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Literature summary extracted from

  • Valle, L.; Abatedaga, I.; Vieyra, F.E.; Bortolotti, A.; Cortez, N.; Borsarelli, C.D.
    Enhancement of photophysical and photosensitizing properties of flavin adenine dinucleotide by mutagenesis of the C-terminal extension of a bacterial flavodoxin reductase (2015), Chemphyschem, 16, 872-883 .
    View publication on PubMed

Protein Variants

EC Number Protein Variants Comment Organism
1.18.1.2 A266Y site-directed mutagenesis, deletion of the six C-terminal amino acids FVGEGI beyond Ala266 is combined with the replacement A266Y to emulate the structure of plastidic reductases. THe mutations produce subtle global conformational changes, but strongly reduce the local rigidity of the FAD-binding pocket, exposing the isoalloxazine ring to the solvent. Thus, the ultrafast charge-transfer quenching of FAD* by the conserved Tyr66 residue is absent in the mutant series, producing enhancement of the excited singlet and triplet-state properties of FAD. All RcFPR variants display higher affinity for NADP+ than the wild-type Rhodobacter capsulatus

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
1.18.1.2 additional information
-
additional information spectroscopic steady-state and dynamic kinetics of wild-type and mutant DELTAA266, DELTAA266Y, and A266Y enzymes, detailed overview Rhodobacter capsulatus

Localization

EC Number Localization Comment Organism GeneOntology No. Textmining
1.18.1.2 chloroplast
-
Rhodobacter capsulatus 9507
-

Natural Substrates/ Products (Substrates)

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

Organism

EC Number Organism UniProt Comment Textmining
1.18.1.2 Rhodobacter capsulatus Q9L6V3
-
-

Reaction

EC Number Reaction Comment Organism Reaction ID
1.18.1.2 2 reduced ferredoxin + NADP+ + H+ = 2 oxidized ferredoxin + NADPH the overall reaction can be separated into a hydride-transfer step between NADP(H) and FAD, and an electron-exchange reaction between FAD and the electron-carrier protein partner Rhodobacter capsulatus

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.18.1.2 2 oxidized ferredoxin + NADPH
-
Rhodobacter capsulatus 2 reduced ferredoxin + NADP+ + H+
-
r

Subunits

EC Number Subunits Comment Organism
1.18.1.2 monomer
-
Rhodobacter capsulatus

Synonyms

EC Number Synonyms Comment Organism
1.18.1.2 ferredoxin-NADP(H) reductase
-
Rhodobacter capsulatus
1.18.1.2 RcFPR
-
Rhodobacter capsulatus

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
1.18.1.2 8
-
assay at Rhodobacter capsulatus

Cofactor

EC Number Cofactor Comment Organism Structure
1.18.1.2 FAD flavoprotein, analysis of specific interactions between FAD and the surrounding amino acids, overview Rhodobacter capsulatus
1.18.1.2 NADP+
-
Rhodobacter capsulatus
1.18.1.2 NADPH
-
Rhodobacter capsulatus