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Literature summary extracted from

  • Nogues, I.; Tejero, J.; Hurley, J.K.; Paladini, D.; Frago, S.; Tollin, G.; Mayhew, S.G.; Gomez-Moreno, C.; Ceccarelli, E.A.; Carrillo, N.; Medina, M.
    Role of the C-terminal tyrosine of ferredoxin-nicotinamide adenine dinucleotide phosphate reductase in the electron transfer processes with its protein partners ferredoxin and flavodoxin (2004), Biochemistry, 43, 6127-6137.
    View publication on PubMed

Cloned(Commentary)

EC Number Cloned (Comment) Organism
1.18.1.2 expression of wild-type and mutant enzymes in Escherichia coli strain BL21(DE3) Anabaena sp.

Protein Variants

EC Number Protein Variants Comment Organism
1.18.1.2 Y303F site-directed mutagenesis, about 30% of the wild-type enzyme activity with ferredoxin, about 25% of the wild-type enzyme activity with flavodoxin Anabaena sp.
1.18.1.2 Y303S site-directed mutagenesis, inactive mutant Anabaena sp.
1.18.1.2 Y303W site-directed mutagenesis, nearly inactive mutant Anabaena sp.
1.18.1.2 Y308F site-directed mutagenesis, about 20% of the wild-type enzyme activity with ferredoxin, about 11% of the wild-type enzyme activity with flavodoxin Pisum sativum
1.18.1.2 Y308S site-directed mutagenesis, about 5% of the wild-type enzyme activity with ferredoxin, no activity with flavodoxin Pisum sativum
1.18.1.2 Y308W site-directed mutagenesis, nearly inactive mutant with ferredoxin, about 25% of the wild-type enzyme activity with flavodoxin Pisum sativum
1.19.1.1 Y303F about 30% of the wild-type enzyme activity with ferredoxin, about 25% of the wild-type enzyme activity with flavodoxin Nostoc sp.
1.19.1.1 Y303S inactive. Mutation shifts the flavin reduction potential to less negative values, whereas semiquinone stabilization is severely hampered Nostoc sp.
1.19.1.1 Y303W almost inactive Nostoc sp.
1.19.1.1 Y308F about 20% of the wild-type enzyme activity with ferredoxin, about 11% of the wild-type enzyme activity with flavodoxin Pisum sativum
1.19.1.1 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 Pisum sativum
1.19.1.1 Y308W about 5% of the wild-type enzyme activity with ferredoxin, no activity with flavodoxin Pisum sativum

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
1.18.1.2 additional information
-
 additional information stopped-flow and laser flash kinetic measurements, steady-state kinetics, dissociation constants and reduction potentials of wild-type and mutant enzymes Pisum sativum
1.18.1.2 additional information
-
 additional information stopped-flow and laser flash kinetic measurements, steady-state kinetics, dissociation constants and reduction potentials of wild-type and mutant enzymes Anabaena sp.
1.18.1.2 0.0058
-
 reduced ferredoxin pH 8.0, 13°C, mutant Y308F Pisum sativum
1.18.1.2 0.0065
-
 reduced ferredoxin pH 8.0, 13°C, wild-type enzyme Pisum sativum
1.18.1.2 0.009
-
 reduced ferredoxin pH 8.0, 13°C, mutant Y308S Pisum sativum
1.18.1.2 0.011
-
 reduced ferredoxin pH 8.0, 13°C, wild-type enzyme Anabaena sp.
1.18.1.2 0.017
-
 reduced ferredoxin pH 8.0, 13°C, mutant Y308W Pisum sativum
1.18.1.2 0.051
-
 reduced ferredoxin pH 8.0, 13°C, mutant Y303F Anabaena sp.
1.19.1.1 0.0167
-
 reduced flavodoxin wild-type, pH 8.0, 25°C Pisum sativum
1.19.1.1 0.017
-
 reduced flavodoxin mutant Y308W, pH 8.0, 25°C Pisum sativum
1.19.1.1 0.02
-
 reduced flavodoxin mutant Y308F, pH 8.0, 25°C Pisum sativum
1.19.1.1 0.033
-
 reduced flavodoxin wild-type, pH 8.0, 25°C Nostoc sp.
1.19.1.1 0.043
-
 reduced flavodoxin mutant Y303F, pH 8.0, 25°C Nostoc sp.

