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Literature summary for 1.7.2.2 extracted from
- Epsilonproteobacterial hydroxylamine oxidoreductase (epsilonHao) characterization of a missing link in the multihaem cytochrome c family (2017), Mol. Microbiol., 105, 127-138 .
Cloned(Commentary)
| Cloned (Comment) | Organism |
|---|---|
| gene haoA, recombinant expression in Wolinella succinogenes strain DSM 1740 as maltose-binding-protein fusion His6-tagged enzyme | Nautilia profundicola |
| gene haoA, recombinant expression of wild-type and mutant enzymes in Wolinella succinogenes strain DSM 1740 as maltose-binding-protein fusion His6-tagged enzyme | Caminibacter mediatlanticus |
| gene haoA, recombinant expression of wild-type and mutant enzymes in Wolinella succinogenes strain DSM 1740 as maltose-binding-protein fusion His6-tagged enzyme | Campylobacter fetus subsp. fetus |
| gene haoA, recombinant expression of wild-type and mutant enzymes in Wolinella succinogenes strain DSM 1740 as maltose-binding-protein fusion His6-tagged enzyme | Campylobacter curvus |
Protein Variants
| Protein Variants | Comment | Organism |
|---|---|---|
| additional information | introduction of a tyrosine residue at a position known to cause covalent trimerization of Hao proteins does neither stimulate hydroxylamine oxidation nor generate the Hao-typical absorbance maximum at 460 nm | Caminibacter mediatlanticus |
| additional information | introduction of a tyrosine residue at a position known to cause covalent trimerization of Hao proteins does neither stimulate hydroxylamine oxidation nor generate the Hao-typical absorbance maximum at 460 nm | Campylobacter fetus subsp. fetus |
| additional information | introduction of a tyrosine residue at a position known to cause covalent trimerization of Hao proteins does neither stimulate hydroxylamine oxidation nor generate the Hao-typical absorbance maximum at 460 nm | Campylobacter curvus |
| W434Y | site-directed mutagenesis, the mutant shows unaltered hydroxylamine oxidation activity, but decreased hydroxylamine reduction and increased nitrite reduction compared to the wild-type enzyme | Caminibacter mediatlanticus |
| W434Y | site-directed mutagenesis, the mutant shows unaltered hydroxylamine oxidation activity, but highly increased hydroxylamine reduction and highly reduced nitrite reduction compared to the wild-type enzyme | Campylobacter fetus subsp. fetus |
| W434Y | site-directed mutagenesis, the mutant shows unaltered hydroxylamine oxidation, but slightly reduced hydroxylamine reduction and significantly reduced nitrite reduction compared to the wild-type enzyme | Campylobacter curvus |
KM Value [mM]
| KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|
| 0.89 | - |
nitrite | recombinant MBP-tagged wild-type enzyme, pH 7.0, 37°C | Campylobacter fetus subsp. fetus |  |
| 1 | - |
hydroxylamine | oxidation reaction, recombinant MBP-tagged wild-type enzyme, pH 7.0, 37°C | Campylobacter fetus subsp. fetus | |
| 1.4 | - |
hydroxylamine | oxidation reaction, recombinant MBP-tagged wild-type enzyme, pH 7.0, 37°C | Caminibacter mediatlanticus | |
| 1.5 | - |
hydroxylamine | oxidation reaction, recombinant MBP-tagged wild-type enzyme, pH 7.0, 37°C | Campylobacter curvus | |
| 1.5 | - |
nitrite | recombinant MBP-tagged wild-type enzyme, pH 7.0, 37°C | Caminibacter mediatlanticus | |
