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Literature summary for 1.18.1.2 extracted from

  • Medina, M.; Gomez-Moreno, C.
    Interaction of ferredoxin-NADP+ reductase with its substrates: optimal interaction for efficient electron transfer (2004), Photosynth. Res., 79, 113-131.
    View publication on PubMed

Crystallization (Commentary)

Crystallization (Comment) Organism
-
Spinacia oleracea

Protein Variants

Protein Variants Comment Organism
E139K site-directed mutagenesis, altered interaction and kinetics of enzyme-ferredoxin association compared to the wild-type enzyme Anabaena sp.
E301A site-directed mutagenesis, altered interaction and kinetics of enzyme-ferredoxin association compared to the wild-type enzyme Anabaena sp.
K138E site-directed mutagenesis, altered interaction and kinetics of enzyme-ferredoxin association compared to the wild-type enzyme Anabaena sp.
K290E site-directed mutagenesis, altered interaction and kinetics of enzyme-ferredoxin association compared to the wild-type enzyme Anabaena sp.
K294E site-directed mutagenesis, altered interaction and kinetics of enzyme-ferredoxin association compared to the wild-type enzyme Anabaena sp.
K72E site-directed mutagenesis, altered interaction and kinetics of enzyme-ferredoxin association compared to the wild-type enzyme Anabaena sp.
K75E site-directed mutagenesis, altered interaction and kinetics of enzyme-ferredoxin association compared to the wild-type enzyme Anabaena sp.
L76D site-directed mutagenesis, altered interaction and kinetics of enzyme-ferredoxin association compared to the wild-type enzyme Anabaena sp.
L76F site-directed mutagenesis, altered interaction and kinetics of enzyme-ferredoxin association compared to the wild-type enzyme Anabaena sp.
L76S site-directed mutagenesis, altered interaction and kinetics of enzyme-ferredoxin association compared to the wild-type enzyme Anabaena sp.
L76V site-directed mutagenesis, altered interaction and kinetics of enzyme-ferredoxin association compared to the wild-type enzyme Anabaena sp.
L78D site-directed mutagenesis, altered interaction and kinetics of enzyme-ferredoxin association compared to the wild-type enzyme Anabaena sp.
L78F site-directed mutagenesis, altered interaction and kinetics of enzyme-ferredoxin association compared to the wild-type enzyme Anabaena sp.
L78S site-directed mutagenesis, altered interaction and kinetics of enzyme-ferredoxin association compared to the wild-type enzyme Anabaena sp.
L78V site-directed mutagenesis, altered interaction and kinetics of enzyme-ferredoxin association compared to the wild-type enzyme Anabaena sp.
R100A site-directed mutagenesis, altered interaction and kinetics of enzyme-ferredoxin association compared to the wild-type enzyme Anabaena sp.
R16E site-directed mutagenesis, altered interaction and kinetics of enzyme-ferredoxin association compared to the wild-type enzyme Anabaena sp.
R264E site-directed mutagenesis, altered interaction and kinetics of enzyme-ferredoxin association compared to the wild-type enzyme Anabaena sp.

Localization

Localization Comment Organism GeneOntology No. Textmining
chloroplast associated to the grana fraction Spinacia oleracea 9507
-
membrane weakly bound Spinacia oleracea 16020
-

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
reduced ferredoxin + NADP+ Anabaena sp. delivers NADPH or reduced ferredoxin for several metabolic reactions, involved in photosynthesis oxidized ferredoxin + NADPH
-
r
reduced ferredoxin + NADP+ Spinacia oleracea delivers NADPH or reduced ferredoxin for several metabolic reactions, involved in photosynthesis, enzyme-substrate interactions, overview oxidized ferredoxin + NADPH
-
r
reduced ferredoxin + NADP+ Escherichia coli reverse reaction is involved in activation of enzymes that participate in anaerobic metabolism oxidized ferredoxin + NADPH
-
r
reduced ferredoxin + NADP+ Azotobacter vinelandii reverse reaction is involved in activation of enzymes that participate in anaerobic metabolism, removal of free radicals gegnerated during the metabolsim oxidized ferredoxin + NADPH
-
r

