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Literature summary for 1.7.2.6 extracted from

  • Haase, D.; Hermann, B.; Einsle, O.; Simon, J.
    Epsilonproteobacterial hydroxylamine oxidoreductase (epsilonHao) characterization of a missing link in the multihaem cytochrome c family (2017), Mol. Microbiol., 105, 127-138 .
    View publication on PubMed

Cloned(Commentary)

Cloned (Comment) Organism
expressed in Wolinella succinogenes as enzyme-maltose binding protein fusion Campylobacter fetus
expressed in Wolinella succinogenes as enzyme-maltose binding protein fusion Caminibacter mediatlanticus
expressed in Wolinella succinogenes as enzyme-maltose binding protein fusion Nautilia profundicola
expressed in Wolinella succinogenes as enzyme-maltose binding protein fusion Campylobacter curvus
expression in Wolinella succinogenes as maltose binding protein fusion Campylobacter fetus
expression in Wolinella succinogenes as maltose binding protein fusion Caminibacter mediatlanticus
expression in Wolinella succinogenes as maltose binding protein fusion Nautilia profundicola
expression in Wolinella succinogenes as maltose binding protein fusion Campylobacter curvus

Protein Variants

Protein Variants Comment Organism
W428Y mutant contains a tyrosine residue at the position corresponding to that in Nitrosomonas europaea Hao, where it is described to crosslink the monomers of the Hao trimer. Hydoxylamine reductase activity is similar to wild-type, nitrite reductase activity decreases considerably Campylobacter curvus
W428Y the mutant produces a higher amount of nitrite from hydroxylamine oxidation than the corresponding wild type enzyme Campylobacter curvus
W434Y mutant contains a tyrosine residue at the position corresponding to that in Nitrosomonas europaea Hao, where it is described to crosslink the monomers of the Hao trimer. Hydoxylamine reductase activity is similar to wild-type, nitrite reductase activity decreases considerably Campylobacter fetus
W464Y mutant contains a tyrosine residue at the position corresponding to that in Nitrosomonas europaea Hao, where it is described to crosslink the monomers of the Hao trimer. Hydoxylamine reductase activity is similar to wild-type, nitrite reductase activity increases 3fold Caminibacter mediatlanticus
W464Y the mutant produces a higher amount of nitrite from hydroxylamine oxidation than the corresponding wild type enzyme Caminibacter mediatlanticus

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.89
-
nitrite wild-type, pH 7.0, 37°C Campylobacter fetus
1.5
-
nitrite wild-type, pH 7.0, 37°C Caminibacter mediatlanticus
1.9
-
hydroxylamine wild-type, pH 7.0, 37°C Campylobacter fetus
2.39
-
nitrite mutant W434Y, pH 7.0, 37°C Campylobacter fetus
2.7
-
nitrite wild-type, pH 7.0, 37°C Campylobacter curvus
2.99
-
nitrite mutant W428Y, pH 7.0, 37°C Campylobacter curvus
4.6
-
nitrite mutant W464Y, pH 7.0, 37°C Caminibacter mediatlanticus
6
-
hydroxylamine wild-type, pH 7.0, 37°C Caminibacter mediatlanticus
6.6
-
hydroxylamine wild-type, pH 7.0, 37°C Campylobacter curvus
6.75
-
hydroxylamine mutant W428Y, pH 7.0, 37°C Campylobacter curvus
7.4
-
hydroxylamine mutant W434Y, pH 7.0, 37°C Campylobacter fetus
16.9
-
hydroxylamine mutant W464Y, pH 7.0, 37°C Caminibacter mediatlanticus

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
hydroxylamine + H2O + 4 ferricytochrome c Campylobacter fetus
-
nitrite + 4 ferrocytochrome c + 5 H+
-
?
hydroxylamine + H2O + 4 ferricytochrome c Caminibacter mediatlanticus
-
nitrite + 4 ferrocytochrome c + 5 H+
-
?
hydroxylamine + H2O + 4 ferricytochrome c Nautilia profundicola
-
nitrite + 4 ferrocytochrome c + 5 H+
-
?
hydroxylamine + H2O + 4 ferricytochrome c Campylobacter curvus
-
nitrite + 4 ferrocytochrome c + 5 H+
-
?