| 1.9 | - |
hydroxylamine | reduction reaction, recombinant MBP-tagged wild-type enzyme, pH 7.0, 37°C | Campylobacter fetus subsp. fetus | |
| 2.39 | - |
nitrite | recombinant MBP-tagged mutant W434Y, pH 7.0, 37°C | Campylobacter fetus subsp. fetus | |
| 2.7 | - |
nitrite | recombinant MBP-tagged wild-type enzyme, pH 7.0, 37°C | Campylobacter curvus | |
| 2.99 | - |
nitrite | recombinant MBP-tagged mutant W434Y, pH 7.0, 37°C | Campylobacter curvus | |
| 4.7 | - |
nitrite | recombinant MBP-tagged mutant W434Y, pH 7.0, 37°C | Caminibacter mediatlanticus | |
| 5.3 | - |
hydroxylamine | oxidation reaction, recombinant MBP-tagged mutant W434Y, pH 7.0, 37°C | Campylobacter curvus | |
| 6 | - |
hydroxylamine | reduction reaction, recombinant MBP-tagged wild-type enzyme, pH 7.0, 37°C | Caminibacter mediatlanticus | |
| 6.6 | - |
hydroxylamine | reduction reaction, recombinant MBP-tagged wild-type enzyme, pH 7.0, 37°C | Campylobacter curvus | |
| 6.75 | - |
hydroxylamine | reduction reaction, recombinant MBP-tagged mutant W434Y, pH 7.0, 37°C | Campylobacter curvus | |
| 7.4 | - |
hydroxylamine | reduction reaction, recombinant MBP-tagged mutant W434Y, pH 7.0, 37°C | Campylobacter fetus subsp. fetus | |
| 16.9 | - |
hydroxylamine | reduction reaction, recombinant MBP-tagged mutant W434Y, pH 7.0, 37°C | Caminibacter mediatlanticus | |
Metals/Ions
| Metals/Ions | Comment | Organism | Structure |
|---|---|---|---|
| Fe2+ | heme | Caminibacter mediatlanticus | |
| Fe2+ | heme | Nautilia profundicola | |
| Fe2+ | heme | Campylobacter fetus subsp. fetus | |
| Fe2+ | heme | Campylobacter curvus | |
Natural Substrates/ Products (Substrates)
| Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| hydroxylamine + ferricytochrome c | Caminibacter mediatlanticus | - |
nitrite + ferrocytochrome c | - |
r | |
| hydroxylamine + ferricytochrome c | Nautilia profundicola | - |
nitrite + ferrocytochrome c | - |
r | |
| hydroxylamine + ferricytochrome c | Campylobacter fetus subsp. fetus | - |
nitrite + ferrocytochrome c | - |
r | |
| hydroxylamine + ferricytochrome c | Campylobacter curvus | - |
nitrite + ferrocytochrome c | - |
r | |
| hydroxylamine + ferrocytochrome c | Caminibacter mediatlanticus | cf. EC 1.7.99.1 | NH3 + H2O + ferricytochrome c | - |
r | |
| hydroxylamine + ferrocytochrome c | Nautilia profundicola | cf. EC 1.7.99.1 | NH3 + H2O + ferricytochrome c | - |
r | |
| hydroxylamine + ferrocytochrome c | Campylobacter fetus subsp. fetus | cf. EC 1.7.99.1 | NH3 + H2O + ferricytochrome c | - |
r | |
| hydroxylamine + ferrocytochrome c | Campylobacter curvus | cf. EC 1.7.99.1 | NH3 + H2O + ferricytochrome c | - |
r | |
| additional information | Caminibacter mediatlanticus | the recombinant enzyme is able to catalyze reduction of nitrite (yielding ammonium) and hydroxylamine, EC 1.7.99.1, whereas hydroxylamine oxidation is negligible | ? | - |
? | |
| additional information | Nautilia profundicola | the recombinant enzyme is able to catalyze reduction of nitrite (yielding ammonium) and hydroxylamine, EC 1.7.99.1, whereas hydroxylamine oxidation is negligible | ? | - |
? | |
| additional information | Campylobacter fetus subsp. fetus | the recombinant enzyme is able to catalyze reduction of nitrite (yielding ammonium) and hydroxylamine, EC 1.7.99.1, whereas hydroxylamine oxidation is negligible | ? | - |
