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Literature summary extracted from

  • Carrillo, N.; Ceccarelli, E.A.
    Open questions in ferredoxin-NADP+ reductase catalytic mechanism (2003), Eur. J. Biochem., 270, 1900-1915.
    View publication on PubMed

Activating Compound

EC Number Activating Compound Comment Organism Structure
1.18.1.2 flavodoxin stimulates about 2fold the reduction of NADP+ Escherichia coli
1.18.1.2 additional information acceptors enhance the oxidation reaction several fold, e.g. ferredoxin, flavodoxin, viologens, nitro derivatives, and quinones, that can readily engage in oxygen-dependent redox cycling leading to formation of superoxide Spinacia oleracea
1.18.1.2 additional information acceptors enhance the oxidation reaction several fold, e.g. ferredoxin, flavodoxin, viologens, nitro derivatives, and quinones, that can readily engage in oxygen-dependent redox cycling leading to formation of superoxide Zea mays
1.18.1.2 additional information acceptors enhance the oxidation reaction several fold, e.g. ferredoxin, flavodoxin, viologens, nitro derivatives, and quinones, that can readily engage in oxygen-dependent redox cycling leading to formation of superoxide Capsicum annuum
1.18.1.2 additional information acceptors enhance the oxidation reaction several fold, e.g. ferredoxin, flavodoxin, viologens, nitroderivatives, and quinones, that can readily engage in oxygen-dependent redox cycling leading to formation of superoxide Pisum sativum
1.18.1.2 additional information acceptors enhance the oxidation reaction several fold, e.g. ferredoxin, flavodoxin, viologens, nitroderivatives, and quinones, that can readily engage in oxygen-dependent redox cycling leading to formation of superoxide Cyanobacteria
1.18.1.2 additional information acceptors enhance the oxidation reaction severalfold, e.g. ferredoxin, flavodoxin, viologens, nitroderivatives, and quinones, that can readily engage in oxygen-dependent redox cycling leading to formation of superoxide Zea mays
1.18.1.2 NADP+ stimulates binding of reduced ferredoxin and reduction of flavin Spinacia oleracea

Protein Variants

EC Number Protein Variants Comment Organism
1.18.1.2 additional information a tyrosine mutant accepts NAD(H) as cofactor and is insensitive to inhibition by NADH Spinacia oleracea
1.18.1.2 Y308S altered cofactor specificity compared to the wild-type enzyme, mutant enzymes is able to utilizes NADP(H) as well as NAD(H) Pisum sativum

Inhibitors

EC Number Inhibitors Comment Organism Structure
1.18.1.2 Dithionite
-
 Escherichia coli
1.18.1.2 NADH
-
 Spinacia oleracea
1.18.1.2 NADPH reversible inhibition, is turned to irreversible in presence of 4 M urea Spinacia oleracea
1.18.1.2 oxidized ferredoxin inhibits binding of reduced ferredoxin and reduction of flavin Spinacia oleracea

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
1.18.1.2 additional information
-
 additional information kinetics Escherichia coli
1.18.1.2 additional information
-
 additional information kinetics Spinacia oleracea
1.18.1.2 additional information
-
 additional information kinetics Anabaena sp.

Localization

EC Number Localization Comment Organism GeneOntology No. Textmining
1.18.1.2 chloroplast
-
 Spinacia oleracea 9507
-
1.18.1.2 chloroplast
-
 Pisum sativum 9507
-
1.18.1.2 chloroplast
-
 Zea mays 9507
-
1.18.1.2 chloroplast
-
 Capsicum annuum 9507
-
1.18.1.2 chloroplast
-
 Cyanobacteria 9507
-
1.18.1.2 plastid
-
 Zea mays 9536
-
1.18.1.2 thylakoid
-
 Pisum sativum 9579
-

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
1.18.1.2 Iron enzyme contains an [2Fe2S] cluster as prosthetic group involved in the reaction Zea mays