Localization

EC Number Localization Comment Organism GeneOntology No. Textmining
1.19.1.1 chloroplast
-
 Pisum sativum 9507
-

Organism

EC Number Organism UniProt Comment Textmining
1.18.1.2 Anabaena sp. P21890
-
-
1.18.1.2 Pisum sativum
-
-
-
1.19.1.1 Nostoc sp. P21890 enzyme catalyzes reactions of both EC 1.18.1.2 and EC 1.19.1.1
-
1.19.1.1 Nostoc sp. ATCC 29151 P21890 enzyme catalyzes reactions of both EC 1.18.1.2 and EC 1.19.1.1
-
1.19.1.1 Pisum sativum P10933 enzyme catalyzes reactions of both EC 1.18.1.2 and EC 1.19.1.1
-

Purification (Commentary)

EC Number Purification (Comment) Organism
1.18.1.2 recombinant wild-type and mutant enzymes from Escherichia coli strain Bl21(DE3) Anabaena sp.

Reaction

EC Number Reaction Comment Organism Reaction ID
1.18.1.2 2 reduced ferredoxin + NADP+ + H+ = 2 oxidized ferredoxin + NADPH catalytic mechanism, initiated by reduction of FAD cofactor by obligatory one-electron carriers ferredoxin or flavodoxin in presence of NADP+, the enzymes' C-terminal tyrosine residue is involved modulating the enzyme affinity for NADP+/NADPH Pisum sativum
a
1.18.1.2 2 reduced ferredoxin + NADP+ + H+ = 2 oxidized ferredoxin + NADPH catalytic mechanism, initiated by reduction of FAD cofactor by obligatory one-electron carriers ferredoxin or flavodoxin in presence of NADP+, the enzymes' C-terminal tyrosine residue is involved modulating the enzyme affinity for NADP+/NADPH Anabaena sp.
a

Source Tissue

EC Number Source Tissue Comment Organism Textmining
1.19.1.1 leaf
-
 Pisum sativum
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.18.1.2 reduced ferredoxin + NADP+
-
 Pisum sativum oxidized ferredoxin + NADPH
-
 r
1.18.1.2 reduced ferredoxin + NADP+
-
 Anabaena sp. oxidized ferredoxin + NADPH
-
 r
1.18.1.2 reduced ferredoxin + NADP+
-
 Pisum sativum oxidized ferredoxin + NADPH + H+
-
 r
1.18.1.2 reduced ferredoxin + NADP+
-
 Anabaena sp. oxidized ferredoxin + NADPH + H+
-
 r
1.18.1.2 reduced flavodoxin + NADP+
-
 Pisum sativum oxidized flavodoxin + NADPH + H+
-
 r
1.18.1.2 reduced flavodoxin + NADP+
-
 Anabaena sp. oxidized flavodoxin + NADPH + H+
-
 r
1.19.1.1 reduced flavodoxin + NADP+
-
 Pisum sativum oxidized flavodoxin + NADPH + H+
-
 ?
1.19.1.1 reduced flavodoxin + NADP+
-
 Nostoc sp. oxidized flavodoxin + NADPH + H+
-
 ?
1.19.1.1 reduced flavodoxin + NADP+
-
 Nostoc sp. ATCC 29151 oxidized flavodoxin + NADPH + H+
-
 ?

Subunits

EC Number Subunits Comment Organism
1.19.1.1 More the C-terminal tyrosine residue lowers the affinity for NADP(H) to levels compatible with steady-state turnover, contributes to the flavin semiquinone stabilization required for electron splitting, and modulates the rates of electron exchange with the protein partners Pisum sativum
1.19.1.1 More the C-terminal tyrosine residue lowers the affinity for NADP(H) to levels compatible with steady-state turnover, contributes to the flavin semiquinone stabilization required for electron splitting, and modulates the rates of electron exchange with the protein partners Nostoc sp.

Synonyms

EC Number Synonyms Comment Organism
1.18.1.2 ferredoxin-nicotinamide adenine dinucleotide phosphate reductase
-
 Pisum sativum
1.18.1.2 ferredoxin-nicotinamide adenine dinucleotide phosphate reductase
-
 Anabaena sp.
1.18.1.2 FNR
-
 Pisum sativum
1.18.1.2 FNR
-
 Anabaena sp.
1.19.1.1 PETH
-
 Pisum sativum
1.19.1.1 PETH
-
 Nostoc sp.

