Protein Variants | Comment | Organism |
---|---|---|
E268A | inactive | Corynebacterium ammoniagenes |
E268D | the mutant shows strongly reduced catalytic efficiency compared to the wild type enzyme | Corynebacterium ammoniagenes |
N210A | inactive | Corynebacterium ammoniagenes |
N210D | the mutant shows strongly reduced catalytic efficiency compared to the wild type enzyme | Corynebacterium ammoniagenes |
T208A | inactive | Corynebacterium ammoniagenes |
T208D | inactive | Corynebacterium ammoniagenes |
KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
0.0021 | - |
riboflavin | apparent value, mutant enzyme N210D, at 37°C in 20 mM PIPES pH 7.0, 0.8 mM MgCl2 | Corynebacterium ammoniagenes | |
0.0041 | - |
riboflavin | apparent value, mutant enzyme E268D, at 37°C in 20 mM PIPES pH 7.0, 0.8 mM MgCl2 | Corynebacterium ammoniagenes | |
0.013 | - |
riboflavin | apparent value, wild type enzyme, at 37°C in 20 mM PIPES pH 7.0, 0.8 mM MgCl2 | Corynebacterium ammoniagenes | |
0.0137 | - |
ATP | apparent value, wild type enzyme, at 37°C in 20 mM PIPES pH 7.0, 0.8 mM MgCl2 | Corynebacterium ammoniagenes | |
0.0176 | - |
ATP | apparent value, mutant enzyme E268D, at 37°C in 20 mM PIPES pH 7.0, 0.8 mM MgCl2 | Corynebacterium ammoniagenes | |
0.0453 | - |
ATP | apparent value, mutant enzyme N210D, at 37°C in 20 mM PIPES pH 7.0, 0.8 mM MgCl2 | Corynebacterium ammoniagenes |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Corynebacterium ammoniagenes | - |
- |
- |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
ATP + riboflavin | - |
Corynebacterium ammoniagenes | ADP + FMN | - |
? |
Synonyms | Comment | Organism |
---|---|---|
ATP: riboflavin kinase | - |
Corynebacterium ammoniagenes |
RFK | - |
Corynebacterium ammoniagenes |
riboflavin kinase/FMN adenylyltransferase | FADS, bifunctional enzyme, the C-terminus exhibits ATP: riboflavin kinase activity | Corynebacterium ammoniagenes |
Turnover Number Minimum [1/s] | Turnover Number Maximum [1/s] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
0.042 | - |
ATP | apparent value, mutant enzyme N210D, at 37°C in 20 mM PIPES pH 7.0, 0.8 mM MgCl2 | Corynebacterium ammoniagenes | |
0.045 | - |
riboflavin | apparent value, mutant enzyme E268D, at 37°C in 20 mM PIPES pH 7.0, 0.8 mM MgCl2 | Corynebacterium ammoniagenes | |
0.07 | - |
ATP | apparent value, mutant enzyme E268D, at 37°C in 20 mM PIPES pH 7.0, 0.8 mM MgCl2 | Corynebacterium ammoniagenes | |
0.085 | - |
riboflavin | apparent value, mutant enzyme N210D, at 37°C in 20 mM PIPES pH 7.0, 0.8 mM MgCl2 | Corynebacterium ammoniagenes | |
1.13 | - |
ATP | apparent value, wild type enzyme, at 37°C in 20 mM PIPES pH 7.0, 0.8 mM MgCl2 | Corynebacterium ammoniagenes | |
5 | - |
riboflavin | apparent value, wild type enzyme, at 37°C in 20 mM PIPES pH 7.0, 0.8 mM MgCl2 | Corynebacterium ammoniagenes |
kcat/KM Value [1/mMs-1] | kcat/KM Value Maximum [1/mMs-1] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
0.83 | - |
ATP | apparent value, mutant enzyme N210D, at 37°C in 20 mM PIPES pH 7.0, 0.8 mM MgCl2 | Corynebacterium ammoniagenes | |
3.83 | - |
ATP | apparent value, mutant enzyme E268D, at 37°C in 20 mM PIPES pH 7.0, 0.8 mM MgCl2 | Corynebacterium ammoniagenes | |
10.83 | - |
riboflavin | apparent value, mutant enzyme E268D, at 37°C in 20 mM PIPES pH 7.0, 0.8 mM MgCl2 | Corynebacterium ammoniagenes | |
40.3 | - |
riboflavin | apparent value, mutant enzyme N210D, at 37°C in 20 mM PIPES pH 7.0, 0.8 mM MgCl2 | Corynebacterium ammoniagenes | |
82.17 | - |
ATP | apparent value, wild type enzyme, at 37°C in 20 mM PIPES pH 7.0, 0.8 mM MgCl2 | Corynebacterium ammoniagenes | |
386 | - |
riboflavin | apparent value, wild type enzyme, at 37°C in 20 mM PIPES pH 7.0, 0.8 mM MgCl2 | Corynebacterium ammoniagenes |