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
1.18.1.2 reduced ferredoxin + NADP+ Rhodobacter capsulatus
-
 oxidized ferredoxin + NADPH
-
 r
1.18.1.2 reduced ferredoxin + NADP+ Azotobacter vinelandii
-
 oxidized ferredoxin + NADPH
-
 r
1.18.1.2 reduced ferredoxin + NADP+ Anabaena sp.
-
 oxidized ferredoxin + NADPH
-
 r
1.18.1.2 reduced ferredoxin + NADP+ Spinacia oleracea enzyme catalyzes the final step of photosynthetic electron transfer from the iron-sulfur protein ferredoxin reduced by photosystem I to NADP+ providing NADPH necessary for CO2 assimilation in plants, in root and heterotrophic tissue, the reaction is driven towards ferredoxin reduction oxidized ferredoxin + NADPH
-
 r
1.18.1.2 reduced ferredoxin + NADP+ Pisum sativum enzyme catalyzes the final step of photosynthetic electron transfer from the iron-sulfur protein ferredoxin reduced by photosystem I to NADP+ providing NADPH necessary for CO2 assimilation in plants, in root and heterotrophic tissue, the reaction is driven towards ferredoxin reduction oxidized ferredoxin + NADPH
-
 r
1.18.1.2 reduced ferredoxin + NADP+ Zea mays enzyme catalyzes the final step of photosynthetic electron transfer from the iron-sulfur protein ferredoxin reduced by photosystem I to NADP+ providing NADPH necessary for CO2 assimilation in plants, in root and heterotrophic tissue, the reaction is driven towards ferredoxin reduction oxidized ferredoxin + NADPH
-
 r
1.18.1.2 reduced ferredoxin + NADP+ Capsicum annuum enzyme catalyzes the final step of photosynthetic electron transfer from the iron-sulfur protein ferredoxin reduced by photosystem I to NADP+ providing NADPH necessary for CO2 assimilation in plants, in root and heterotrophic tissue, the reaction is driven towards ferredoxin reduction oxidized ferredoxin + NADPH
-
 r
1.18.1.2 reduced ferredoxin + NADP+ Cyanobacteria enzyme catalyzes the final step of photosynthetic electron transfer fron the iron-sulfur protein ferredoxin reduced by photosystem I to NADP+ providing NADPH necessary for CO2 assimilation, enzyme is involved in dinitrogen fixation in heterocysts oxidized ferredoxin + NADPH
-
 r
1.18.1.2 reduced ferredoxin + NADP+ Escherichia coli enzyme is involved in protection against oxidative stress, and in activation of anaerobic enzymes oxidized ferredoxin + NADPH
-
 r
1.18.1.2 reduced ferredoxin + NADP+ Zea mays in root and heterotrophic tissue, the reaction is driven towards ferredoxin reduction, reaction is part of nitrogen assimilation in nonphotosynthetic tissues oxidized ferredoxin + NADPH
-
 r

Organism

EC Number Organism UniProt Comment Textmining
1.18.1.2 Anabaena sp.
-
-
-
1.18.1.2 Azotobacter vinelandii
-
-
-
1.18.1.2 Capsicum annuum
-
-
-
1.18.1.2 Cyanobacteria
-
-
-
1.18.1.2 Escherichia coli
-
-
-
1.18.1.2 Pisum sativum
-
-
-
1.18.1.2 Rhodobacter capsulatus
-
-
-
1.18.1.2 Spinacia oleracea
-
-
-
1.18.1.2 Zea mays
-
-
-

