Cloned (Comment) | Organism |
---|---|
gene frd2, DNA and amino acid sequence determination and analysis, sequence comparisons, recombinant overexpression of N-terminally His-tagged enzyme in Escherichia coli strain BL21(DE3) | Corynebacterium crenatum |
Protein Variants | Comment | Organism |
---|---|---|
additional information | improvement of the intracellular environment for enhancing L-arginine production of Corynebacterium glutamicum by inactivation of H2O2-forming flavin reductases and optimization of ATP supply. Construction of mutants of gene frd2, strain 5-5(frd2) and deletion strains 5-5DELTAfrd2 and 5-5DELTAfrd12. The extracellular H2O2 concentrations of mutant 5-5DELTAfrd12 are lower than that of the wild-type strain SYPA5-5, and the extracellular H2O2 concentrations of mutant 5-5(frd2) is increased compared to the wild-type. Flavin reductase activities in frd1 and frd2 overexpression and deletion strains with NADH and FAD, overview | Corynebacterium crenatum |
KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
0.0084 | - |
NADH | with FMN, pH 7.5, 30°C, recombinant enzyme | Corynebacterium crenatum | |
0.0141 | - |
NADH | with FAD, pH 7.5, 30°C, recombinant enzyme | Corynebacterium crenatum |
Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
FAD + NAD(P)H | Corynebacterium crenatum | - |
FADH2 + NAD(P)+ | - |
r | |
FMN + NAD(P)H | Corynebacterium crenatum | - |
FMNH2 + NAD(P)+ | - |
r |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Corynebacterium crenatum | - |
- |
- |
Corynebacterium crenatum SYPA5-5 | - |
- |
- |
Purification (Comment) | Organism |
---|---|
recombinant N-terminally His-tagged enzyme from Escherichia coli strain BL21(DE3) by nickel affinity chromatography | Corynebacterium crenatum |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
FAD + NAD(P)H | - |
Corynebacterium crenatum | FADH2 + NAD(P)+ | - |
r | |
FMN + NAD(P)H | - |
Corynebacterium crenatum | FMNH2 + NAD(P)+ | - |
r | |
FMN + NADH | - |
Corynebacterium crenatum | FMNH2 + NAD+ | - |
r | |
FMN + NADPH | - |
Corynebacterium crenatum | FMNH2 + NADP+ | - |
r | |
additional information | the enzyme is also active with FMN and NADPH, cf. EC 1.5.1.30 | Corynebacterium crenatum | ? | - |
? | |
additional information | the enzyme is also active with FMN and NADPH, cf. EC 1.5.1.30 | Corynebacterium crenatum SYPA5-5 | ? | - |
? |
Synonyms | Comment | Organism |
---|---|---|
Frd188 | - |
Corynebacterium crenatum |
frd2 | - |
Corynebacterium crenatum |
NAD(P)H-dependent H2O2-forming flavin reductase | - |
Corynebacterium crenatum |
Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
---|---|---|---|
30 | - |
assay at | Corynebacterium crenatum |
Turnover Number Minimum [1/s] | Turnover Number Maximum [1/s] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
0.0247 | - |
NADH | with FMN, pH 7.5, 30°C, recombinant enzyme | Corynebacterium crenatum | |
0.0357 | - |
NADH | with FAD, pH 7.5, 30°C, recombinant enzyme | Corynebacterium crenatum |
pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|
7.5 | - |
assay at | Corynebacterium crenatum |
Cofactor | Comment | Organism | Structure |
---|---|---|---|
NAD+ | - |
Corynebacterium crenatum | |
NADH | - |
Corynebacterium crenatum |
kcat/KM Value [1/mMs-1] | kcat/KM Value Maximum [1/mMs-1] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
2.53 | - |
NADH | with FAD, pH 7.5, 30°C, recombinant enzyme | Corynebacterium crenatum | |
2.94 | - |
NADH | with FMN, pH 7.5, 30°C, recombinant enzyme | Corynebacterium crenatum |