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Literature summary for 1.18.1.2 extracted from

  • Komori, H.; Seo, D.; Sakurai, T.; Higuchi, Y.
    Crystal structure analysis of Bacillus subtilis ferredoxin-NADP+ oxidoreductase and the structural basis for its substrate selectivity (2010), Protein Sci., 19, 2279-2290.
    View publication on PubMedView publication on EuropePMC
Search for more literature for 1.18.1.2

Crystallization (Commentary)

Crystallization (Comment) Organism
FNR in complex with NADP+, two different crystal forms, mixing of 0.001 ml of 10 mg/ml protein and 2.5 mM NADP+ with 0.001 ml of reservoir solution containing 0.1 M HEPES buffer, pH 7.5, 30% 1,2-propanediol, and 20% PEG 400 for form I, and 20% PEG 3350, 0.2 M sodium fluoride, and 5% trehalose for form II, 20°C, X-ray diffraction structure determination and analysis at 1.8-1.9 A resolution, respetively, molecular replacement Bacillus subtilis

Protein Variants

Protein Variants Comment Organism
H324F site-directed mutagenesis, the mutant shows altered kinetics and reduced activity compared to the wild-type FNR Bacillus subtilis
H324S site-directed mutagenesis, the mutant shows altered kinetics and reduced activity compared to the wild-type FNR Bacillus subtilis
additional information site-directed mutagenesis of NADPH-specific BsFNR to replace Arg186, Asp187, Arg190, and His324 with the residues occurring in NADH/NADPH-bispecific Chlorobium tepidum FNR Bacillus subtilis
R186G site-directed mutagenesis, replacement of Arg186 with glycine leads to drastically reduced amounts of recombinant protein Bacillus subtilis
R186G/D187H site-directed mutagenesis, the mutant shows altered kinetics and reduced activity compared to the wild-type FNR Bacillus subtilis
R186G/D187H/R190Q site-directed mutagenesis, the mutant shows altered kinetics and reduced activity compared to the wild-type FNR Bacillus subtilis
R190Q site-directed mutagenesis, the mutant shows altered kinetics and reduced activity compared to the wild-type FNR Bacillus subtilis

Natural Substrates/ Products (Substrates)

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

Organism

Organism UniProt Comment Textmining
Bacillus subtilis O05268 gene yumC
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2 reduced ferredoxin + NADP+
-
 Bacillus subtilis 2 oxidized ferredoxin + NADPH + H+
-
 r
2 reduced ferredoxin + NADP+ with K3[Fe(CN)6] as electron acceptor in the enzyme assay. Ferredoxin is a low-redox-potential iron-sulfur protein. BsFNR features two distinct binding domains for FAD and NADPH, the deduced mode of NADP+ binding to the BsFNR molecule is nonproductive in that the nicotinamide and isoalloxazine rings are over 15A A apart, binding structures, overview Bacillus subtilis 2 oxidized ferredoxin + NADPH + H+
-
 r

Subunits

Subunits Comment Organism
More structure, primary sequence and oligomeric conformation, comparisons, overview Bacillus subtilis

Synonyms

Synonyms Comment Organism
ferredoxin-NADP+ oxidoreductase
-
 Bacillus subtilis
FNR
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 Bacillus subtilis

Temperature Optimum [°C]

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

pH Optimum

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

Cofactor

Cofactor Comment Organism Structure
FAD BsFNR features two distinct binding domains for FAD and NADPH, binding structure, overview. A unique C-terminal extension covers the re-face of the isoalloxazine moiety of FAD. Tyr50 in the FAD-binding region and His324 in the Cterminal extension stack on the si- and re-faces of the isoalloxazine ring of FAD, respectively Bacillus subtilis