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Literature summary extracted from

  • Jackson, R.H.; Cole, J.A.; Cornish-Bowden, A.
    The steady-state kinetics of the NADH-dependent nitrite reductase from Escherichia coli K12 (1981), Biochem. J., 199, 171-178.
    View publication on PubMedView publication on EuropePMC

Activating Compound

EC Number Activating Compound Comment Organism Structure
1.7.1.4 NAD+ activation of hydroxylamine reduction at low concentrations Escherichia coli
1.7.1.15 NAD+ the apparent maximum velocity with NADH as varied substrate increases as the NAD+ concentration increases from 0.05 to 0.7 mM with 1 mM nitrite or 100 mM hydroxylamine as oxidized substrate Escherichia coli

Inhibitors

EC Number Inhibitors Comment Organism Structure
1.7.1.4 NAD+ hydroxylamine reduction, substrate inhibition at low concentration, mixed inhibition vs. NADH Escherichia coli
1.7.1.15 NAD+ NAD+ shows mixed product inhibition with respect to NADH and mixed or uncompetitive inhibition with respect to hydroxylamine Escherichia coli

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
1.7.1.15 nitrite + NADH + H+ Escherichia coli
-
 ammonia + NAD+ + H2O
-
 ?

Organism

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

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.7.1.15 hydroxylamine + NADH + H+
-
 Escherichia coli ?
-
 ?
1.7.1.15 nitrite + NADH + H+
-
 Escherichia coli ammonia + NAD+ + H2O
-
 ?

Synonyms

EC Number Synonyms Comment Organism
1.7.1.15 NADH-dependent nitrite reductase
-
 Escherichia coli

Cofactor

EC Number Cofactor Comment Organism Structure
1.7.1.4 NAD+ substrate inhibition at low concentration Escherichia coli
1.7.1.4 NADH
-
 Escherichia coli
1.7.1.15 NADH
-
 Escherichia coli