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
1.18.1.2 13
-
 assay at Pisum sativum
1.18.1.2 13
-
 assay at Anabaena sp.

Turnover Number [1/s]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
1.18.1.2 1
-
 reduced ferredoxin pH 8.0, 13°C, mutant Y303W Anabaena sp.
1.18.1.2 2.5
-
 reduced flavodoxin pH 8.0, 13°C, mutant Y303W Anabaena sp.
1.18.1.2 2.5
-
 reduced ferredoxin pH 8.0, 13°C, mutant Y308W Pisum sativum
1.18.1.2 4
-
 reduced flavodoxin pH 8.0, 13°C, mutant Y308F Pisum sativum
1.18.1.2 7
-
 reduced flavodoxin pH 8.0, 13°C, mutant Y303F Anabaena sp.
1.18.1.2 7.7
-
 reduced ferredoxin pH 8.0, 13°C, mutant Y308S Pisum sativum
1.18.1.2 8.3
-
 reduced flavodoxin pH 8.0, 13°C, mutant Y308W Pisum sativum
1.18.1.2 23.3
-
 reduced flavodoxin pH 8.0, 13°C, wild-type enzyme Anabaena sp.
1.18.1.2 23.9
-
 reduced ferredoxin pH 8.0, 13°C, mutant Y308F Pisum sativum
1.18.1.2 30.6
-
 reduced flavodoxin pH 8.0, 13°C, wild-type enzyme Pisum sativum
1.18.1.2 32
-
 reduced ferredoxin pH 8.0, 13°C, mutant Y303F Anabaena sp.
1.18.1.2 139
-
 reduced ferredoxin pH 8.0, 13°C, wild-type enzyme Pisum sativum
1.18.1.2 200
-
 reduced ferredoxin pH 8.0, 13°C, wild-type enzyme Anabaena sp.
1.19.1.1 2.5
-
 reduced flavodoxin mutant Y303W, pH 8.0, 25°C Nostoc sp.
1.19.1.1 4
-
 reduced flavodoxin mutant Y308F, pH 8.0, 25°C Pisum sativum
1.19.1.1 7
-
 reduced flavodoxin mutant Y303F, pH 8.0, 25°C Nostoc sp.
1.19.1.1 8.3
-
 reduced flavodoxin mutant Y308W, pH 8.0, 25°C Pisum sativum
1.19.1.1 23.3
-
 reduced flavodoxin wild-type, pH 8.0, 25°C Nostoc sp.
1.19.1.1 30.6
-
 reduced flavodoxin wild-type, pH 8.0, 25°C Pisum sativum

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
1.18.1.2 8
-
 assay at Pisum sativum
1.18.1.2 8
-
 assay at Anabaena sp.

Cofactor

EC Number Cofactor Comment Organism Structure
1.18.1.2 FAD binding and hydride/electron transfer mechanism Pisum sativum
1.18.1.2 FAD binding and hydride/electron transfer mechanism Anabaena sp.
1.18.1.2 NADP+ binding and hydride transfer mechanism Pisum sativum
1.18.1.2 NADP+ binding and hydride transfer mechanism Anabaena sp.
1.18.1.2 NADPH binding and hydride transfer mechanism Pisum sativum
1.18.1.2 NADPH binding and hydride transfer mechanism Anabaena sp.

kcat/KM [mM/s]

EC Number kcat/KM Value [1/mMs-1] kcat/KM Value Maximum [1/mMs-1] Substrate Comment Organism Structure
1.19.1.1 170
-
 reduced flavodoxin mutant Y303F, pH 8.0, 25°C Nostoc sp.
1.19.1.1 200
-
 reduced flavodoxin mutant Y308F, pH 8.0, 25°C Pisum sativum
1.19.1.1 500
-
 reduced flavodoxin mutant Y308W, pH 8.0, 25°C Pisum sativum
1.19.1.1 700
-
 reduced flavodoxin wild-type, pH 8.0, 25°C Nostoc sp.
1.19.1.1 1800
-
 reduced flavodoxin wild-type, pH 8.0, 25°C Pisum sativum