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Literature summary for 1.18.1.2 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)

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

Protein Variants

Protein Variants Comment Organism
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.
Y303S site-directed mutagenesis, inactive mutant Anabaena sp.
Y303W site-directed mutagenesis, nearly inactive mutant Anabaena sp.
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
Y308S site-directed mutagenesis, about 5% of the wild-type enzyme activity with ferredoxin, no activity with flavodoxin Pisum sativum
Y308W site-directed mutagenesis, nearly inactive mutant with ferredoxin, about 25% of the wild-type enzyme activity with flavodoxin Pisum sativum

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
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
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.
0.0058
-
reduced ferredoxin pH 8.0, 13°C, mutant Y308F Pisum sativum
0.0065
-
reduced ferredoxin pH 8.0, 13°C, wild-type enzyme Pisum sativum
0.009
-
reduced ferredoxin pH 8.0, 13°C, mutant Y308S Pisum sativum
0.011
-
reduced ferredoxin pH 8.0, 13°C, wild-type enzyme Anabaena sp.
0.017
-
reduced ferredoxin pH 8.0, 13°C, mutant Y308W Pisum sativum
0.051
-
reduced ferredoxin pH 8.0, 13°C, mutant Y303F Anabaena sp.

Organism

Organism UniProt Comment Textmining
Anabaena sp. P21890
-
-
Pisum sativum
-
-
-

Purification (Commentary)

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

Reaction

Reaction Comment Organism Reaction ID
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
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.

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
reduced ferredoxin + NADP+
-
Pisum sativum oxidized ferredoxin + NADPH
-
r
reduced ferredoxin + NADP+
-
Anabaena sp. oxidized ferredoxin + NADPH
-
r
reduced ferredoxin + NADP+
-
Pisum sativum oxidized ferredoxin + NADPH + H+
-
r
reduced ferredoxin + NADP+
-
Anabaena sp. oxidized ferredoxin + NADPH + H+
-
r
reduced flavodoxin + NADP+
-
Pisum sativum oxidized flavodoxin + NADPH + H+
-
r
reduced flavodoxin + NADP+
-
Anabaena sp. oxidized flavodoxin + NADPH + H+
-
r

Synonyms

Synonyms Comment Organism
ferredoxin-nicotinamide adenine dinucleotide phosphate reductase
-
Pisum sativum
ferredoxin-nicotinamide adenine dinucleotide phosphate reductase
-
Anabaena sp.
FNR
-
Pisum sativum
FNR
-
Anabaena sp.

Temperature Optimum [°C]

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

Turnover Number [1/s]

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

pH Optimum

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

Cofactor

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