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Literature summary 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)

EC Number Cloned (Comment) Organism
1.7.2.2 gene haoA, recombinant expression in Wolinella succinogenes strain DSM 1740 as maltose-binding-protein fusion His6-tagged enzyme Nautilia profundicola
1.7.2.2 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
1.7.2.2 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
1.7.2.2 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
1.7.2.6 expressed in Wolinella succinogenes as enzyme-maltose binding protein fusion Campylobacter fetus
1.7.2.6 expressed in Wolinella succinogenes as enzyme-maltose binding protein fusion Caminibacter mediatlanticus
1.7.2.6 expressed in Wolinella succinogenes as enzyme-maltose binding protein fusion Nautilia profundicola
1.7.2.6 expressed in Wolinella succinogenes as enzyme-maltose binding protein fusion Campylobacter curvus
1.7.2.6 expression in Wolinella succinogenes as maltose binding protein fusion Campylobacter fetus
1.7.2.6 expression in Wolinella succinogenes as maltose binding protein fusion Caminibacter mediatlanticus
1.7.2.6 expression in Wolinella succinogenes as maltose binding protein fusion Nautilia profundicola
1.7.2.6 expression in Wolinella succinogenes as maltose binding protein fusion Campylobacter curvus
1.7.99.1 gene haoA, recombinant expression in Wolinella succinogenes strain DSM 1740 as maltose-binding-protein fusion His6-tagged enzyme Nautilia profundicola
1.7.99.1 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
1.7.99.1 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
1.7.99.1 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

