EC Number | Cloned (Comment) | Organism |
---|---|---|
1.19.1.1 | expression in Escherichia coli | Escherichia coli |
EC Number | KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|---|
1.19.1.1 | 0.0039 | - |
NADPH | pH 7.5, 30°C | Escherichia coli | |
1.19.1.1 | 0.0068 | - |
reduced flavodoxin | pH 7.5, 30°C | Escherichia coli | |
1.19.1.1 | 0.0176 | - |
ferricytochrome c2 | pH 7.5, 30°C | Escherichia coli | |
1.19.1.1 | 0.0236 | - |
ferricyanide | pH 7.5, 30°C | Escherichia coli |
EC Number | Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
---|---|---|---|---|
1.19.1.1 | 27648 | - |
- |
Escherichia coli |
EC Number | Organism | UniProt | Comment | Textmining |
---|---|---|---|---|
1.19.1.1 | Escherichia coli | - |
- |
- |
1.19.1.1 | Escherichia coli HMS174 | - |
- |
- |
EC Number | Purification (Comment) | Organism |
---|---|---|
1.19.1.1 | recpmbinant protein. FLDR is bright yellow in its oxidized form and it is converted to a neutral blue semiquinone by the addition of one reducing equivalent | Escherichia coli |
EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
1.19.1.1 | 2 ferricyanide + NADPH | - |
Escherichia coli | 2 ferrocyanide + NADP+ + H+ | - |
? | |
1.19.1.1 | 2 ferricyanide + NADPH | - |
Escherichia coli HMS174 | 2 ferrocyanide + NADP+ + H+ | - |
? | |
1.19.1.1 | 2 ferricytochrome c2 + NADPH | - |
Escherichia coli | 2 ferrocytochrome c2 + NADP+ + H+ | - |
? | |
1.19.1.1 | 2 ferricytochrome c2 + NADPH | - |
Escherichia coli HMS174 | 2 ferrocytochrome c2 + NADP+ + H+ | - |
? | |
1.19.1.1 | additional information | the electron-transfer route is NADPH to FLDR to flavodoxin. The midpoint reduction potentials of the oxidized/semiquinone and semiquinone/hydroquinone couples of FLDR are 2308 mV and 2268 mV, respectively. Binding of 2'-adenosine monophosphate increases the midpoint reduction potentials for both FLDR couples | Escherichia coli | ? | - |
? | |
1.19.1.1 | additional information | the electron-transfer route is NADPH to FLDR to flavodoxin. The midpoint reduction potentials of the oxidized/semiquinone and semiquinone/hydroquinone couples of FLDR are 2308 mV and 2268 mV, respectively. Binding of 2'-adenosine monophosphate increases the midpoint reduction potentials for both FLDR couples | Escherichia coli HMS174 | ? | - |
? | |
1.19.1.1 | reduced flavodoxin + NADP+ | - |
Escherichia coli | oxidized flavodoxin + NADPH + H+ | - |
? | |
1.19.1.1 | reduced flavodoxin + NADP+ | - |
Escherichia coli HMS174 | oxidized flavodoxin + NADPH + H+ | - |
? |
EC Number | Subunits | Comment | Organism |
---|---|---|---|
1.19.1.1 | monomer | 1 * 27620, calculated, 1 * 27 648, electrospray mass spectroscopy | Escherichia coli |
EC Number | Synonyms | Comment | Organism |
---|---|---|---|
1.19.1.1 | FLDR | - |
Escherichia coli |
EC Number | Turnover Number Minimum [1/s] | Turnover Number Maximum [1/s] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|---|
1.19.1.1 | 2.35 | - |
ferricytochrome c2 | pH 7.5, 30°C | Escherichia coli | |
1.19.1.1 | 26.8 | - |
ferricyanide | pH 7.5, 30°C | Escherichia coli |
EC Number | Cofactor | Comment | Organism | Structure |
---|---|---|---|---|
1.19.1.1 | FAD | oxidized FLDR has flavin absorbance maxima at 456 nm and 400 nm, with a shoulder on the longer wavelength band at 483 nm | Escherichia coli |
EC Number | Organism | Comment | pI Value Maximum | pI Value |
---|---|---|---|---|
1.19.1.1 | Escherichia coli | isoelectric focusing | - |
4.8 |
1.19.1.1 | Escherichia coli | calculated | - |
6.2 |