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Literature summary extracted from

  • McIver, L.; Leadbeater, C.; Campopiano, D.J.; Baxter, R.L.; Daff, S.N.; Chapman, S.K.; Munro, A.W.
    Characterisation of flavodoxin NADP+ oxidoreductase and flavodoxin; key components of electron transfer in Escherichia coli (1998), Eur. J. Biochem., 257, 577-585.
    View publication on PubMed

Cloned(Commentary)

EC Number Cloned (Comment) Organism
1.19.1.1 expression in Escherichia coli Escherichia coli

KM Value [mM]

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

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
1.19.1.1 27648
-
-
 Escherichia coli

Organism

EC Number Organism UniProt Comment Textmining
1.19.1.1 Escherichia coli
-
-
-
1.19.1.1 Escherichia coli HMS174
-
-
-

Purification (Commentary)

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

Substrates and Products (Substrate)

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+
-
 ?

Subunits

EC Number Subunits Comment Organism
1.19.1.1 monomer 1 * 27620, calculated, 1 * 27 648, electrospray mass spectroscopy Escherichia coli

Synonyms

EC Number Synonyms Comment Organism
1.19.1.1 FLDR
-
 Escherichia coli

Turnover Number [1/s]

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

Cofactor

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

pI Value

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