EC Number Protein Variants Comment Organism
1.7.2.2 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
1.7.2.2 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
1.7.2.2 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
1.7.2.2 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
1.7.2.2 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
1.7.2.2 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
1.7.2.6 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
1.7.2.6 W428Y the mutant produces a higher amount of nitrite from hydroxylamine oxidation than the corresponding wild type enzyme Campylobacter curvus
1.7.2.6 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
1.7.2.6 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
1.7.2.6 W464Y the mutant produces a higher amount of nitrite from hydroxylamine oxidation than the corresponding wild type enzyme Caminibacter mediatlanticus
1.7.99.1 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
1.7.99.1 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
1.7.99.1 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
1.7.99.1 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
1.7.99.1 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
1.7.99.1 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]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
1.7.2.2 0.89
-
 nitrite recombinant MBP-tagged wild-type enzyme, pH 7.0, 37°C Campylobacter fetus subsp. fetus
1.7.2.2 1
-
 hydroxylamine oxidation reaction, recombinant MBP-tagged wild-type enzyme, pH 7.0, 37°C Campylobacter fetus subsp. fetus
1.7.2.2 1.4
-
 hydroxylamine oxidation reaction, recombinant MBP-tagged wild-type enzyme, pH 7.0, 37°C Caminibacter mediatlanticus
1.7.2.2 1.5
-
 hydroxylamine oxidation reaction, recombinant MBP-tagged wild-type enzyme, pH 7.0, 37°C Campylobacter curvus
1.7.2.2 1.5
-
 nitrite recombinant MBP-tagged wild-type enzyme, pH 7.0, 37°C Caminibacter mediatlanticus
1.7.2.2 1.9
-
 hydroxylamine reduction reaction, recombinant MBP-tagged wild-type enzyme, pH 7.0, 37°C Campylobacter fetus subsp. fetus
1.7.2.2 2.39
-
 nitrite recombinant MBP-tagged mutant W434Y, pH 7.0, 37°C Campylobacter fetus subsp. fetus
1.7.2.2 2.7
-
 nitrite recombinant MBP-tagged wild-type enzyme, pH 7.0, 37°C Campylobacter curvus
1.7.2.2 2.99
-
 nitrite recombinant MBP-tagged mutant W434Y, pH 7.0, 37°C Campylobacter curvus
1.7.2.2 4.7
-
 nitrite recombinant MBP-tagged mutant W434Y, pH 7.0, 37°C Caminibacter mediatlanticus
1.7.2.2 5.3
-
 hydroxylamine oxidation reaction, recombinant MBP-tagged mutant W434Y, pH 7.0, 37°C Campylobacter curvus
1.7.2.2 6
-
 hydroxylamine reduction reaction, recombinant MBP-tagged wild-type enzyme, pH 7.0, 37°C Caminibacter mediatlanticus
1.7.2.2 6.6
-
 hydroxylamine reduction reaction, recombinant MBP-tagged wild-type enzyme, pH 7.0, 37°C Campylobacter curvus
1.7.2.2 6.75
-
 hydroxylamine reduction reaction, recombinant MBP-tagged mutant W434Y, pH 7.0, 37°C Campylobacter curvus
1.7.2.2 7.4
-
 hydroxylamine reduction reaction, recombinant MBP-tagged mutant W434Y, pH 7.0, 37°C Campylobacter fetus subsp. fetus
1.7.2.2 16.9
-
 hydroxylamine reduction reaction, recombinant MBP-tagged mutant W434Y, pH 7.0, 37°C Caminibacter mediatlanticus
1.7.2.6 0.89
-
 nitrite wild-type, pH 7.0, 37°C Campylobacter fetus
1.7.2.6 1.5
-
 nitrite wild-type, pH 7.0, 37°C Caminibacter mediatlanticus
1.7.2.6 1.9
-
 hydroxylamine wild-type, pH 7.0, 37°C Campylobacter fetus
1.7.2.6 2.39
-
 nitrite mutant W434Y, pH 7.0, 37°C Campylobacter fetus
1.7.2.6 2.7
-
 nitrite wild-type, pH 7.0, 37°C Campylobacter curvus
1.7.2.6 2.99
-
 nitrite mutant W428Y, pH 7.0, 37°C Campylobacter curvus
1.7.2.6 4.6
-
 nitrite mutant W464Y, pH 7.0, 37°C Caminibacter mediatlanticus
1.7.2.6 6
-
 hydroxylamine wild-type, pH 7.0, 37°C Caminibacter mediatlanticus
1.7.2.6 6.6
-
 hydroxylamine wild-type, pH 7.0, 37°C Campylobacter curvus
1.7.2.6 6.75
-
 hydroxylamine mutant W428Y, pH 7.0, 37°C Campylobacter curvus
1.7.2.6 7.4
-
 hydroxylamine mutant W434Y, pH 7.0, 37°C Campylobacter fetus
1.7.2.6 16.9
-
 hydroxylamine mutant W464Y, pH 7.0, 37°C Caminibacter mediatlanticus
1.7.99.1 1
-
 hydroxylamine oxidation reaction, recombinant MBP-tagged wild-type enzyme, pH 7.0, 37°C Campylobacter fetus subsp. fetus
1.7.99.1 1.4
-
 hydroxylamine oxidation reaction, recombinant MBP-tagged wild-type enzyme, pH 7.0, 37°C Caminibacter mediatlanticus
1.7.99.1 1.5
-
 hydroxylamine oxidation reaction, recombinant MBP-tagged wild-type enzyme, pH 7.0, 37°C Campylobacter curvus
1.7.99.1 1.5
-
 nitrite recombinant MBP-tagged wild-type enzyme, pH 7.0, 37°C Caminibacter mediatlanticus
1.7.99.1 1.9
-
 hydroxylamine reduction reaction, recombinant MBP-tagged wild-type enzyme, pH 7.0, 37°C Campylobacter fetus subsp. fetus
1.7.99.1 4.7
-
 nitrite recombinant MBP-tagged mutant W434Y, pH 7.0, 37°C Caminibacter mediatlanticus
1.7.99.1 5.3
-
 hydroxylamine oxidation reaction, recombinant MBP-tagged mutant W434Y, pH 7.0, 37°C Campylobacter curvus
1.7.99.1 6
-
 hydroxylamine reduction reaction, recombinant MBP-tagged wild-type enzyme, pH 7.0, 37°C Caminibacter mediatlanticus
1.7.99.1 6.6
-
 hydroxylamine reduction reaction, recombinant MBP-tagged wild-type enzyme, pH 7.0, 37°C Campylobacter curvus
1.7.99.1 6.75
-
 hydroxylamine reduction reaction, recombinant MBP-tagged mutant W434Y, pH 7.0, 37°C Campylobacter curvus
1.7.99.1 7.4
-
 hydroxylamine reduction reaction, recombinant MBP-tagged mutant W434Y, pH 7.0, 37°C Campylobacter fetus subsp. fetus
1.7.99.1 16.9
-
 hydroxylamine reduction reaction, recombinant MBP-tagged mutant W434Y, pH 7.0, 37°C Caminibacter mediatlanticus

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
1.7.2.2 Fe2+ heme Caminibacter mediatlanticus
1.7.2.2 Fe2+ heme Nautilia profundicola
1.7.2.2 Fe2+ heme Campylobacter fetus subsp. fetus
1.7.2.2 Fe2+ heme Campylobacter curvus
1.7.99.1 Fe2+ heme Caminibacter mediatlanticus
1.7.99.1 Fe2+ heme Nautilia profundicola
1.7.99.1 Fe2+ heme Campylobacter fetus subsp. fetus
1.7.99.1 Fe2+ heme Campylobacter curvus