Organism

Organism UniProt Comment Textmining
Caminibacter mediatlanticus
-
-
-
Campylobacter curvus
-
-
-
Campylobacter fetus
-
-
-
Nautilia profundicola
-
-
-

Purification (Commentary)

Purification (Comment) Organism
maltose binding protein Trap column chromatography Campylobacter fetus
maltose binding protein Trap column chromatography Caminibacter mediatlanticus
maltose binding protein Trap column chromatography Nautilia profundicola
maltose binding protein Trap column chromatography Campylobacter curvus

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
1
-
nitrite reduction, pH 7.0, 37°C Caminibacter mediatlanticus
1.2
-
nitrite reduction, pH 7.0, 37°C Nautilia profundicola
27
-
nitrite reduction, pH 7.0, 37°C Campylobacter curvus
29
-
hydroxylamine reduction, pH 7.0, 37°C Nautilia profundicola
68
-
hydroxylamine reduction, pH 7.0, 37°C Campylobacter curvus
149
-
hydroxylamine reduction, pH 7.0, 37°C Campylobacter fetus
158
-
hydroxylamine reduction, pH 7.0, 37°C Caminibacter mediatlanticus
181
-
nitrite reduction, pH 7.0, 37°C Campylobacter fetus

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
hydroxylamine + 3-(4,5-dimethyl-2-thiazolyl)-2,5-diphenyl-2H-tetrazolium bromide
-
Campylobacter fetus nitrite + reduced 3-(4,5-dimethyl-2-thiazolyl)-2,5-diphenyl-2H-tetrazolium bromide
-
?
hydroxylamine + 3-(4,5-dimethyl-2-thiazolyl)-2,5-diphenyl-2H-tetrazolium bromide
-
Caminibacter mediatlanticus nitrite + reduced 3-(4,5-dimethyl-2-thiazolyl)-2,5-diphenyl-2H-tetrazolium bromide
-
?
hydroxylamine + 3-(4,5-dimethyl-2-thiazolyl)-2,5-diphenyl-2H-tetrazolium bromide
-
Nautilia profundicola nitrite + reduced 3-(4,5-dimethyl-2-thiazolyl)-2,5-diphenyl-2H-tetrazolium bromide
-
?
hydroxylamine + 3-(4,5-dimethyl-2-thiazolyl)-2,5-diphenyl-2H-tetrazolium bromide
-
Campylobacter curvus nitrite + reduced 3-(4,5-dimethyl-2-thiazolyl)-2,5-diphenyl-2H-tetrazolium bromide
-
?
hydroxylamine + 3-(4,5-dimethyl-2-thiazolyl)-2,5-diphenyl-2H-tetrazolium bromide + H2O
-
Campylobacter fetus NH3 + oxidized 3-(4,5-dimethyl-2-thiazolyl)-2,5-diphenyl-2H-tetrazolium bromide
-
?
hydroxylamine + 3-(4,5-dimethyl-2-thiazolyl)-2,5-diphenyl-2H-tetrazolium bromide + H2O
-
Caminibacter mediatlanticus NH3 + oxidized 3-(4,5-dimethyl-2-thiazolyl)-2,5-diphenyl-2H-tetrazolium bromide
-
?
hydroxylamine + 3-(4,5-dimethyl-2-thiazolyl)-2,5-diphenyl-2H-tetrazolium bromide + H2O
-
Nautilia profundicola NH3 + oxidized 3-(4,5-dimethyl-2-thiazolyl)-2,5-diphenyl-2H-tetrazolium bromide
-
?
hydroxylamine + 3-(4,5-dimethyl-2-thiazolyl)-2,5-diphenyl-2H-tetrazolium bromide + H2O
-
Campylobacter curvus NH3 + oxidized 3-(4,5-dimethyl-2-thiazolyl)-2,5-diphenyl-2H-tetrazolium bromide
-
?
