is switched from dopamine to 4-nitrophenol, enzyme form SULT1D1 |
660962 |
2.8.2.1 | D249G |
the mutant shows higher specific activity towards 3-cyano-7-hydroxycumarin (0.1 mM and above) compared to the wild type enzyme. The mutant is less heat stable than the wild type enzyme |
726285 |
2.8.2.1 | D86A |
M-PST mutant by site-directed mutagenesis, reduced activity |
645674, 645684 |
2.8.2.1 | D86A |
no stimulating effect by Mn2+, probably due to abolished substrate/Mn2+-complex binding via Asp86 |
645684 |