Any feedback?
Please rate this page
(all_enzymes.php)
(0/150)

BRENDA support

1.19.1.1: flavodoxin-NADP+ reductase

This is an abbreviated version!
For detailed information about flavodoxin-NADP+ reductase, go to the full flat file.

Reaction

reduced flavodoxin
+
NADP+
=
oxidized flavodoxin
 +
NADPH
 +
H+

Synonyms

Bc_0385, ferredoxin (flavodoxin):NADP+ oxidoreductase, ferredoxin/flavodoxin-NADP(H) oxidoreductase, FLDR, FNR, FPR, PETH, YumC

ECTree

     1 Oxidoreductases
         1.19 Acting on reduced flavodoxin as donor
             1.19.1 With NAD+ or NADP+ as acceptor
                1.19.1.1 flavodoxin-NADP+ reductase

Engineering

Engineering on EC 1.19.1.1 - flavodoxin-NADP+ reductase

Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Y50G
mutation results in a blue shift of the FAD transition bands, with enhancement of fluorescence emission. Mutant displays decreased thermal stability
Y50S
mutation results in a blue shift of the FAD transition bands, with enhancement of fluorescence emission. Mutant displays decreased thermal stability
Y50W
mutation results in a blue shift of the FAD transition bands, with quenching of fluorescence emission. Mutant displays decreased thermal stability
Y50G
-
mutation results in a blue shift of the FAD transition bands, with enhancement of fluorescence emission. Mutant displays decreased thermal stability
-
Y50S
-
mutation results in a blue shift of the FAD transition bands, with enhancement of fluorescence emission. Mutant displays decreased thermal stability
-
R144A
-
mutation in the proposed NADPH-binding site, mutant exhibits decreased NADPH-dependent cytochrome c reductase activity and increased Km for NADPH
R174A
-
mutation in the proposed NADPH-binding site, mutant exhibits decreased NADPH-dependent cytochrome c reductase activity and increased Km for NADPH
R184A
-
mutation in the proposed NADPH-binding site, mutant exhibits decreased NADPH-dependent cytochrome c reductase activity and increased Km for NADPH
Y308S
mutant uses NAD(H) instead of NADP(H), expression of the mutant has no effect on soxRS induction and fails to protect FPR deficient cells from methyl viologen toxicity
R144A
-
mutation in the proposed NADPH-binding site, mutant exhibits decreased NADPH-dependent cytochrome c reductase activity and increased Km for NADPH
-
R174A
-
mutation in the proposed NADPH-binding site, mutant exhibits decreased NADPH-dependent cytochrome c reductase activity and increased Km for NADPH
-
R184A
-
mutation in the proposed NADPH-binding site, mutant exhibits decreased NADPH-dependent cytochrome c reductase activity and increased Km for NADPH
-
Y303F
about 30% of the wild-type enzyme activity with ferredoxin, about 25% of the wild-type enzyme activity with flavodoxin
Y303S
inactive. Mutation shifts the flavin reduction potential to less negative values, whereas semiquinone stabilization is severely hampered
Y303W
almost inactive
Y303F
-
about 30% of the wild-type enzyme activity with ferredoxin, about 25% of the wild-type enzyme activity with flavodoxin
-
Y303S
-
inactive. Mutation shifts the flavin reduction potential to less negative values, whereas semiquinone stabilization is severely hampered
-
Y303W
-
almost inactive
-
Y308F
about 20% of the wild-type enzyme activity with ferredoxin, about 11% of the wild-type enzyme activity with flavodoxin
Y308S
nearly inactive mutant with ferredoxin, about 25% of the wild-type enzyme activity with flavodoxin. Mutation shifts the flavin reduction potential to less negative values, whereas semiquinone stabilization is severely hampered
Y308W
about 5% of the wild-type enzyme activity with ferredoxin, no activity with flavodoxin
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
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
Del267-272
deletion emulates the structure present in plastidic versions of the protein, mutant displays higher affinity for NADP+ than wild-type