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
1.7.2.2 hydroxylamine + ferricytochrome c Caminibacter mediatlanticus
-
 nitrite + ferrocytochrome c
-
 r
1.7.2.2 hydroxylamine + ferricytochrome c Nautilia profundicola
-
 nitrite + ferrocytochrome c
-
 r
1.7.2.2 hydroxylamine + ferricytochrome c Campylobacter fetus subsp. fetus
-
 nitrite + ferrocytochrome c
-
 r
1.7.2.2 hydroxylamine + ferricytochrome c Campylobacter curvus
-
 nitrite + ferrocytochrome c
-
 r
1.7.2.2 hydroxylamine + ferrocytochrome c Caminibacter mediatlanticus cf. EC 1.7.99.1 NH3 + H2O + ferricytochrome c
-
 r
1.7.2.2 hydroxylamine + ferrocytochrome c Nautilia profundicola cf. EC 1.7.99.1 NH3 + H2O + ferricytochrome c
-
 r
1.7.2.2 hydroxylamine + ferrocytochrome c Campylobacter fetus subsp. fetus cf. EC 1.7.99.1 NH3 + H2O + ferricytochrome c
-
 r
1.7.2.2 hydroxylamine + ferrocytochrome c Campylobacter curvus cf. EC 1.7.99.1 NH3 + H2O + ferricytochrome c
-
 r
1.7.2.2 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 ?
-
 ?
1.7.2.2 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 ?
-
 ?
1.7.2.2 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 ?
-
 ?
1.7.2.2 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 ?
-
 ?
1.7.2.2 nitrite + 6 ferrocytochrome c + 7 H+ Caminibacter mediatlanticus
-
 NH3 + 2 H2O + 6 ferricytochrome c
-
 ?
1.7.2.2 nitrite + 6 ferrocytochrome c + 7 H+ Nautilia profundicola
-
 NH3 + 2 H2O + 6 ferricytochrome c
-
 ?
1.7.2.2 nitrite + 6 ferrocytochrome c + 7 H+ Campylobacter fetus subsp. fetus
-
 NH3 + 2 H2O + 6 ferricytochrome c
-
 ?
1.7.2.2 nitrite + 6 ferrocytochrome c + 7 H+ Campylobacter curvus
-
 NH3 + 2 H2O + 6 ferricytochrome c
-
 ?
1.7.2.6 hydroxylamine + H2O + 4 ferricytochrome c Campylobacter fetus
-
 nitrite + 4 ferrocytochrome c + 5 H+
-
 ?
1.7.2.6 hydroxylamine + H2O + 4 ferricytochrome c Caminibacter mediatlanticus
-
 nitrite + 4 ferrocytochrome c + 5 H+
-
 ?
1.7.2.6 hydroxylamine + H2O + 4 ferricytochrome c Nautilia profundicola
-
 nitrite + 4 ferrocytochrome c + 5 H+
-
 ?
1.7.2.6 hydroxylamine + H2O + 4 ferricytochrome c Campylobacter curvus
-
 nitrite + 4 ferrocytochrome c + 5 H+
-
 ?
1.7.99.1 hydroxylamine + ferricytochrome c Caminibacter mediatlanticus
-
 nitrite + ferrocytochrome c
-
 r
1.7.99.1 hydroxylamine + ferricytochrome c Nautilia profundicola
-
 nitrite + ferrocytochrome c
-
 r
1.7.99.1 hydroxylamine + ferricytochrome c Campylobacter fetus subsp. fetus
-
 nitrite + ferrocytochrome c
-
 r
1.7.99.1 hydroxylamine + ferricytochrome c Campylobacter curvus
-
 nitrite + ferrocytochrome c
-
 r
1.7.99.1 hydroxylamine + ferrocytochrome c Caminibacter mediatlanticus
-
 NH3 + H2O + ferricytochrome c
-
 r
1.7.99.1 hydroxylamine + ferrocytochrome c Nautilia profundicola
-
 NH3 + H2O + ferricytochrome c
-
 r
1.7.99.1 hydroxylamine + ferrocytochrome c Campylobacter fetus subsp. fetus
-
 NH3 + H2O + ferricytochrome c
-
 r
1.7.99.1 hydroxylamine + ferrocytochrome c Campylobacter curvus
-
 NH3 + H2O + ferricytochrome c
-
 r
1.7.99.1 additional information Campylobacter fetus subsp. fetus the recombinant enzyme is able to catalyze reduction of nitrite (yielding ammonium), EC 1.7.2.2, and hydroxylamine whereas hydroxylamine oxidation is negligible ?
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
1.7.2.2 Caminibacter mediatlanticus
-
-
-
1.7.2.2 Campylobacter curvus A7GXH2
-
-
1.7.2.2 Campylobacter fetus subsp. fetus
-
-
-
1.7.2.2 Nautilia profundicola
-
-
-
1.7.2.6 Caminibacter mediatlanticus
-
-
-
1.7.2.6 Campylobacter curvus
-
-
-
1.7.2.6 Campylobacter fetus
-
-
-
1.7.2.6 Nautilia profundicola
-
-
-
1.7.99.1 Caminibacter mediatlanticus
-
-
-
1.7.99.1 Campylobacter curvus A7GXH2
-
-
1.7.99.1 Campylobacter fetus subsp. fetus
-
-
-
1.7.99.1 Nautilia profundicola
-
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
1.7.2.2 recombinant MBP-tagged enzyme from Wolinella succinogenes strain DSM 1740 by affinity chromatography, cleavage of the MBP-tag by TEV protease Nautilia profundicola
1.7.2.2 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
1.7.2.2 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
1.7.2.2 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
1.7.2.6 maltose binding protein Trap column chromatography Campylobacter fetus
1.7.2.6 maltose binding protein Trap column chromatography Caminibacter mediatlanticus
1.7.2.6 maltose binding protein Trap column chromatography Nautilia profundicola
1.7.2.6 maltose binding protein Trap column chromatography Campylobacter curvus
1.7.99.1 recombinant MBP-tagged enzyme from Wolinella succinogenes strain DSM 1740 by affinity chromatography, cleavage of the MBP-tag by TEV protease Nautilia profundicola
1.7.99.1 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
1.7.99.1 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
1.7.99.1 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]

