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Literature summary extracted from

  • Coleman, K.J.; Cornish-Bowden, A.; Cole, J.A.
    Activation of nitrite reductase from Escherichia coli K12 by oxidized nicotinamide-adenine dinucleotide (1978), Biochem. J., 175, 495-499.
    View publication on PubMedView publication on EuropePMC

Activating Compound

EC Number Activating Compound Comment Organism Structure
1.7.1.4 NAD+ enzyme from crude extracts and purified enzyme requires NAD+ for full activity, maximal activation at 1 mM Escherichia coli

Inhibitors

EC Number Inhibitors Comment Organism Structure
1.7.1.4 NAD+ substrate inhibition at high concentration, required for full activity at low concentrations, maximum at 1 mM Escherichia coli

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
1.7.1.4 0.005
-
NO2-
-
Escherichia coli
1.7.1.4 0.016
-
NADH in presence of 1 mM NAD+ and 2 mM NO2- Escherichia coli
1.7.1.4 5.3
-
hydroxylamine
-
Escherichia coli

Organism

EC Number Organism UniProt Comment Textmining
1.7.1.4 Escherichia coli
-
K12
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.7.1.4 NAD(P)H + NH2OH
-
Escherichia coli NAD(P)+ + NH3 + H2O
-
?
1.7.1.4 NAD(P)H + nitrite + H+
-
Escherichia coli NAD(P)+ + NH3 + H2O
-
?
1.7.1.4 nitrite + NADH + H+
-
Escherichia coli NH3 + NAD+ + H2O
-
r

Cofactor

EC Number Cofactor Comment Organism Structure
1.7.1.4 NAD+ substrate inhibition at high concentration, at low concentration required for full activity, maximum at 1 mM Escherichia coli
1.7.1.4 NADH
-
Escherichia coli