Reaction

EC Number Reaction Comment Organism Reaction ID
1.18.1.2 2 reduced ferredoxin + NADP+ + H+ = 2 oxidized ferredoxin + NADPH reaction mechanism Rhodobacter capsulatus
a
1.18.1.2 2 reduced ferredoxin + NADP+ + H+ = 2 oxidized ferredoxin + NADPH reaction mechanism Azotobacter vinelandii
a
1.18.1.2 2 reduced ferredoxin + NADP+ + H+ = 2 oxidized ferredoxin + NADPH active site structure, reaction mechanism Pisum sativum
a
1.18.1.2 2 reduced ferredoxin + NADP+ + H+ = 2 oxidized ferredoxin + NADPH active site structure, reaction mechanism Zea mays
a
1.18.1.2 2 reduced ferredoxin + NADP+ + H+ = 2 oxidized ferredoxin + NADPH active site structure, reaction mechanism Capsicum annuum
a
1.18.1.2 2 reduced ferredoxin + NADP+ + H+ = 2 oxidized ferredoxin + NADPH active site structure of the plant-type enzyme, reaction mechanism Cyanobacteria
a
1.18.1.2 2 reduced ferredoxin + NADP+ + H+ = 2 oxidized ferredoxin + NADPH active site structure, ping pong reaction mechanism Spinacia oleracea
a
1.18.1.2 2 reduced ferredoxin + NADP+ + H+ = 2 oxidized ferredoxin + NADPH reaction mechanism, interaction and electron transfer Anabaena sp.
a
1.18.1.2 2 reduced ferredoxin + NADP+ + H+ = 2 oxidized ferredoxin + NADPH reaction mechanism, substrate recognition mechanism Escherichia coli
a

