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Literature summary extracted from

  • Peregrina, J.R.; Sanchez-Azqueta, A.; Herguedas, B.; Martinez-Julvez, M.; Medina, M.
    Role of specific residues in coenzyme binding, charge-transfer complex formation, and catalysis in Anabaena ferredoxin NADP+-reductase (2010), Biochim. Biophys. Acta, 1797, 1638-1646.
    View publication on PubMed

Protein Variants

EC Number Protein Variants Comment Organism
1.18.1.2 E301A site-directed mutagensis, kinetic parameters for hydride and deuteride transfer processes between enzyme and NADP+ in comparison to the wild-type enzyme, overview Anabaena sp.
1.18.1.2 additional information construction of active site mutants Anabaena sp.
1.18.1.2 R100A site-directed mutagensis, kinetic parameters for hydride and deuteride transfer processes between enzyme and NADP+ in comparison to the wild-type enzyme, overview Anabaena sp.
1.18.1.2 Y303F site-directed mutagensis, kinetic parameters for hydride and deuteride transfer processes between enzyme and NADP+ in comparison to the wild-type enzyme, overview Anabaena sp.
1.18.1.2 Y303S site-directed mutagensis, kinetic parameters for hydride and deuteride transfer processes between enzyme and NADP+ in comparison to the wild-type enzyme, overview Anabaena sp.
1.18.1.2 Y303W site-directed mutagensis, kinetic parameters for hydride and deuteride transfer processes between enzyme and NADP+ in comparison to the wild-type enzyme, overview Anabaena sp.

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 pre-steady-state kinetics, overview Anabaena sp.

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
1.18.1.2 2 reduced ferredoxin + NADP+ Anabaena sp.
-
2 oxidized ferredoxin + NADPH + H+
-
r

Organism

EC Number Organism UniProt Comment Textmining
1.18.1.2 Anabaena sp.
-
-
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.18.1.2 2 reduced ferredoxin + NADP+
-
Anabaena sp. 2 oxidized ferredoxin + NADPH + H+
-
r
1.18.1.2 2 reduced ferredoxin + NADP+ two transient charge-transfer complexes occur prior and upon hydride transfer in the reversible reaction, spectral properties and activities of wild-type and mutant enzymes, overview. Need for an adequate initial interaction between the 2'P-AMP portion of NADP+/H and FNR that provides subsequent conformational changes leading to charge-transfer complex formation Anabaena sp. 2 oxidized ferredoxin + NADPH + H+
-
r

Synonyms

EC Number Synonyms Comment Organism
1.18.1.2 adrenodoxin reductase
-
Anabaena sp.
1.18.1.2 FNR
-
Anabaena sp.

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
1.18.1.2 25
-
assay at Anabaena sp.

pH Optimum

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

Cofactor

EC Number Cofactor Comment Organism Structure
1.18.1.2 FAD dependent on Anabaena sp.

General Information

EC Number General Information Comment Organism
1.18.1.2 additional information while in the wild-type, vibrational enhanced modulation of the active site contributes to the tunnel probability of hydride transfer, complexes of some of the active site mutants with the coenzyme hardly allow the relative movement of isoalloxazine and nicotinamide rings along the hydride transfer reaction. The architecture of the wild-type FNR active site precisely contributes to reduce the stacking probability between the isoalloxazine and nicotinamide rings in the catalytically competent complex, modulating the angle and distance between the N5 of the FAD isoalloxazine and the C4 of the coenzyme nicotinamide to values that ensure efficient hydride transfer processes Anabaena sp.