hydroxylamine + H2O + 4 ferricytochrome c
-
Campylobacter fetus nitrite + 4 ferrocytochrome c + 5 H+
-
?
hydroxylamine + H2O + 4 ferricytochrome c
-
Caminibacter mediatlanticus nitrite + 4 ferrocytochrome c + 5 H+
-
?
hydroxylamine + H2O + 4 ferricytochrome c
-
Nautilia profundicola nitrite + 4 ferrocytochrome c + 5 H+
-
?
hydroxylamine + H2O + 4 ferricytochrome c
-
Campylobacter curvus nitrite + 4 ferrocytochrome c + 5 H+
-
?
hydroxylamine + phenazine methosulfate + H2O
-
Campylobacter fetus NH3 + oxidized phenazine methosulfate
-
?
hydroxylamine + phenazine methosulfate + H2O
-
Caminibacter mediatlanticus NH3 + oxidized phenazine methosulfate
-
?
hydroxylamine + phenazine methosulfate + H2O
-
Nautilia profundicola NH3 + oxidized phenazine methosulfate
-
?
hydroxylamine + phenazine methosulfate + H2O
-
Campylobacter curvus NH3 + oxidized phenazine methosulfate
-
?
additional information hydroxylamine oxidation is negligible Campylobacter fetus ?
-
?
additional information hydroxylamine oxidation is negligible Caminibacter mediatlanticus ?
-
?
additional information hydroxylamine oxidation is negligible Nautilia profundicola ?
-
?
additional information hydroxylamine oxidation is negligible Campylobacter curvus ?
-
?
nitrite + reduced benzyl viologen + H+
-
Campylobacter fetus NH4+ + reduced methyl viologen + H2O
-
?
nitrite + reduced benzyl viologen + H+
-
Caminibacter mediatlanticus NH4+ + reduced methyl viologen + H2O
-
?
nitrite + reduced benzyl viologen + H+
-
Nautilia profundicola NH4+ + reduced methyl viologen + H2O
-
?
nitrite + reduced benzyl viologen + H+
-
Campylobacter curvus NH4+ + reduced methyl viologen + H2O
-
?

Subunits

Subunits Comment Organism
? x * about 80000, SDS-PAGE Campylobacter fetus
? x * about 80000, SDS-PAGE Caminibacter mediatlanticus
? x * about 80000, SDS-PAGE Nautilia profundicola
? x * about 80000, SDS-PAGE Campylobacter curvus

Synonyms

Synonyms Comment Organism
HAO
-
Campylobacter fetus
HAO
-
Caminibacter mediatlanticus
HAO
-
Nautilia profundicola
HAO
-
Campylobacter curvus
haoA
-
Campylobacter fetus
haoA
-
Caminibacter mediatlanticus
haoA
-
Nautilia profundicola
haoA
-
Campylobacter curvus
hydroxylamine oxidoreductase
-
Campylobacter fetus
hydroxylamine oxidoreductase
-
Caminibacter mediatlanticus
hydroxylamine oxidoreductase
-
Nautilia profundicola
hydroxylamine oxidoreductase
-
Campylobacter curvus

Cofactor

Cofactor Comment Organism Structure
cytochrome c
-
Campylobacter fetus
cytochrome c
-
Caminibacter mediatlanticus
cytochrome c
-
Nautilia profundicola
cytochrome c
-
Campylobacter curvus
heme
-
Campylobacter fetus
heme
-
Caminibacter mediatlanticus
heme
-
Nautilia profundicola
heme
-
Campylobacter curvus