Source Tissue

EC Number Source Tissue Comment Organism Textmining
1.18.1.2 heterocyst
-
 Cyanobacteria
-
1.18.1.2 leaf
-
 Spinacia oleracea
-
1.18.1.2 leaf
-
 Zea mays
-
1.18.1.2 root
-
 Zea mays
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.18.1.2 2 ferricyanide + NADPH diaphorase reaction Escherichia coli 2 ferrocyanide + NADP+ + H+
-
 ?
1.18.1.2 2 ferricyanide + NADPH diaphorase reaction Spinacia oleracea 2 ferrocyanide + NADP+ + H+
-
 ?
1.18.1.2 2 ferricyanide + NADPH diaphorase reaction Anabaena sp. 2 ferrocyanide + NADP+ + H+
-
 ir
1.18.1.2 additional information the diaphorase reaction with NADPH and different electron acceptors, such as ferricyanide, complexed transition metals, substituted phenols, nitro derivatives, tetrazolium salts, NAD+, viologens, quinones, and cytochromes, is highly irreversible Rhodobacter capsulatus ?
-
 ?
1.18.1.2 additional information the diaphorase reaction with NADPH and different electron acceptors, such as ferricyanide, complexed transition metals, substituted phenols, nitro derivatives, tetrazolium salts, NAD+, viologens, quinones, and cytochromes, is highly irreversible Anabaena sp. ?
-
 ?
1.18.1.2 additional information the diaphorase reaction with NADPH and different electron acceptors, such as ferricyanide, complexed transition metals, substituted phenols, nitroderivatives, tetrazolium salts, NAD+, viologens, quinones, and cytochromes, is highly irreversible Escherichia coli ?
-
 ?
1.18.1.2 additional information the diaphorase reaction with NADPH and different electron acceptors, such as ferricyanide, complexed transition metals, substituted phenols, nitroderivatives, tetrazolium salts, NAD+, viologens, quinones, and cytochromes, is highly irreversible Azotobacter vinelandii ?
-
 ?
1.18.1.2 NADPH + acceptor the diaphorase reaction with NADPH and different electron acceptors, such as ferricyanide, complexed transition metals, substituted phenols, nitro derivatives, tetrazolium salts, NAD+, viologens, quinones, and cytochromes, is mostly irreversible, probably due to restrictions of formation of the caged radical pair and/or the covalent (C4alpha)-flavin hydroperoxide intermediates required for efficient oxygen reduction, acceptors enhance the oxidation reaction several fold, e.g. ferredoxin, flavodoxin, viologens, nitro derivatives, and quinones, that can readily engage in oxygen-dependent redox cycling leading to formation of superoxide Spinacia oleracea NADP+ + reduced acceptor
-
 ?
1.18.1.2 NADPH + acceptor the diaphorase reaction with NADPH and different electron acceptors, such as ferricyanide, complexed transition metals, substituted phenols, nitro derivatives, tetrazolium salts, NAD+, viologens, quinones, and cytochromes, is mostly irreversible, probably due to restrictions of formation of the caged radical pair and/or the covalent (C4alpha)-flavin hydroperoxide intermediates required for efficient oxygen reduction, acceptors enhance the oxidation reaction several fold, e.g. ferredoxin, flavodoxin, viologens, nitro derivatives, and quinones, that can readily engage in oxygen-dependent redox cycling leading to formation of superoxide Cyanobacteria NADP+ + reduced acceptor
-
 ?
1.18.1.2 NADPH + acceptor the diaphorase reaction with NADPH and different electron acceptors, such as ferricyanide, complexed transition metals, substituted phenols, nitro derivatives, tetrazolium salts, NAD+, viologens, quinones, and cytochromes, is mostly irreversible, probably due to restrictions of formation of the caged radical pair and/or the covalent (C4alpha)-flavin hydroperoxide intermediates required for efficient oxygen reduction, acceptors enhance the oxidation reaction severalfold, e.g. ferredoxin, flavodoxin, viologens, nitro derivatives, and quinones, that can readily engage in oxygen-dependent redox cycling leading to formation of superoxide Zea mays NADP+ + reduced acceptor
-
 ?
1.18.1.2 NADPH + acceptor the diaphorase reaction with NADPH and different electron acceptors, such as ferricyanide, complexed transition metals, substituted phenols, nitro derivatives, tetrazolium salts, NAD+, viologens, quinones, and cytochromes, is mostly irreversible, probably due to restrictions of formation of the caged radical pair and/or the covalent (C4alpha)-flavin hydroperoxide intermediates required for efficient oxygen reduction, acceptors enhance the oxidation reaction severalfold, e.g. ferredoxin, flavodoxin, viologens, nitro derivatives, and quinones, that can readily engage in oxygen-dependent redox cycling leading to formation of superoxide Capsicum annuum NADP+ + reduced acceptor