EC Number Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
1.7.2.2 0.01
-
 below, purified recombinant MBP-tagged enzyme mutant W434Y, substrate hydroxylamine, oxidation, pH 7.0, 37°C Caminibacter mediatlanticus
1.7.2.2 0.01
-
 below, purified recombinant MBP-tagged enzyme mutant W434Y, substrate hydroxylamine, oxidation, pH 7.0, 37°C Campylobacter fetus subsp. fetus
1.7.2.2 0.01
-
 below, purified recombinant MBP-tagged wild-type enzyme, substrate hydroxylamine, oxidation, pH 7.0, 37°C Nautilia profundicola
1.7.2.2 0.03
-
 purified recombinant MBP-tagged wild-type enzyme, substrate hydroxylamine, oxidation, pH 7.0, 37°C Campylobacter curvus
1.7.2.2 0.04
-
 below, purified recombinant MBP-tagged enzyme mutant W434Y, substrate hydroxylamine, oxidation, pH 7.0, 37°C Campylobacter curvus
1.7.2.2 0.07
-
 purified recombinant MBP-tagged wild-type enzyme, substrate hydroxylamine, oxidation, pH 7.0, 37°C Campylobacter fetus subsp. fetus
1.7.2.2 0.1
-
 purified recombinant MBP-tagged wild-type enzyme, substrate hydroxylamine, oxidation, pH 7.0, 37°C Caminibacter mediatlanticus
1.7.2.2 1
-
 purified recombinant MBP-tagged wild-type enzyme, substrate nitrite, pH 7.0, 37°C Caminibacter mediatlanticus
1.7.2.2 1.2
-
 purified recombinant MBP-tagged wild-type enzyme, substrate nitrite, pH 7.0, 37°C Nautilia profundicola
1.7.2.2 2.9
-
 purified recombinant MBP-tagged enzyme mutant W434Y, substrate nitrite, pH 7.0, 37°C Caminibacter mediatlanticus
1.7.2.2 8
-
 purified recombinant MBP-tagged enzyme mutant W434Y, substrate nitrite, pH 7.0, 37°C Campylobacter curvus
1.7.2.2 16.7
-
 purified recombinant MBP-tagged enzyme mutant W434Y, substrate nitrite, pH 7.0, 37°C Campylobacter fetus subsp. fetus
1.7.2.2 27
-
 purified recombinant MBP-tagged wild-type enzyme, substrate nitrite, pH 7.0, 37°C Campylobacter curvus
1.7.2.2 29
-
 purified recombinant MBP-tagged wild-type enzyme, substrate hydroxylamine, reduction, pH 7.0, 37°C Nautilia profundicola
1.7.2.2 68
-
 purified recombinant MBP-tagged wild-type enzyme, substrate hydroxylamine, reduction, pH 7.0, 37°C Campylobacter curvus
1.7.2.2 77
-
 purified recombinant MBP-tagged enzyme mutant W434Y, substrate hydroxylamine, reduction, pH 7.0, 37°C Campylobacter curvus
1.7.2.2 98
-
 purified recombinant MBP-tagged enzyme mutant W434Y, substrate hydroxylamine, reduction, pH 7.0, 37°C Caminibacter mediatlanticus
1.7.2.2 149
-
 purified recombinant MBP-tagged wild-type enzyme, substrate hydroxylamine, reduction, pH 7.0, 37°C Campylobacter fetus subsp. fetus
1.7.2.2 158
-
 purified recombinant MBP-tagged wild-type enzyme, substrate hydroxylamine, reduction, pH 7.0, 37°C Caminibacter mediatlanticus
1.7.2.2 181
-
 purified recombinant MBP-tagged wild-type enzyme, substrate nitrite, pH 7.0, 37°C Campylobacter fetus subsp. fetus
1.7.2.2 225
-
 purified recombinant MBP-tagged enzyme mutant W434Y, substrate hydroxylamine, reduction, pH 7.0, 37°C Campylobacter fetus subsp. fetus
