EC Number   |
Protein Variants |
Reference |
|---|
   1.8.4.10 | C139S |
no activity |
667787 |
| 1.8.4.10 | C140S |
mutant enzyme shows 3% of wild-type activity |
667787 |
| 1.8.4.10 | C228S |
no activity |
667787 |
| 1.8.4.10 | C231S |
no activity |
667787 |
| 1.8.4.10 | C256S |
no activity |
667787 |
| 1.8.4.10 | D122G |
mutant does not display improved activity with 3'-phosphoadenosine-5'-phosphosulfate and shows significantly reduced activity with 5'-adenylylsulfate as the substrate |
742508 |
| 1.8.4.10 | more |
a heterologous system is constructed in which the C domain of EiAPR (EC 1.8.4.9) is fused to the carboxyl terminus of the APS reductase from Pseudomonas aeruginosa (EC 1.8.4.10), an enzyme that normally uses thioredoxin as an electron donor and is incapable of using glutathione for this function. The hybrid enzyme, which retains the [4Fe-4S] cluster from PaAPR, can use both thioredoxin and glutathione as an electron donor for APS reduction. The ability to use glutathione is enhanced by the addition of Na2SO4 to the reaction buffer, a property that the hybrid enzyme shares with EiAPR |
667746 |
| 1.8.4.10 | more |
construction of APR-B knockout plants, the mutant plants are able to grow on sulfate as a sole sulfur source, and the content of low molecular weight thiols is not different from wild-type plants. However, when treated with low concentrations of cadmium, the APR-B knockout plants are more sensitive than wild-type plants, phenotype, overview |
694695 |
