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Literature summary for 1.7.2.6 extracted from

  • Irisa, T.; Hira, D.; Furukawa, K.; Fujii, T.
    Reduction of nitric oxide catalyzed by hydroxylamine oxidoreductase from an anammox bacterium (2014), J. Biosci. Bioeng., 118, 616-621 .
    View publication on PubMed
Search for more literature for 1.7.2.6

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
additional information
-
 additional information quasi steady-state and steady-state kinetics, kinetic analysis, overview Candidatus Kuenenia stuttgartiensis

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
hydroxylamine + H2O + 4 ferricytochrome c Candidatus Kuenenia stuttgartiensis via NO as intermediate nitrite + 4 ferrocytochrome c + 5 H+
-
 r
hydroxylamine + H2O + 4 ferricytochrome c Candidatus Kuenenia stuttgartiensis KSU-1 via NO as intermediate nitrite + 4 ferrocytochrome c + 5 H+
-
 r

Organism

Organism UniProt Comment Textmining
Candidatus Kuenenia stuttgartiensis
-
-
-
Candidatus Kuenenia stuttgartiensis KSU-1
-
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
hydroxylamine + H2O + 4 ferricytochrome c via NO as intermediate Candidatus Kuenenia stuttgartiensis nitrite + 4 ferrocytochrome c + 5 H+
-
 r
hydroxylamine + H2O + 4 ferricytochrome c via NO as intermediate Candidatus Kuenenia stuttgartiensis KSU-1 nitrite + 4 ferrocytochrome c + 5 H+
-
 r
hydroxylamine + H2O + benzylviologen
-
 Candidatus Kuenenia stuttgartiensis NO + reduced benzylviologen + 2 H+
-
 ?
hydroxylamine + H2O + benzylviologen
-
 Candidatus Kuenenia stuttgartiensis KSU-1 NO + reduced benzylviologen + 2 H+
-
 ?
hydroxylamine + H2O + methylviologen
-
 Candidatus Kuenenia stuttgartiensis NO + reduced methylviologen + 2 H+
-
 ?
hydroxylamine + H2O + methylviologen
-
 Candidatus Kuenenia stuttgartiensis KSU-1 NO + reduced methylviologen + 2 H+
-
 ?
additional information enzyme HAO can catalyze the interconversion of NO and NH2OH. The enzyme catalyzes a three-electron oxidation of NH2OH to NO using bovine cytochrome c as an oxidant. Strain KSU-1 catalyzes the reduction of NO with reduced benzyl viologen (BVred) and the NO-releasing reagent hydroxy-2-oxo-3-(N-methyl-3-amino-propyl)-3-methyl-1-triazene, i.e. NOC 7. Substrate specificity of strain KSU-1 enzyme HAO, overview Candidatus Kuenenia stuttgartiensis ?
-
 ?
additional information enzyme HAO can catalyze the interconversion of NO and NH2OH. The enzyme catalyzes a three-electron oxidation of NH2OH to NO using bovine cytochrome c as an oxidant. Strain KSU-1 catalyzes the reduction of NO with reduced benzyl viologen (BVred) and the NO-releasing reagent hydroxy-2-oxo-3-(N-methyl-3-amino-propyl)-3-methyl-1-triazene, i.e. NOC 7. Substrate specificity of strain KSU-1 enzyme HAO, overview Candidatus Kuenenia stuttgartiensis KSU-1 ?
-
 ?
NO + ferrocytochrome c + 2 H+
-
 Candidatus Kuenenia stuttgartiensis hydroxylamine + H2O + ferricytochrome c
-
 r
NO + ferrocytochrome c + 2 H+
-
 Candidatus Kuenenia stuttgartiensis KSU-1 hydroxylamine + H2O + ferricytochrome c
-
 r
NO + H2O + ferricytochrome c
-
 Candidatus Kuenenia stuttgartiensis nitrite + ferrocytochrome c + 2 H+
-
 r

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
35
-
 assay at Candidatus Kuenenia stuttgartiensis

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7
-
 assay at Candidatus Kuenenia stuttgartiensis

Cofactor

Cofactor Comment Organism Structure
cytochrome c
-
 Candidatus Kuenenia stuttgartiensis

General Information

General Information Comment Organism
physiological function the anammox HAO can catalyze the interconversion of NO and NH2OH. The anammox HAO functions to adjust anammox by inter-conversion of NO and NH2OH depending on the redox potential of the physiological electron transfer protein in anammox bacteria Candidatus Kuenenia stuttgartiensis