1.7.2.6 1
-
 nitrite reduction, pH 7.0, 37°C Caminibacter mediatlanticus
1.7.2.6 1.2
-
 nitrite reduction, pH 7.0, 37°C Nautilia profundicola
1.7.2.6 27
-
 nitrite reduction, pH 7.0, 37°C Campylobacter curvus
1.7.2.6 29
-
 hydroxylamine reduction, pH 7.0, 37°C Nautilia profundicola
1.7.2.6 68
-
 hydroxylamine reduction, pH 7.0, 37°C Campylobacter curvus
1.7.2.6 149
-
 hydroxylamine reduction, pH 7.0, 37°C Campylobacter fetus
1.7.2.6 158
-
 hydroxylamine reduction, pH 7.0, 37°C Caminibacter mediatlanticus
1.7.2.6 181
-
 nitrite reduction, pH 7.0, 37°C Campylobacter fetus
1.7.99.1 0.01
-
 below, purified recombinant MBP-tagged enzyme mutant W434Y, substrate hydroxylamine, oxidation, pH 7.0, 37°C Caminibacter mediatlanticus
1.7.99.1 0.01
-
 below, purified recombinant MBP-tagged enzyme mutant W434Y, substrate hydroxylamine, oxidation, pH 7.0, 37°C Campylobacter fetus subsp. fetus
1.7.99.1 0.01
-
 below, purified recombinant MBP-tagged wild-type enzyme, substrate hydroxylamine, oxidation, pH 7.0, 37°C Nautilia profundicola
1.7.99.1 0.03
-
 purified recombinant MBP-tagged wild-type enzyme, substrate hydroxylamine, oxidation, pH 7.0, 37°C Campylobacter curvus
1.7.99.1 0.04
-
 below, purified recombinant MBP-tagged enzyme mutant W434Y, substrate hydroxylamine, oxidation, pH 7.0, 37°C Campylobacter curvus
1.7.99.1 0.07
-
 purified recombinant MBP-tagged wild-type enzyme, substrate hydroxylamine, oxidation, pH 7.0, 37°C Campylobacter fetus subsp. fetus
1.7.99.1 0.1
-
 purified recombinant MBP-tagged wild-type enzyme, substrate hydroxylamine, oxidation, pH 7.0, 37°C Caminibacter mediatlanticus
1.7.99.1 1
-
 purified recombinant MBP-tagged wild-type enzyme, substrate nitrite, pH 7.0, 37°C Caminibacter mediatlanticus
1.7.99.1 2.9
-
 purified recombinant MBP-tagged enzyme mutant W434Y, substrate nitrite, pH 7.0, 37°C Caminibacter mediatlanticus
1.7.99.1 29
-
 purified recombinant MBP-tagged wild-type enzyme, substrate hydroxylamine, reduction, pH 7.0, 37°C Nautilia profundicola
1.7.99.1 68
-
 purified recombinant MBP-tagged wild-type enzyme, substrate hydroxylamine, reduction, pH 7.0, 37°C Campylobacter curvus
1.7.99.1 77
-
 purified recombinant MBP-tagged enzyme mutant W434Y, substrate hydroxylamine, reduction, pH 7.0, 37°C Campylobacter curvus
1.7.99.1 98
-
 purified recombinant MBP-tagged enzyme mutant W434Y, substrate hydroxylamine, reduction, pH 7.0, 37°C Caminibacter mediatlanticus
1.7.99.1 149
-
 purified recombinant MBP-tagged wild-type enzyme, substrate hydroxylamine, reduction, pH 7.0, 37°C Campylobacter fetus subsp. fetus
1.7.99.1 158
-
 purified recombinant MBP-tagged wild-type enzyme, substrate hydroxylamine, reduction, pH 7.0, 37°C Caminibacter mediatlanticus
1.7.99.1 225
-
 purified recombinant MBP-tagged enzyme mutant W434Y, substrate hydroxylamine, reduction, pH 7.0, 37°C Campylobacter fetus subsp. fetus