? | |
| additional information | Campylobacter curvus | the recombinant enzyme is able to catalyze reduction of nitrite (yielding ammonium) and hydroxylamine, EC 1.7.99.1, whereas hydroxylamine oxidation is negligible | ? | - |
? | |
| nitrite + 6 ferrocytochrome c + 7 H+ | Caminibacter mediatlanticus | - |
NH3 + 2 H2O + 6 ferricytochrome c | - |
? | |
| nitrite + 6 ferrocytochrome c + 7 H+ | Nautilia profundicola | - |
NH3 + 2 H2O + 6 ferricytochrome c | - |
? | |
| nitrite + 6 ferrocytochrome c + 7 H+ | Campylobacter fetus subsp. fetus | - |
NH3 + 2 H2O + 6 ferricytochrome c | - |
? | |
| nitrite + 6 ferrocytochrome c + 7 H+ | Campylobacter curvus | - |
NH3 + 2 H2O + 6 ferricytochrome c | - |
? | |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Caminibacter mediatlanticus | - |
- |
- |
| Campylobacter curvus | A7GXH2 | - |
- |
| Campylobacter fetus subsp. fetus | - |
- |
- |
| Nautilia profundicola | - |
- |
- |
Purification (Commentary)
| Purification (Comment) | Organism |
|---|---|
| recombinant MBP-tagged enzyme from Wolinella succinogenes strain DSM 1740 by affinity chromatography, cleavage of the MBP-tag by TEV protease | Nautilia profundicola |
| recombinant wild-type and mutant MBP-tagged enzymes from Wolinella succinogenes strain DSM 1740 by affinity chromatography, cleavage of the MBP-tag by TEV protease | Caminibacter mediatlanticus |
| recombinant wild-type and mutant MBP-tagged enzymes from Wolinella succinogenes strain DSM 1740 by affinity chromatography, cleavage of the MBP-tag by TEV protease | Campylobacter fetus subsp. fetus |
| recombinant wild-type and mutant MBP-tagged enzymes from Wolinella succinogenes strain DSM 1740 by affinity chromatography, cleavage of the MBP-tag by TEV protease | Campylobacter curvus |
Specific Activity [micromol/min/mg]
| Specific Activity Minimum [µmol/min/mg] | Specific Activity Maximum [µmol/min/mg] | Comment | Organism |
|---|---|---|---|
| 0.01 | - |
below, purified recombinant MBP-tagged enzyme mutant W434Y, substrate hydroxylamine, oxidation, pH 7.0, 37°C | Caminibacter mediatlanticus |
| 0.01 | - |
below, purified recombinant MBP-tagged enzyme mutant W434Y, substrate hydroxylamine, oxidation, pH 7.0, 37°C | Campylobacter fetus subsp. fetus |
| 0.01 | - |
below, purified recombinant MBP-tagged wild-type enzyme, substrate hydroxylamine, oxidation, pH 7.0, 37°C | Nautilia profundicola |
| 0.03 | - |
purified recombinant MBP-tagged wild-type enzyme, substrate hydroxylamine, oxidation, pH 7.0, 37°C | Campylobacter curvus |
| 0.04 | - |
below, purified recombinant MBP-tagged enzyme mutant W434Y, substrate hydroxylamine, oxidation, pH 7.0, 37°C | Campylobacter curvus |
| 0.07 | - |
purified recombinant MBP-tagged wild-type enzyme, substrate hydroxylamine, oxidation, pH 7.0, 37°C | Campylobacter fetus subsp. fetus |
| 0.1 | - |
purified recombinant MBP-tagged wild-type enzyme, substrate hydroxylamine, oxidation, pH 7.0, 37°C | Caminibacter mediatlanticus |
| 1 | - |
purified recombinant MBP-tagged wild-type enzyme, substrate nitrite, pH 7.0, 37°C | Caminibacter mediatlanticus |
| 1.2 | - |
purified recombinant MBP-tagged wild-type enzyme, substrate nitrite, pH 7.0, 37°C | Nautilia profundicola |
| 2.9 | - |
purified recombinant MBP-tagged enzyme mutant W434Y, substrate nitrite, pH 7.0, 37°C | Caminibacter mediatlanticus |
| 8 | - |
