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Literature summary for 1.19.1.1 extracted from

  • Bortolotti, A.; Sanchez-Azqueta, A.; Maya, C.M.; Velazquez-Campoy, A.; Hermoso, J.A.; Medina, M.; Cortez, N.
    The C-terminal extension of bacterial flavodoxin-reductases: involvement in the hydride transfer mechanism from the coenzyme (2014), Biochim. Biophys. Acta, 1837, 33-43.
    View publication on PubMed
Search for more literature for 1.19.1.1

Protein Variants

Protein Variants Comment Organism
A266Y mutant does not allow formation of active charge-transfer complexes, probably due to restraints of C-terminus pliability. Mutant displays higher affinity for NADP+ than wild-type Rhodobacter capsulatus
A266y/Del267-272 deletion/mutation emulates the structure present in plastidic versions of the protein. It does not modify the general geometry of FAD itself, but increases exposure of the flavin to the solvent, prevents a productive geometry of FAD:NADP(H) complex and decreases the protein thermal stability. Mutant displays higher affinity for NADP+ than wild-type Rhodobacter capsulatus
Del267-272 deletion emulates the structure present in plastidic versions of the protein, mutant displays higher affinity for NADP+ than wild-type Rhodobacter capsulatus

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.009
-
 NADPH mutant Del267-272, substrate 2,6-dichlorophenolindophenol, pH 7.2, 25°C Rhodobacter capsulatus
0.02
-
 NADPH mutant Del267-272, substrate ferricyanide, pH 7.2, 25°C Rhodobacter capsulatus
0.032
-
 NADPH mutant A266Y, substrate ferricyanide, pH 7.2, 25°C Rhodobacter capsulatus
0.039
-
 NADPH mutant A266Y/Del267-272, substrate 2,6-dichlorophenolindophenol, pH 7.2, 25°C Rhodobacter capsulatus
0.043
-
 NADPH mutant A266Y, substrate 2,6-dichlorophenolindophenol, pH 7.2, 25°C Rhodobacter capsulatus
0.043
-
 NADPH mutant A266Y/Del267-272, substrate ferricyanide, pH 7.2, 25°C Rhodobacter capsulatus
0.085
-
 NADPH wild-type, substrate 2,6-dichlorophenolindophenol, pH 7.2, 25°C Rhodobacter capsulatus
0.093
-
 NADPH wild-type, substrate ferricyanide, pH 7.2, 25°C Rhodobacter capsulatus

Organism

Organism UniProt Comment Textmining
Rhodobacter capsulatus Q9L6V3 enzyme catalyzes reactions of both EC 1.18.1.2 and EC 1.19.1.1
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2 ferricyanide + NADPH
-
 Rhodobacter capsulatus 2 ferrocyanide + NADP+ + H+
-
 ?
2,6-dichlorophenolindophenol + NADPH
-
 Rhodobacter capsulatus reduced 2,6-dichlorophenolindophenol + NADP+
-
 ?

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
1
-
 NADPH mutant Del267-272, substrate 2,6-dichlorophenolindophenol, pH 7.2, 25°C Rhodobacter capsulatus
7
-
 NADPH mutant A266Y, substrate 2,6-dichlorophenolindophenol, pH 7.2, 25°C Rhodobacter capsulatus
8
-
 NADPH mutant Del267-272, substrate ferricyanide, pH 7.2, 25°C Rhodobacter capsulatus
12
-
 NADPH mutant A266Y/Del267-272, substrate ferricyanide, pH 7.2, 25°C Rhodobacter capsulatus
20
-
 NADPH wild-type, substrate 2,6-dichlorophenolindophenol, pH 7.2, 25°C Rhodobacter capsulatus
68
-
 NADPH mutant A266Y, substrate ferricyanide, pH 7.2, 25°C Rhodobacter capsulatus
222
-
 NADPH wild-type, substrate ferricyanide, pH 7.2, 25°C Rhodobacter capsulatus