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.7.2.2 hydroxylamine + ferricytochrome c
-
 Caminibacter mediatlanticus nitrite + ferrocytochrome c
-
 r
1.7.2.2 hydroxylamine + ferricytochrome c
-
 Nautilia profundicola nitrite + ferrocytochrome c
-
 r
1.7.2.2 hydroxylamine + ferricytochrome c
-
 Campylobacter fetus subsp. fetus nitrite + ferrocytochrome c
-
 r
1.7.2.2 hydroxylamine + ferricytochrome c
-
 Campylobacter curvus nitrite + ferrocytochrome c
-
 r
1.7.2.2 hydroxylamine + ferrocytochrome c cf. EC 1.7.99.1 Caminibacter mediatlanticus NH3 + H2O + ferricytochrome c
-
 r
1.7.2.2 hydroxylamine + ferrocytochrome c cf. EC 1.7.99.1 Nautilia profundicola NH3 + H2O + ferricytochrome c
-
 r
1.7.2.2 hydroxylamine + ferrocytochrome c cf. EC 1.7.99.1 Campylobacter fetus subsp. fetus NH3 + H2O + ferricytochrome c
-
 r
1.7.2.2 hydroxylamine + ferrocytochrome c cf. EC 1.7.99.1 Campylobacter curvus NH3 + H2O + ferricytochrome c
-
 r
1.7.2.2 hydroxylamine + ferrocytochrome c best substrate, cf. EC 1.7.99.1 Caminibacter mediatlanticus NH3 + H2O + ferricytochrome c
-
 r
1.7.2.2 hydroxylamine + ferrocytochrome c best substrate, cf. EC 1.7.99.1 Nautilia profundicola NH3 + H2O + ferricytochrome c
-
 r
1.7.2.2 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 ?
-
 ?
1.7.2.2 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 ?
-
 ?
1.7.2.2 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 ?
-
 ?
1.7.2.2 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 ?
-
 ?
1.7.2.2 nitrite + 6 ferrocytochrome c + 7 H+
-
 Caminibacter mediatlanticus NH3 + 2 H2O + 6 ferricytochrome c
-
 ?
1.7.2.2 nitrite + 6 ferrocytochrome c + 7 H+
-
 Nautilia profundicola NH3 + 2 H2O + 6 ferricytochrome c
-
 ?
1.7.2.2 nitrite + 6 ferrocytochrome c + 7 H+
-
 Campylobacter fetus subsp. fetus NH3 + 2 H2O + 6 ferricytochrome c
-
 ?
1.7.2.2 nitrite + 6 ferrocytochrome c + 7 H+
-
 Campylobacter curvus NH3 + 2 H2O + 6 ferricytochrome c
-
 ?
1.7.2.2 nitrite + 6 ferrocytochrome c + 7 H+ very low activity Caminibacter mediatlanticus NH3 + 2 H2O + 6 ferricytochrome c
-
 ?
1.7.2.2 nitrite + 6 ferrocytochrome c + 7 H+ best substrate Campylobacter fetus subsp. fetus NH3 + 2 H2O + 6 ferricytochrome c
-
 ?
1.7.2.6 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
-
 ?
1.7.2.6 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
-
 ?
1.7.2.6 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
-
 ?
1.7.2.6 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
-
 ?
1.7.2.6 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
-
 ?
1.7.2.6 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
-
 ?
1.7.2.6 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
-
 ?
1.7.2.6 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
-
 ?
1.7.2.6 hydroxylamine + H2O + 4 ferricytochrome c
-
 Campylobacter fetus nitrite + 4 ferrocytochrome c + 5 H+
-
 ?
1.7.2.6 hydroxylamine + H2O + 4 ferricytochrome c
-
 Caminibacter mediatlanticus nitrite + 4 ferrocytochrome c + 5 H+
-
 ?
1.7.2.6 hydroxylamine + H2O + 4 ferricytochrome c
-
 Nautilia profundicola nitrite + 4 ferrocytochrome c + 5 H+
-
 ?
1.7.2.6 hydroxylamine + H2O + 4 ferricytochrome c
-
 Campylobacter curvus nitrite + 4 ferrocytochrome c + 5 H+
-
 ?
1.7.2.6 hydroxylamine + phenazine methosulfate + H2O
-