purified recombinant MBP-tagged enzyme mutant W434Y, substrate nitrite, pH 7.0, 37°C | Campylobacter curvus |
| 16.7 | - |
purified recombinant MBP-tagged enzyme mutant W434Y, substrate nitrite, pH 7.0, 37°C | Campylobacter fetus subsp. fetus |
| 27 | - |
purified recombinant MBP-tagged wild-type enzyme, substrate nitrite, pH 7.0, 37°C | Campylobacter curvus |
| 29 | - |
purified recombinant MBP-tagged wild-type enzyme, substrate hydroxylamine, reduction, pH 7.0, 37°C | Nautilia profundicola |
| 68 | - |
purified recombinant MBP-tagged wild-type enzyme, substrate hydroxylamine, reduction, pH 7.0, 37°C | Campylobacter curvus |
| 77 | - |
purified recombinant MBP-tagged enzyme mutant W434Y, substrate hydroxylamine, reduction, pH 7.0, 37°C | Campylobacter curvus |
| 98 | - |
purified recombinant MBP-tagged enzyme mutant W434Y, substrate hydroxylamine, reduction, pH 7.0, 37°C | Caminibacter mediatlanticus |
| 149 | - |
purified recombinant MBP-tagged wild-type enzyme, substrate hydroxylamine, reduction, pH 7.0, 37°C | Campylobacter fetus subsp. fetus |
| 158 | - |
purified recombinant MBP-tagged wild-type enzyme, substrate hydroxylamine, reduction, pH 7.0, 37°C | Caminibacter mediatlanticus |
| 181 | - |
purified recombinant MBP-tagged wild-type enzyme, substrate nitrite, pH 7.0, 37°C | Campylobacter fetus subsp. fetus |
| 225 | - |
purified recombinant MBP-tagged enzyme mutant W434Y, substrate hydroxylamine, reduction, pH 7.0, 37°C | Campylobacter fetus subsp. fetus |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| hydroxylamine + ferricytochrome c | - |
Caminibacter mediatlanticus | nitrite + ferrocytochrome c | - |
r | |
| hydroxylamine + ferricytochrome c | - |
Nautilia profundicola | nitrite + ferrocytochrome c | - |
r | |
| hydroxylamine + ferricytochrome c | - |
Campylobacter fetus subsp. fetus | nitrite + ferrocytochrome c | - |
r | |
| hydroxylamine + ferricytochrome c | - |
Campylobacter curvus | nitrite + ferrocytochrome c | - |
r | |
| hydroxylamine + ferrocytochrome c | cf. EC 1.7.99.1 | Caminibacter mediatlanticus | NH3 + H2O + ferricytochrome c | - |
r | |
| hydroxylamine + ferrocytochrome c | cf. EC 1.7.99.1 | Nautilia profundicola | NH3 + H2O + ferricytochrome c | - |
r | |
| hydroxylamine + ferrocytochrome c | cf. EC 1.7.99.1 | Campylobacter fetus subsp. fetus | NH3 + H2O + ferricytochrome c | - |
r | |
| hydroxylamine + ferrocytochrome c | cf. EC 1.7.99.1 | Campylobacter curvus | NH3 + H2O + ferricytochrome c | - |
r | |
| hydroxylamine + ferrocytochrome c | best substrate, cf. EC 1.7.99.1 | Caminibacter mediatlanticus | NH3 + H2O + ferricytochrome c | - |
r | |
| hydroxylamine + ferrocytochrome c | best substrate, cf. EC 1.7.99.1 | Nautilia profundicola | NH3 + H2O + ferricytochrome c | - |
r | |
| additional information | the recombinant enzyme is able to catalyze reduction of nitrite (yielding ammonium) and hydroxylamine, EC 1.7.99.1, whereas hydroxylamine oxidation is negligible | Caminibacter mediatlanticus | ? | - |
? | |
| additional information | the recombinant enzyme is able to catalyze reduction of nitrite (yielding ammonium) and hydroxylamine, EC 1.7.99.1, whereas hydroxylamine oxidation is negligible | Nautilia profundicola | ? | - |
? | |
| additional information | the recombinant enzyme is able to catalyze reduction of nitrite (yielding ammonium) and hydroxylamine, EC 1.7.99.1, whereas hydroxylamine oxidation is negligible | Campylobacter fetus subsp. fetus | ? | - |