-
 ?
1.18.1.2 NADPH + acceptor the diaphorase reaction with NADPH and different electron acceptors, such as ferricyanide, complexed transition metals, substituted phenols, nitroderivatives, tetrazolium salts, NAD+, viologens, quinones, and cytochromes, is mostly irreversible, probably due to restrictions of formation of the caged radical pair and/or the covalent (C4alpha)-flavin hydroperoxide intermediates required for efficient oxygen reduction, acceptors enhance the oxidation reaction severalfold, e.g. ferredoxin, flavodoxin, viologens, nitroderivatives, and quinones, that can readily engage in oxygen-dependent redox cycling leading to formation of superoxide Pisum sativum NADP+ + reduced acceptor
-
 ?
1.18.1.2 reduced ferredoxin + NADP+
-
 Escherichia coli oxidized ferredoxin + NADPH
-
 r
1.18.1.2 reduced ferredoxin + NADP+
-
 Rhodobacter capsulatus oxidized ferredoxin + NADPH
-
 r
1.18.1.2 reduced ferredoxin + NADP+
-
 Azotobacter vinelandii oxidized ferredoxin + NADPH
-
 r
1.18.1.2 reduced ferredoxin + NADP+
-
 Anabaena sp. oxidized ferredoxin + NADPH
-
 r
1.18.1.2 reduced ferredoxin + NADP+ enzyme catalyzes the final step of photosynthetic electron transfer from the iron-sulfur protein ferredoxin reduced by photosystem I to NADP+ providing NADPH necessary for CO2 assimilation in plants, in root and heterotrophic tissue, the reaction is driven towards ferredoxin reduction Spinacia oleracea oxidized ferredoxin + NADPH
-
 r
1.18.1.2 reduced ferredoxin + NADP+ enzyme catalyzes the final step of photosynthetic electron transfer from the iron-sulfur protein ferredoxin reduced by photosystem I to NADP+ providing NADPH necessary for CO2 assimilation in plants, in root and heterotrophic tissue, the reaction is driven towards ferredoxin reduction Pisum sativum oxidized ferredoxin + NADPH
-
 r
1.18.1.2 reduced ferredoxin + NADP+ enzyme catalyzes the final step of photosynthetic electron transfer from the iron-sulfur protein ferredoxin reduced by photosystem I to NADP+ providing NADPH necessary for CO2 assimilation in plants, in root and heterotrophic tissue, the reaction is driven towards ferredoxin reduction Zea mays oxidized ferredoxin + NADPH
-
 r
1.18.1.2 reduced ferredoxin + NADP+ enzyme catalyzes the final step of photosynthetic electron transfer from the iron-sulfur protein ferredoxin reduced by photosystem I to NADP+ providing NADPH necessary for CO2 assimilation in plants, in root and heterotrophic tissue, the reaction is driven towards ferredoxin reduction Capsicum annuum oxidized ferredoxin + NADPH
-
 r
1.18.1.2 reduced ferredoxin + NADP+ enzyme catalyzes the final step of photosynthetic electron transfer fron the iron-sulfur protein ferredoxin reduced by photosystem I to NADP+ providing NADPH necessary for CO2 assimilation, enzyme is involved in dinitrogen fixation in heterocysts Cyanobacteria oxidized ferredoxin + NADPH
-
 r
1.18.1.2 reduced ferredoxin + NADP+ enzyme is involved in protection against oxidative stress, and in activation of anaerobic enzymes Escherichia coli oxidized ferredoxin + NADPH
-
 r
1.18.1.2 reduced ferredoxin + NADP+ in root and heterotrophic tissue, the reaction is driven towards ferredoxin reduction, reaction is part of nitrogen assimilation in nonphotosynthetic tissues Zea mays oxidized ferredoxin + NADPH
-
 r
1.18.1.2 reduced ferredoxin + NADP+ release of oxidized ferredoxin is rate-limiting Spinacia oleracea oxidized ferredoxin + NADPH
-
 r
1.18.1.2 reduced ferredoxin + NADP+ release of oxidized ferredoxin is rate-limiting Capsicum annuum oxidized ferredoxin + NADPH
-
 r
1.18.1.2 reduced ferredoxin + NADP+ structure of the ferredoxin-enzyme complex, ferredoxin binds to the concave region of the FAD domain, overview, release of oxidized ferredoxin is rate-limiting Zea mays oxidized ferredoxin + NADPH
-
 r
1.18.1.2 reduced ferredoxin + NADP+ structure of the ferredoxin-enzyme complex, release of oxidized ferredoxin is rate-limiting Pisum sativum oxidized ferredoxin + NADPH
-
 r
1.18.1.2 reduced ferredoxin + NADP+ structure of the ferredoxin-enzyme complex, release of oxidized ferredoxin is rate-limiting Zea mays oxidized ferredoxin + NADPH
-
 r
1.18.1.2 reduced ferredoxin + NADP+ structure of the ferredoxin-enzyme complex, release of oxidized ferredoxin is rate-limiting Cyanobacteria oxidized ferredoxin + NADPH
-
 r