 Campylobacter fetus NH3 + oxidized phenazine methosulfate
-
 ?
1.7.2.6 hydroxylamine + phenazine methosulfate + H2O
-
 Caminibacter mediatlanticus NH3 + oxidized phenazine methosulfate
-
 ?
1.7.2.6 hydroxylamine + phenazine methosulfate + H2O
-
 Nautilia profundicola NH3 + oxidized phenazine methosulfate
-
 ?
1.7.2.6 hydroxylamine + phenazine methosulfate + H2O
-
 Campylobacter curvus NH3 + oxidized phenazine methosulfate
-
 ?
1.7.2.6 additional information hydroxylamine oxidation is negligible Campylobacter fetus ?
-
 ?
1.7.2.6 additional information hydroxylamine oxidation is negligible Caminibacter mediatlanticus ?
-
 ?
1.7.2.6 additional information hydroxylamine oxidation is negligible Nautilia profundicola ?
-
 ?
1.7.2.6 additional information hydroxylamine oxidation is negligible Campylobacter curvus ?
-
 ?
1.7.2.6 nitrite + reduced benzyl viologen + H+
-
 Campylobacter fetus NH4+ + reduced methyl viologen + H2O
-
 ?
1.7.2.6 nitrite + reduced benzyl viologen + H+
-
 Caminibacter mediatlanticus NH4+ + reduced methyl viologen + H2O
-
 ?
1.7.2.6 nitrite + reduced benzyl viologen + H+
-
 Nautilia profundicola NH4+ + reduced methyl viologen + H2O
-
 ?
1.7.2.6 nitrite + reduced benzyl viologen + H+
-
 Campylobacter curvus NH4+ + reduced methyl viologen + H2O
-
 ?
1.7.99.1 hydroxylamine + ferricytochrome c
-
 Caminibacter mediatlanticus nitrite + ferrocytochrome c
-
 r
1.7.99.1 hydroxylamine + ferricytochrome c
-
 Nautilia profundicola nitrite + ferrocytochrome c
-
 r
1.7.99.1 hydroxylamine + ferricytochrome c
-
 Campylobacter fetus subsp. fetus nitrite + ferrocytochrome c
-
 r
1.7.99.1 hydroxylamine + ferricytochrome c
-
 Campylobacter curvus nitrite + ferrocytochrome c
-
 r
1.7.99.1 hydroxylamine + ferrocytochrome c
-
 Caminibacter mediatlanticus NH3 + H2O + ferricytochrome c
-
 r
1.7.99.1 hydroxylamine + ferrocytochrome c
-
 Nautilia profundicola NH3 + H2O + ferricytochrome c
-
 r
1.7.99.1 hydroxylamine + ferrocytochrome c
-
 Campylobacter fetus subsp. fetus NH3 + H2O + ferricytochrome c
-
 r
1.7.99.1 hydroxylamine + ferrocytochrome c
-
 Campylobacter curvus NH3 + H2O + ferricytochrome c
-
 r
1.7.99.1 hydroxylamine + ferrocytochrome c best substrate Caminibacter mediatlanticus NH3 + H2O + ferricytochrome c
-
 r
1.7.99.1 hydroxylamine + ferrocytochrome c best substrate Nautilia profundicola NH3 + H2O + ferricytochrome c
-
 r
1.7.99.1 additional information the recombinant enzyme is able to catalyze reduction of nitrite (yielding ammonium), EC 1.7.2.2, and hydroxylamine whereas hydroxylamine oxidation is negligible Caminibacter mediatlanticus ?
-
 ?
1.7.99.1 additional information the recombinant enzyme is able to catalyze reduction of nitrite (yielding ammonium), EC 1.7.2.2, and hydroxylamine whereas hydroxylamine oxidation is negligible Nautilia profundicola ?
-
 ?
1.7.99.1 additional information the recombinant enzyme is able to catalyze reduction of nitrite (yielding ammonium), EC 1.7.2.2, and hydroxylamine whereas hydroxylamine oxidation is negligible Campylobacter fetus subsp. fetus ?
-
 ?
1.7.99.1 additional information the recombinant enzyme is able to catalyze reduction of nitrite (yielding ammonium), EC 1.7.2.2, and hydroxylamine whereas hydroxylamine oxidation is negligible Campylobacter curvus ?
-
 ?