? | |
| additional information | the recombinant enzyme is able to catalyze reduction of nitrite (yielding ammonium) and hydroxylamine, EC 1.7.99.1, whereas hydroxylamine oxidation is negligible | Campylobacter curvus | ? | - |
? | |
| nitrite + 6 ferrocytochrome c + 7 H+ | - |
Caminibacter mediatlanticus | NH3 + 2 H2O + 6 ferricytochrome c | - |
? | |
| nitrite + 6 ferrocytochrome c + 7 H+ | - |
Nautilia profundicola | NH3 + 2 H2O + 6 ferricytochrome c | - |
? | |
| nitrite + 6 ferrocytochrome c + 7 H+ | - |
Campylobacter fetus subsp. fetus | NH3 + 2 H2O + 6 ferricytochrome c | - |
? | |
| nitrite + 6 ferrocytochrome c + 7 H+ | - |
Campylobacter curvus | NH3 + 2 H2O + 6 ferricytochrome c | - |
? | |
| nitrite + 6 ferrocytochrome c + 7 H+ | very low activity | Caminibacter mediatlanticus | NH3 + 2 H2O + 6 ferricytochrome c | - |
? | |
| nitrite + 6 ferrocytochrome c + 7 H+ | best substrate | Campylobacter fetus subsp. fetus | NH3 + 2 H2O + 6 ferricytochrome c | - |
? | |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| CcuHao | - |
Campylobacter curvus |
| CfHao | - |
Campylobacter fetus subsp. fetus |
| CmHao | - |
Caminibacter mediatlanticus |
| epsilonHao | - |
Caminibacter mediatlanticus |
| epsilonHao | - |
Nautilia profundicola |
| epsilonHao | - |
Campylobacter fetus subsp. fetus |
| epsilonHao | - |
Campylobacter curvus |
| epsilonproteobacterial hydroxylamine oxidoreductase | - |
Caminibacter mediatlanticus |
| epsilonproteobacterial hydroxylamine oxidoreductase | - |
Nautilia profundicola |
| epsilonproteobacterial hydroxylamine oxidoreductase | - |
Campylobacter fetus subsp. fetus |
| epsilonproteobacterial hydroxylamine oxidoreductase | - |
Campylobacter curvus |
| haoA | - |
Caminibacter mediatlanticus |
| haoA | - |
Nautilia profundicola |
| haoA | - |
Campylobacter fetus subsp. fetus |
| haoA | - |
Campylobacter curvus |
| More | cf. EC 1.7.99.1 | Caminibacter mediatlanticus |
| More | cf. EC 1.7.99.1 | Nautilia profundicola |
| More | cf. EC 1.7.99.1 | Campylobacter fetus subsp. fetus |
| More | cf. EC 1.7.99.1 | Campylobacter curvus |
| NpHao | - |
Nautilia profundicola |
Temperature Optimum [°C]
| Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
|---|---|---|---|
| 37 | - |
assay at | Caminibacter mediatlanticus |
| 37 | - |
assay at | Nautilia profundicola |
| 37 | - |
assay at | Campylobacter fetus subsp. fetus |
| 37 | - |
assay at | Campylobacter curvus |
pH Optimum
| pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|
| 7 | - |
assay at | Caminibacter mediatlanticus |
| 7 | - |
assay at | Nautilia profundicola |
| 7 | - |
assay at | Campylobacter fetus subsp. fetus |
| 7 | - |
assay at | Campylobacter curvus |
Cofactor
| Cofactor | Comment | Organism | Structure |
|---|---|---|---|
| cytochrome c | multiheme | Caminibacter mediatlanticus | |
| cytochrome c | multiheme | Nautilia profundicola | |
| cytochrome c | multiheme | Campylobacter fetus subsp. fetus | |
| cytochrome c | multiheme | Campylobacter curvus | |
General Information
| General Information | Comment | Organism |
|---|---|---|