Subunits

EC Number Subunits Comment Organism
1.18.1.2 monomer
-
 Escherichia coli
1.18.1.2 monomer
-
 Spinacia oleracea
1.18.1.2 monomer
-
 Pisum sativum
1.18.1.2 monomer
-
 Zea mays
1.18.1.2 monomer
-
 Rhodobacter capsulatus
1.18.1.2 monomer
-
 Azotobacter vinelandii
1.18.1.2 monomer
-
 Capsicum annuum
1.18.1.2 monomer
-
 Anabaena sp.
1.18.1.2 monomer
-
 Cyanobacteria

Synonyms

EC Number Synonyms Comment Organism
1.18.1.2 ferredoxin (flavodoxin)-NAD(P)H reductase
-
 Escherichia coli
1.18.1.2 ferredoxin (flavodoxin)-NAD(P)H reductase
-
 Spinacia oleracea
1.18.1.2 ferredoxin (flavodoxin)-NAD(P)H reductase
-
 Pisum sativum
1.18.1.2 ferredoxin (flavodoxin)-NAD(P)H reductase
-
 Zea mays
1.18.1.2 ferredoxin (flavodoxin)-NAD(P)H reductase
-
 Rhodobacter capsulatus
1.18.1.2 ferredoxin (flavodoxin)-NAD(P)H reductase
-
 Azotobacter vinelandii
1.18.1.2 ferredoxin (flavodoxin)-NAD(P)H reductase
-
 Capsicum annuum
1.18.1.2 ferredoxin (flavodoxin)-NAD(P)H reductase
-
 Anabaena sp.
1.18.1.2 ferredoxin (flavodoxin)-NAD(P)H reductase
-
 Cyanobacteria
1.18.1.2 ferredoxin-NAD(P)H reductase
-
 Escherichia coli
1.18.1.2 ferredoxin-NAD(P)H reductase
-
 Spinacia oleracea
1.18.1.2 ferredoxin-NAD(P)H reductase
-
 Pisum sativum
1.18.1.2 ferredoxin-NAD(P)H reductase
-
 Zea mays
1.18.1.2 ferredoxin-NAD(P)H reductase
-
 Rhodobacter capsulatus
1.18.1.2 ferredoxin-NAD(P)H reductase
-
 Azotobacter vinelandii
1.18.1.2 ferredoxin-NAD(P)H reductase
-
 Capsicum annuum
1.18.1.2 ferredoxin-NAD(P)H reductase
-
 Anabaena sp.
1.18.1.2 ferredoxin-NAD(P)H reductase
-
 Cyanobacteria
1.18.1.2 ferredoxin-NADP+ reductase
-
 Escherichia coli
1.18.1.2 ferredoxin-NADP+ reductase
-
 Spinacia oleracea
1.18.1.2 ferredoxin-NADP+ reductase
-
 Pisum sativum
1.18.1.2 ferredoxin-NADP+ reductase
-
 Zea mays
1.18.1.2 ferredoxin-NADP+ reductase
-
 Rhodobacter capsulatus
1.18.1.2 ferredoxin-NADP+ reductase
-
 Azotobacter vinelandii
1.18.1.2 ferredoxin-NADP+ reductase
-
 Capsicum annuum
1.18.1.2 ferredoxin-NADP+ reductase
-
 Anabaena sp.
1.18.1.2 ferredoxin-NADP+ reductase
-
 Cyanobacteria
1.18.1.2 FNR
-
 Escherichia coli
1.18.1.2 FNR
-
 Spinacia oleracea
1.18.1.2 FNR
-
 Pisum sativum
1.18.1.2 FNR
-
 Zea mays
1.18.1.2 FNR
-
 Rhodobacter capsulatus
1.18.1.2 FNR
-
 Azotobacter vinelandii
1.18.1.2 FNR
-
 Capsicum annuum
1.18.1.2 FNR
-
 Anabaena sp.
1.18.1.2 FNR
-
 Cyanobacteria
1.18.1.2 More formerly termed thylakoid-bound diaphorase Pisum sativum

Temperature Stability [°C]

EC Number Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
1.18.1.2 41
-
 inactivation of the reduced enzyme Escherichia coli
1.18.1.2 66
-
 inactivation of the oxidized enzyme Escherichia coli

Turnover Number [1/s]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
1.18.1.2 additional information
-
 additional information
-
 Escherichia coli
1.18.1.2 0.15
-
 oxidized ferredoxin with NADPH Escherichia coli
1.18.1.2 27
-
 NADPH electron transfer via the enzyme to Fe(CN)63- Escherichia coli
1.18.1.2 200
-
 reduced ferredoxin above, electron transfer via the enzyme to NADP+ Anabaena sp.
1.18.1.2 225
-
 NADPH electron transfer via the enzyme to oxidized ferredoxin and further to cytochrome c Anabaena sp.
1.18.1.2 225 520 NADPH electron transfer via the enzyme to K3Fe(CN)6 Anabaena sp.
1.18.1.2 250
-
 NADPH electron transfer via the enzyme to oxidized ferredoxin and further to cytochrome c Spinacia oleracea
1.18.1.2 520
-
 NADPH electron transfer via the enzyme to oxidized ferredoxin and further to cytochrome c Escherichia coli
1.18.1.2 550
-
 NADPH electron transfer via the enzyme to K3Fe(CN)6 Spinacia oleracea
1.18.1.2 600
-
 reduced ferredoxin electron transfer via the enzyme to NADP+ Spinacia oleracea

