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Literature summary extracted from

  • Burlat, B.; Gwyer, J.D.; Poock, S.; Clarke, T.; Cole, J.A.; Hemmings, A.M.; Cheesman, M.R.; Butt, J.N.; Richardson, D.J.
    Cytochrome c nitrite reductase: from structural to physicochemical analysis (2005), Biochem. Soc. Trans., 33, 137-140.
    View publication on PubMed

Activating Compound

EC Number Activating Compound Comment Organism Structure
1.7.2.2 Ca2+
-
Escherichia coli

Inhibitors

EC Number Inhibitors Comment Organism Structure
1.7.2.2 additional information inhibition in the absence of Ca2+ is noted at potentials where heme 4 and/or 5 is reduced, this may implicate Ca2+ association with the propionate of heme 4 as being essential for maintaining steady-state activity from the fully reduced enzyme-substrate complex Escherichia coli

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
1.7.2.2 0.00025
-
nitrite
-
Escherichia coli

Organism

EC Number Organism UniProt Comment Textmining
1.7.2.2 Escherichia coli
-
-
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.7.2.2 hydroxylammonium + ferrocytochrome c
-
Escherichia coli NH3 + ferricytochrome c + H2O
-
?
1.7.2.2 nitric oxide + ferrocytochrome c
-
Escherichia coli NH3 + ferricytochrome c + H2O
-
?
1.7.2.2 nitrite + ferrocytochrome c
-
Escherichia coli NH3 + ferricytochrome c + H2O
-
?

Subunits

EC Number Subunits Comment Organism
1.7.2.2 homodimer
-
Escherichia coli

Synonyms

EC Number Synonyms Comment Organism
1.7.2.2 cytochrome c nitrite reductase
-
Escherichia coli
1.7.2.2 NrfA
-
Escherichia coli

Cofactor

EC Number Cofactor Comment Organism Structure
1.7.2.2 heme
-
Escherichia coli