EC Number   |
Protein Variants |
Reference |
|---|
   1.18.1.2 | 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 |
| 1.18.1.2 | A266Y |
site-directed mutagenesis, deletion of the six C-terminal amino acids FVGEGI beyond Ala266 is combined with the replacement A266Y to emulate the structure of plastidic reductases. THe mutations produce subtle global conformational changes, but strongly reduce the local rigidity of the FAD-binding pocket, exposing the isoalloxazine ring to the solvent. Thus, the ultrafast charge-transfer quenching of FAD* by the conserved Tyr66 residue is absent in the mutant series, producing enhancement of the excited singlet and triplet-state properties of FAD. All RcFPR variants display higher affinity for NADP+ than the wild-type |
742301 |
| 1.18.1.2 | 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 |
| 1.18.1.2 | Del267-272 |
deletion emulates the structure present in plastidic versions of the protein, mutant displays higher affinity for NADP+ than wild-type |
737746 |
| 1.18.1.2 | DELTA1-15 |
removal of the N-terminal 15 residues of enzyme enhances the interaction with ferredoxin |
672139 |
| 1.18.1.2 | DELTA81-118 |
deleted amino acid comprise a species-specific subdomain containing an insertion of 28 residues, deletion results in an catalytically active enzyme form with 10fold decreased affinity for ferredoxin |
672139 |
| 1.18.1.2 | E139? |
different conformation |
285551 |
| 1.18.1.2 | E139D |
site-directed mutagenesis, altered conformation compared to the wild-type enzyme, slightly reduced activity compared to the wild-type enzyme |
658611 |
| 1.18.1.2 | E139K |
site-directed mutagenesis, altered interaction and kinetics of enzyme-ferredoxin association compared to the wild-type enzyme |
660065 |
| 1.18.1.2 | E139K |
site-directed mutagenesis, mutant enzyme shows increased interaction with ferredoxin and reduces the appropriate orientation of flavodoxin, altered conformation compared to the wild-type enzyme, increased activity compared to the wild-type enzyme |
658611 |