Cofactor

EC Number Cofactor Comment Organism Structure
1.18.1.2 FAD noncovalently bound prosthetic group Escherichia coli
1.18.1.2 FAD noncovalently bound prosthetic group Spinacia oleracea
1.18.1.2 FAD noncovalently bound prosthetic group Pisum sativum
1.18.1.2 FAD noncovalently bound prosthetic group Zea mays
1.18.1.2 FAD noncovalently bound prosthetic group Rhodobacter capsulatus
1.18.1.2 FAD noncovalently bound prosthetic group Azotobacter vinelandii
1.18.1.2 FAD noncovalently bound prosthetic group Capsicum annuum
1.18.1.2 FAD noncovalently bound prosthetic group Anabaena sp.
1.18.1.2 FAD noncovalently bound prosthetic group Cyanobacteria
1.18.1.2 FAD noncovalently bound prosthetic group, binding domain structure, ferredoxin binds to the concave region of the FAD domain Zea mays
1.18.1.2 additional information poor activity with NAD(H) Escherichia coli
1.18.1.2 additional information poor activity with NAD(H) Spinacia oleracea
1.18.1.2 additional information poor activity with NAD(H) Pisum sativum
1.18.1.2 additional information poor activity with NAD(H) Zea mays
1.18.1.2 additional information poor activity with NAD(H) Rhodobacter capsulatus
1.18.1.2 additional information poor activity with NAD(H) Azotobacter vinelandii
1.18.1.2 additional information poor activity with NAD(H) Capsicum annuum
1.18.1.2 additional information poor activity with NAD(H) Anabaena sp.
1.18.1.2 additional information poor activity with NAD(H) Cyanobacteria
1.18.1.2 NADP+ binding domain structure of the plant-type enzyme, binding mechanism Cyanobacteria
1.18.1.2 NADP+ binding domain structure, binding mechanism Zea mays
1.18.1.2 NADP+ binding domain structure, binding mechanism Capsicum annuum
1.18.1.2 NADP+ binding domain structure, binding mechanism, binding site structure and involved residues, overview Spinacia oleracea
1.18.1.2 NADP+ binding domain structure, binding mechanism, binding site structure and involved residues, overview Pisum sativum
1.18.1.2 NADP+ binding mechanism Rhodobacter capsulatus
1.18.1.2 NADP+ binding mechanism Azotobacter vinelandii
1.18.1.2 NADP+ binding mechanism Anabaena sp.
1.18.1.2 NADP+ binding mechanism, cofactor is tightly bound, binding site structure and involved residues, overview Escherichia coli
1.18.1.2 NADPH binding domain structure of the plant-type enzyme, binding mechanism Cyanobacteria
1.18.1.2 NADPH binding domain structure, binding mechanism Zea mays
1.18.1.2 NADPH binding domain structure, binding mechanism Capsicum annuum
1.18.1.2 NADPH binding domain structure, binding mechanism, binding site structure and involved residues, overview Spinacia oleracea
1.18.1.2 NADPH binding domain structure, binding mechanism, binding site structure and involved residues, overview Pisum sativum
1.18.1.2 NADPH binding mechanism Rhodobacter capsulatus
1.18.1.2 NADPH binding mechanism Azotobacter vinelandii
1.18.1.2 NADPH binding mechanism Anabaena sp.
1.18.1.2 NADPH binding mechanism, cofactor is tightly bound, binding site structure and involved residues, overview Escherichia coli