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Literature summary for 1.7.2.9 extracted from

  • Maalcke, W.; Dietl, A.; Marritt, S.; Butt, J.; Jetten, M.; Keltjens, J.; Barends, T.; Kartal, B.
    Structural basis of biological no generation by octaheme oxidoreductases (2014), J. Biol. Chem., 289, 1228-1242 .
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

Cloned (Comment) Organism
-
Candidatus Kuenenia stuttgartiensis

Crystallization (Commentary)

Crystallization (Comment) Organism
structure at 1.8 A resolution, structure is very similar to EC 1.7.2.6, hydroxylamine dehydrogenase with differences in their N- and C-terminal parts Candidatus Kuenenia stuttgartiensis

Inhibitors

Inhibitors Comment Organism Structure
additional information not inhibitory: NO up to 0.08 mM Candidatus Kuenenia stuttgartiensis

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.0044
-
hydroxylamine 37┬░C, pH not specified in the publication Candidatus Kuenenia stuttgartiensis
0.054
-
hydrazine 37┬░C, pH not specified in the publication Candidatus Kuenenia stuttgartiensis

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
184200
-
sedimentation equilibrium ultracentrifugation Candidatus Kuenenia stuttgartiensis

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
hydrazine + ferricytochrome c Candidatus Kuenenia stuttgartiensis
-
? + ferrocytochrome c + H+
-
?
hydroxylamine + 3 ferricytochrome c Candidatus Kuenenia stuttgartiensis
-
nitric oxide + 3 ferrocytochrome c + 3 H+
-
?
additional information Candidatus Kuenenia stuttgartiensis enzyme does not catalyze any hydroxylamine disproportionation to ammonium and NO, nitrite, N2O, or N2 ?
-
-

Organism

Organism UniProt Comment Textmining
Candidatus Kuenenia stuttgartiensis Q1PX48
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
hydrazine + ferricytochrome c
-
Candidatus Kuenenia stuttgartiensis ? + ferrocytochrome c + H+
-
?
hydroxylamine + 3 ferricytochrome c
-
Candidatus Kuenenia stuttgartiensis nitric oxide + 3 ferrocytochrome c + 3 H+
-
?
additional information enzyme does not catalyze any hydroxylamine disproportionation to ammonium and NO, nitrite, N2O, or N2 Candidatus Kuenenia stuttgartiensis ?
-
-
nitrite + reduced methyl viologen
-
Candidatus Kuenenia stuttgartiensis NO + oxidized methyl viologen
-
?

Subunits

Subunits Comment Organism
More the subunits are linked by two covalent bonds between Tyr451 of one subunit and heme 4 of an adjacent subunit. Heme 4 is ligated by a single amino acid (His227) Candidatus Kuenenia stuttgartiensis
trimer 3 * 61500, calculated from sequence Candidatus Kuenenia stuttgartiensis

Synonyms

Synonyms Comment Organism
HAO
-
Candidatus Kuenenia stuttgartiensis
hydroxylamine oxidoreductase
-
Candidatus Kuenenia stuttgartiensis
kustc1061
-
Candidatus Kuenenia stuttgartiensis
NO-producing hydroxylamine oxidase
-
Candidatus Kuenenia stuttgartiensis

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
4.9
-
hydrazine 37┬░C, pH not specified in the publication Candidatus Kuenenia stuttgartiensis
15
-
hydroxylamine 37┬░C, pH not specified in the publication Candidatus Kuenenia stuttgartiensis

Cofactor

Cofactor Comment Organism Structure
heme protein harbors 24 heme c molecules in total, with low spin ferric c-heme. The P460 chromophore heme displays an Em' of 300 mV Candidatus Kuenenia stuttgartiensis

kcat/KM [mM/s]

kcat/KM Value [1/mMs-1] kcat/KM Value Maximum [1/mMs-1] Substrate Comment Organism Structure
100
-
hydrazine 37┬░C, pH not specified in the publication Candidatus Kuenenia stuttgartiensis
3400
-
hydroxylamine 37┬░C, pH not specified in the publication Candidatus Kuenenia stuttgartiensis