Organism

Organism UniProt Comment Textmining
Anabaena sp.
-
-
-
Azotobacter vinelandii
-
-
-
Escherichia coli
-
-
-
Spinacia oleracea
-
-
-

Reaction

Reaction Comment Organism Reaction ID
2 reduced ferredoxin + NADP+ + H+ = 2 oxidized ferredoxin + NADPH reaction mechanism via semiquinone intermediate and radical formation Escherichia coli
2 reduced ferredoxin + NADP+ + H+ = 2 oxidized ferredoxin + NADPH reaction mechanism via semiquinone intermediate and radical formation Azotobacter vinelandii
2 reduced ferredoxin + NADP+ + H+ = 2 oxidized ferredoxin + NADPH reaction mechanism via semiquinone intermediate and radical formation, enzyme-substrate interactions, overview Spinacia oleracea
2 reduced ferredoxin + NADP+ + H+ = 2 oxidized ferredoxin + NADPH reaction mechanism via semiquinone intermediate and radical formation, enzyme-substrate interactions, overview Anabaena sp.

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
additional information the enzyme is asscoiated to phycobilin pigments Anabaena sp. ?
-
?
reduced ferredoxin + NADP+ delivers NADPH or reduced ferredoxin for several metabolic reactions, involved in photosynthesis Anabaena sp. oxidized ferredoxin + NADPH
-
r
reduced ferredoxin + NADP+ delivers NADPH or reduced ferredoxin for several metabolic reactions, involved in photosynthesis, enzyme-substrate interactions, overview Spinacia oleracea oxidized ferredoxin + NADPH
-
r
reduced ferredoxin + NADP+ reverse reaction is involved in activation of enzymes that participate in anaerobic metabolism Escherichia coli oxidized ferredoxin + NADPH
-
r
reduced ferredoxin + NADP+ reverse reaction is involved in activation of enzymes that participate in anaerobic metabolism, removal of free radicals gegnerated during the metabolsim Azotobacter vinelandii oxidized ferredoxin + NADPH
-
r
reduced ferredoxin + NADP+ plant-type ferredoxin contains a [2Fe2S] cluster, enzyme requires ferredoxin, substrate is a bulky protein, enzyme-substrate interactions involve residues R16, K72, K88, K116, E139, R264, K290, and K294, overview Spinacia oleracea oxidized ferredoxin + NADPH
-
r
reduced ferredoxin + NADP+ plant-type ferredoxin contains a [2Fe2S] cluster, substrate is an acidic, bulky protein, enzyme-substrate interactions involve residues R16, K72, K75, R100, E139, R264, K290, and K294 Anabaena sp. oxidized ferredoxin + NADPH
-
r
reduced ferredoxin + NADP+ substrate is a bulky protein Escherichia coli oxidized ferredoxin + NADPH
-
r
reduced ferredoxin + NADP+ substrate is a bulky protein Azotobacter vinelandii oxidized ferredoxin + NADPH
-
r

Subunits

Subunits Comment Organism
More three-dimensional structure analysis, intramolecular stabilization and stabilizationof enzyme-substrate complex, overview Anabaena sp.
More three-dimensional structure analysis, overview Escherichia coli
More three-dimensional structure analysis, overview Spinacia oleracea
More three-dimensional structure analysis, overview Azotobacter vinelandii

Synonyms

Synonyms Comment Organism
FNR
-
Escherichia coli
FNR
-
Spinacia oleracea
FNR
-
Azotobacter vinelandii
FNR
-
Anabaena sp.

Cofactor

Cofactor Comment Organism Structure
FAD involved in reaction splitting a two-electron-reaction into 2 one-electron-reactions Escherichia coli
FAD involved in reaction splitting a two-electron-reaction into 2 one-electron-reactions Spinacia oleracea
FAD involved in reaction splitting a two-electron-reaction into 2 one-electron-reactions Azotobacter vinelandii
FAD involved in reaction splitting a two-electron-reaction into 2 one-electron-reactions Anabaena sp.
NADP+
-
Escherichia coli
NADP+
-
Azotobacter vinelandii
NADP+ interaction with the enzyme, complex structure, specificity-determining structures, overview Spinacia oleracea
NADP+ interaction with the enzyme, complex structure, specificity-determining structures, overview Anabaena sp.