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Literature summary extracted from

  • Seo, D.; Naito, H.; Nishimura, E.; Sakurai, T.
    Replacement of Tyr50 stacked on the si-face of the isoalloxazine ring of the flavin adenine dinucleotide prosthetic group modulates Bacillus subtilis ferredoxin-NADP+ oxidoreductase activity toward NADPH (2015), Photosynth. Res., 125, 321-328 .
    View publication on PubMed

Protein Variants

EC Number Protein Variants Comment Organism
1.18.1.2 additional information replacement of Tyr50 stacked on the si-face of the isoalloxazine ring of the flavin adenine dinucleotide prosthetic group modulates Bacillus subtilis ferredoxin-NADP+ oxidoreductase activity toward NADPH. The Y50G and Y50S mutations enhance the FAD fluorescence emission, whereas those of the wild type and Y50W mutant are quenched Bacillus subtilis
1.18.1.2 Y50G site-directed mutagenesis, the mutant shows a blue shift of the FAD transition band and decreased thermal stability compared to wild-type. Using the diaphorase assay, the kcat values for the Y50G mutant in the presence of NADPH and ferricyanide is decreased to less than 5% of the wild-type activity Bacillus subtilis
1.18.1.2 Y50G the mutation decreases thermal stability compared to the wild type enzyme Bacillus subtilis
1.18.1.2 Y50S site-directed mutagenesis, the mutant shows a blue shift of the FAD transition band and decreased thermal stability compared to wild-type. Using the diaphorase assay, the kcat values for the Y50G mutant in the presence of NADPH and ferricyanide is decreased to less than 5% of the wild-type activity Bacillus subtilis
1.18.1.2 Y50S the mutation decreases thermal stability compared to the wild type enzyme Bacillus subtilis
1.18.1.2 Y50W site-directed mutagenesis, the mutant shows a blue shift of the FAD transition band and decreased thermal stability compared to wild-type. The mutant retains approximately 20 % reactivity in the diaphorase assay and BsFd-dependent cytochrome c reduction assay relative to wild-type Bacillus subtilis
1.18.1.2 Y50W the mutation decreases thermal stability compared to the wild type enzyme, The mutant retains approximately 20% of wild type reactivity Bacillus subtilis

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
1.18.1.2 additional information
-
 additional information Michaelis-Menten kinetics Bacillus subtilis
1.18.1.2 0.0019
-
 NADPH pH 7.0, 25°C, recombinant mutant Y50S Bacillus subtilis
1.18.1.2 0.004
-
 NADPH pH 7.0, 25°C, recombinant mutant Y50W Bacillus subtilis
1.18.1.2 0.0043
-
 NADPH pH 7.0, 25°C, recombinant mutant Y50G Bacillus subtilis
1.18.1.2 0.0197
-
 NADPH pH 7.0, 25°C, recombinant wild-type enzyme Bacillus subtilis

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
1.18.1.2 40000
-
 recombinant mutant enzymes, gel filtration Bacillus subtilis

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
1.18.1.2 2 oxidized ferredoxin + NADPH Bacillus subtilis
-
 2 reduced ferredoxin + NADP+ + H+
-
 r
1.18.1.2 2 oxidized ferredoxin + NADPH Bacillus subtilis 168
-
 2 reduced ferredoxin + NADP+ + H+
-
 r
1.18.1.2 reduced ferredoxin + NADP+ + H+ Bacillus subtilis
-
 oxidized ferredoxin + NADPH
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
1.18.1.2 Bacillus subtilis
-
-
-
1.18.1.2 Bacillus subtilis O05268
-
-
1.18.1.2 Bacillus subtilis 168 O05268
-
-

Reaction

EC Number Reaction Comment Organism Reaction ID
1.18.1.2 2 reduced ferredoxin + NADP+ + H+ = 2 oxidized ferredoxin + NADPH a hydride transfer reaction with NAD(P)H and two separate one-electron transfer reactions with ferredoxin are generally involved in te reaction process Bacillus subtilis
a

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.18.1.2 2 oxidized ferredoxin + NADPH
-
 Bacillus subtilis 2 reduced ferredoxin + NADP+ + H+
-
 r
1.18.1.2 2 oxidized ferredoxin + NADPH
-
 Bacillus subtilis 168 2 reduced ferredoxin + NADP+ + H+
-
 r
1.18.1.2 reduced cytochrome c + NADP+
-
 Bacillus subtilis oxidized cytochrome c + NADPH + H+
-
 ?
1.18.1.2 reduced ferredoxin + NADP+ + H+
-
 Bacillus subtilis oxidized ferredoxin + NADPH
-
 ?

Subunits

EC Number Subunits Comment Organism
1.18.1.2 homodimer 2 * 40000, SDS-PAGE Bacillus subtilis
1.18.1.2 monomer 1 * 40000, recombinant mutant enzymes, SDS-PAGE Bacillus subtilis

Synonyms

EC Number Synonyms Comment Organism
1.18.1.2 BsFNR
-
 Bacillus subtilis
1.18.1.2 ferredoxin-NADP+ oxidoreductase
-
 Bacillus subtilis
1.18.1.2 FNR
-
 Bacillus subtilis

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
1.18.1.2 25
-
 assay at Bacillus subtilis

Turnover Number [1/s]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
1.18.1.2 16.2
-
 NADPH pH 7.0, 25°C, recombinant mutant Y50S Bacillus subtilis
1.18.1.2 42.8
-
 NADPH pH 7.0, 25°C, recombinant mutant Y50G Bacillus subtilis
1.18.1.2 183
-
 NADPH pH 7.0, 25°C, recombinant mutant Y50W Bacillus subtilis
1.18.1.2 1012
-
 NADPH pH 7.0, 25°C, recombinant wild-type enzyme Bacillus subtilis

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
1.18.1.2 7
-
 assay at Bacillus subtilis

Cofactor

EC Number Cofactor Comment Organism Structure
1.18.1.2 FAD
-
 Bacillus subtilis
1.18.1.2 FAD flavin adenine dinucleotide prosthetic group, the FAD prosthetic group is noncovalently bound in the open conformation. The fluorescence intensity of the protein-bound FAD is influenced by its environment. The fluorescence emissions of enzyme mutants Y50G and Y50S enzymes increase six to sevenfold compared with that of free FAD, whereas the fluorescence emission of wild-type and Y50W enzymes is efficiently quenched to below 3% and 9% of that of free FAD. ENzyme residue Tyr50 plays an important role to stabilize the FAD prosthetic group Bacillus subtilis
1.18.1.2 Ferredoxin
-
 Bacillus subtilis
1.18.1.2 NADP+
-
 Bacillus subtilis
1.18.1.2 NADPH
-
 Bacillus subtilis

General Information

EC Number General Information Comment Organism
1.18.1.2 evolution the enzyme is a member of the flavoprotein superfamily Bacillus subtilis

kcat/KM [mM/s]

EC Number kcat/KM Value [1/mMs-1] kcat/KM Value Maximum [1/mMs-1] Substrate Comment Organism Structure
1.18.1.2 8526
-
 NADPH pH 7.0, 25°C, recombinant mutant Y50S Bacillus subtilis
1.18.1.2 9953
-
 NADPH pH 7.0, 25°C, recombinant mutant Y50G Bacillus subtilis
1.18.1.2 45750
-
 NADPH pH 7.0, 25°C, recombinant mutant Y50W Bacillus subtilis
1.18.1.2 51370
-
 NADPH pH 7.0, 25°C, recombinant wild-type enzyme Bacillus subtilis