| evolution | the enzyme is a member of the multiheme cytochrome c family. Members of the Hao subfamily, here called epilonHao proteins, have been predicted from the genomes of nitrate/nitrite-ammonifying bacteria that usually lack NrfA. Formation of a membrane-bound HaoCA assembly reminiscent of the menaquinol-oxidizing NrfHA complex. epsilonHao proteins form a subfamily of ammonifying cytochrome c nitrite reductases that represents a missing link in the evolution of NrfA, EC 1.7.2.2, and Hao, EC 1.7.99.1, enzymes, epsilonHao-type proteins are ancestors of different multiheme cytochrome c (MCC) subfamilies that catalyze either reductive (NrfA-type MCCs) or oxidative (Hao/Hdh-type MCCs) reactions. Comparison of the enzyme from Caminibacter mediatlanticus with NrfA from Wolinella succinogenes and Hao from Nitrosomonas europaea, overview | Caminibacter mediatlanticus |
| evolution | the enzyme is a member of the multiheme cytochrome c family. Members of the Hao subfamily, here called epilonHao proteins, have been predicted from the genomes of nitrate/nitrite-ammonifying bacteria that usually lack NrfA. Formation of a membrane-bound HaoCA assembly reminiscent of the menaquinol-oxidizing NrfHA complex. epsilonHao proteins form a subfamily of ammonifying cytochrome c nitrite reductases that represents a missing link in the evolution of NrfA, EC 1.7.2.2, and Hao, EC 1.7.99.1, enzymes, epsilonHao-type proteins are ancestors of different multiheme cytochrome c (MCC) subfamilies that catalyze either reductive (NrfA-type MCCs) or oxidative (Hao/Hdh-type MCCs) reactions. Comparison of the enzyme from Campylobacter curvus with NrfA from Wolinella succinogenes and Hao from Nitrosomonas europaea, overview | Campylobacter curvus |
| evolution | the enzyme is a member of the multiheme cytochrome c family. Members of the Hao subfamily, here called epilonHao proteins, have been predicted from the genomes of nitrate/nitrite-ammonifying bacteria that usually lack NrfA. Formation of a membrane-bound HaoCA assembly reminiscent of the menaquinol-oxidizing NrfHA complex. epsilonHao proteins form a subfamily of ammonifying cytochrome c nitrite reductases that represents a missing link in the evolution of NrfA, EC 1.7.2.2, and Hao, EC 1.7.99.1, enzymes, epsilonHao-type proteins are ancestors of different multiheme cytochrome c (MCC) subfamilies that catalyze either reductive (NrfA-type MCCs) or oxidative (Hao/Hdh-type MCCs) reactions. Comparison of the enzyme from Campylobacter fetus with NrfA from Wolinella succinogenes and Hao from Nitrosomonas europaea, overview | Campylobacter fetus subsp. fetus |
| evolution | the enzyme is a member of the multiheme cytochrome c family. Members of the Hao subfamily, here called epilonHao proteins, have been predicted from the genomes of nitrate/nitrite-ammonifying bacteria that usually lack NrfA. Formation of a membrane-bound HaoCA assembly reminiscent of the menaquinol-oxidizing NrfHA complex. epsilonHao proteins form a subfamily of ammonifying cytochrome c nitrite reductases that represents a missing link in the evolution of NrfA, EC 1.7.2.2, and Hao, EC 1.7.99.1, enzymes, epsilonHao-type proteins are ancestors of different multiheme cytochrome c (MCC) subfamilies that catalyze either reductive (NrfA-type MCCs) or oxidative (Hao/Hdh-type MCCs) reactions. Comparison of the enzyme from Nautilia profundicola with NrfA from Wolinella succinogenes and Hao from Nitrosomonas europaea, overview | Nautilia profundicola |
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