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Literature summary for 1.18.1.2 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
Search for more literature for 1.18.1.2

Protein Variants

Protein Variants Comment Organism
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.
additional information construction of active site mutants Anabaena sp.
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.
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.
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.
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]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
additional information
-
 additional information Stopped-flow pre-steady-state kinetics, overview Anabaena sp.

Natural Substrates/ Products (Substrates)

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

Organism

Organism UniProt Comment Textmining
Anabaena sp.
-
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2 reduced ferredoxin + NADP+
-
 Anabaena sp. 2 oxidized ferredoxin + NADPH + H+
-
 r
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

Synonyms Comment Organism
adrenodoxin reductase
-
 Anabaena sp.
FNR
-
 Anabaena sp.

Temperature Optimum [°C]

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

pH Optimum

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

Cofactor

Cofactor Comment Organism Structure
FAD dependent on Anabaena sp.

General Information

General Information Comment Organism
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.