EC Number   |
Protein Variants |
Reference |
|---|
  1.19.1.1 | A266Y |
mutant does not allow formation of active charge-transfer complexes, probably due to restraints of C-terminus pliability. Mutant displays higher affinity for NADP+ than wild-type |
737746 |
| 1.19.1.1 | A266y/Del267-272 |
deletion/mutation emulates the structure present in plastidic versions of the protein. It does not modify the general geometry of FAD itself, but increases exposure of the flavin to the solvent, prevents a productive geometry of FAD:NADP(H) complex and decreases the protein thermal stability. Mutant displays higher affinity for NADP+ than wild-type |
737746 |
| 1.19.1.1 | Del267-272 |
deletion emulates the structure present in plastidic versions of the protein, mutant displays higher affinity for NADP+ than wild-type |
737746 |
| 1.19.1.1 | R144A |
mutation in the proposed NADPH-binding site, mutant exhibits decreased NADPH-dependent cytochrome c reductase activity and increased Km for NADPH |
-, 737634 |
| 1.19.1.1 | R174A |
mutation in the proposed NADPH-binding site, mutant exhibits decreased NADPH-dependent cytochrome c reductase activity and increased Km for NADPH |
-, 737634 |
| 1.19.1.1 | R184A |
mutation in the proposed NADPH-binding site, mutant exhibits decreased NADPH-dependent cytochrome c reductase activity and increased Km for NADPH |
-, 737634 |
| 1.19.1.1 | Y303F |
about 30% of the wild-type enzyme activity with ferredoxin, about 25% of the wild-type enzyme activity with flavodoxin |
-, 658076 |
| 1.19.1.1 | Y303S |
inactive. Mutation shifts the flavin reduction potential to less negative values, whereas semiquinone stabilization is severely hampered |
-, 658076 |
| 1.19.1.1 | Y303W |
almost inactive |
-, 658076 |
| 1.19.1.1 | Y308F |
about 20% of the wild-type enzyme activity with ferredoxin, about 11% of the wild-type enzyme activity with flavodoxin |
658076 |