Subunits

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

Synonyms

EC Number Synonyms Comment Organism
1.7.2.2 CcuHao
-
 Campylobacter curvus
1.7.2.2 CfHao
-
 Campylobacter fetus subsp. fetus
1.7.2.2 CmHao
-
 Caminibacter mediatlanticus
1.7.2.2 epsilonHao
-
 Caminibacter mediatlanticus
1.7.2.2 epsilonHao
-
 Nautilia profundicola
1.7.2.2 epsilonHao
-
 Campylobacter fetus subsp. fetus
1.7.2.2 epsilonHao
-
 Campylobacter curvus
1.7.2.2 epsilonproteobacterial hydroxylamine oxidoreductase
-
 Caminibacter mediatlanticus
1.7.2.2 epsilonproteobacterial hydroxylamine oxidoreductase
-
 Nautilia profundicola
1.7.2.2 epsilonproteobacterial hydroxylamine oxidoreductase
-
 Campylobacter fetus subsp. fetus
1.7.2.2 epsilonproteobacterial hydroxylamine oxidoreductase
-
 Campylobacter curvus
1.7.2.2 haoA
-
 Caminibacter mediatlanticus
1.7.2.2 haoA
-
 Nautilia profundicola
1.7.2.2 haoA
-
 Campylobacter fetus subsp. fetus
1.7.2.2 haoA
-
 Campylobacter curvus
1.7.2.2 More cf. EC 1.7.99.1 Caminibacter mediatlanticus
1.7.2.2 More cf. EC 1.7.99.1 Nautilia profundicola
1.7.2.2 More cf. EC 1.7.99.1 Campylobacter fetus subsp. fetus
1.7.2.2 More cf. EC 1.7.99.1 Campylobacter curvus
1.7.2.2 NpHao
-
 Nautilia profundicola
1.7.2.6 HAO
-
 Campylobacter fetus
1.7.2.6 HAO
-
 Caminibacter mediatlanticus
1.7.2.6 HAO
-
 Nautilia profundicola
1.7.2.6 HAO
-
 Campylobacter curvus
1.7.2.6 haoA
-
 Campylobacter fetus
1.7.2.6 haoA
-
 Caminibacter mediatlanticus
1.7.2.6 haoA
-
 Nautilia profundicola
1.7.2.6 haoA
-
 Campylobacter curvus
1.7.2.6 hydroxylamine oxidoreductase
-
 Campylobacter fetus
1.7.2.6 hydroxylamine oxidoreductase
-
 Caminibacter mediatlanticus
1.7.2.6 hydroxylamine oxidoreductase
-
 Nautilia profundicola
1.7.2.6 hydroxylamine oxidoreductase
-
 Campylobacter curvus
1.7.99.1 CcuHao
-
 Campylobacter curvus
1.7.99.1 CfHao
-
 Campylobacter fetus subsp. fetus
1.7.99.1 CmHao
-
 Caminibacter mediatlanticus
1.7.99.1 epsilonHao
-
 Caminibacter mediatlanticus
1.7.99.1 epsilonHao
-
 Nautilia profundicola
1.7.99.1 epsilonHao
-
 Campylobacter fetus subsp. fetus
1.7.99.1 epsilonHao
-
 Campylobacter curvus
1.7.99.1 epsilonproteobacterial hydroxylamine oxidoreductase
-
 Caminibacter mediatlanticus
1.7.99.1 epsilonproteobacterial hydroxylamine oxidoreductase
-
 Nautilia profundicola
1.7.99.1 epsilonproteobacterial hydroxylamine oxidoreductase
-
 Campylobacter fetus subsp. fetus
1.7.99.1 epsilonproteobacterial hydroxylamine oxidoreductase
-
 Campylobacter curvus
1.7.99.1 haoA
-
 Caminibacter mediatlanticus
1.7.99.1 haoA
-
 Nautilia profundicola
1.7.99.1 haoA
-
 Campylobacter fetus subsp. fetus
1.7.99.1 haoA
-
 Campylobacter curvus
1.7.99.1 More cf. EC 1.7.2.2 Caminibacter mediatlanticus
1.7.99.1 More cf. EC 1.7.2.2 Nautilia profundicola
1.7.99.1 More cf. EC 1.7.2.2 Campylobacter fetus subsp. fetus
1.7.99.1 More cf. EC 1.7.2.2 Campylobacter curvus
1.7.99.1 NpHao
-
 Nautilia profundicola

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
1.7.2.2 37
-
 assay at Caminibacter mediatlanticus
1.7.2.2 37
-
 assay at Nautilia profundicola
1.7.2.2 37
-
 assay at Campylobacter fetus subsp. fetus
1.7.2.2 37
-
 assay at Campylobacter curvus
1.7.99.1 37
-
 assay at Caminibacter mediatlanticus
1.7.99.1 37
-
 assay at Nautilia profundicola
1.7.99.1 37
-
 assay at Campylobacter fetus subsp. fetus
1.7.99.1 37
-
 assay at Campylobacter curvus

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
1.7.2.2 7
-
 assay at Caminibacter mediatlanticus
1.7.2.2 7
-
 assay at Nautilia profundicola
1.7.2.2 7
-
 assay at Campylobacter fetus subsp. fetus
1.7.2.2 7
-
 assay at Campylobacter curvus
1.7.99.1 7
-
 assay at Caminibacter mediatlanticus
1.7.99.1 7
-
 assay at Nautilia profundicola
1.7.99.1 7
-
 assay at Campylobacter fetus subsp. fetus
1.7.99.1 7
-
 assay at Campylobacter curvus

Cofactor

EC Number Cofactor Comment Organism Structure
1.7.2.2 cytochrome c multiheme Caminibacter mediatlanticus
1.7.2.2 cytochrome c multiheme Nautilia profundicola
1.7.2.2 cytochrome c multiheme Campylobacter fetus subsp. fetus
1.7.2.2 cytochrome c multiheme Campylobacter curvus
1.7.2.6 cytochrome c
-
 Campylobacter fetus
1.7.2.6 cytochrome c
-
 Caminibacter mediatlanticus
1.7.2.6 cytochrome c
-
 Nautilia profundicola
1.7.2.6 cytochrome c
-
 Campylobacter curvus
1.7.2.6 heme
-
 Campylobacter fetus
1.7.2.6 heme
-
 Caminibacter mediatlanticus
1.7.2.6 heme
-
 Nautilia profundicola
1.7.2.6 heme
-
 Campylobacter curvus
1.7.99.1 cytochrome c multiheme Caminibacter mediatlanticus
1.7.99.1 cytochrome c multiheme Nautilia profundicola
1.7.99.1 cytochrome c multiheme Campylobacter fetus subsp. fetus
1.7.99.1 cytochrome c multiheme Campylobacter curvus

General Information

EC Number General Information Comment Organism
1.7.2.2 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
1.7.2.2 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
1.7.2.2 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
1.7.2.2 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
1.7.99.1 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
1.7.99.1 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
1.7.99.1 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
1.7.99.1 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