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Literature summary extracted from

  • Shimamura, M.; Nishiyama, T.; Shigetomo, H.; Toyomoto, T.; Kawahara, Y.; Furukawa, K.; Fujii, T.
    Isolation of a multiheme protein with features of a hydrazine-oxidizing enzyme from an anaerobic ammonium-oxidizing enrichment culture (2007), Appl. Environ. Microbiol., 73, 1065-1072.
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

EC Number Cloned (Comment) Organism
1.7.2.8
-
 Candidatus Jettenia caeni

Inhibitors

EC Number Inhibitors Comment Organism Structure
1.7.2.8 hydroxylamine inhibits activity with hydrazine as substrate Candidatus Jettenia caeni

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
1.7.2.8 0.0055
-
 hydrazine pH 8.0, 35°C Candidatus Jettenia caeni

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
1.7.2.8 62000
-
 2 * 62000, SDS-PAGE Candidatus Jettenia caeni
1.7.2.8 130000
-
 gel filtration Candidatus Jettenia caeni

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
1.7.2.8 additional information Candidatus Jettenia caeni hydrazine-oxidizing enzyme (HZO, wich has no activity with hydroxylamine) and hydroxylamine oxidoreductase (HAO, which oxidizes hydroxylamine and hydrazine) occur both in planctomycete KSU-1 ?
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
1.7.2.8 Candidatus Jettenia caeni A0P951
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
1.7.2.8
-
 Candidatus Jettenia caeni

Source Tissue

EC Number Source Tissue Comment Organism Textmining

Specific Activity [micromol/min/mg]

EC Number Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
1.7.2.8 5.8
-
 reaction with ferricytochrome c Candidatus Jettenia caeni

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.7.2.8 hydrazine + 2,6-dichloroindophenol
-
 Candidatus Jettenia caeni ? + reduced 2,6-dichloroindophenol
-
 ?
1.7.2.8 hydrazine + ferricyanide
-
 Candidatus Jettenia caeni ? + ferrocyanide
-
 ?
1.7.2.8 hydrazine + ferricytochrome c
-
 Candidatus Jettenia caeni ? + ferrocytochrome c
-
 ?
1.7.2.8 hydrazine + methylthiazolyltetrazolium bromide reduction of methylthiazolyltetrazolium bromide via phenazine methosulfate Candidatus Jettenia caeni ? + reduced methylthiazolyltetrazolium bromide
-
 ?
1.7.2.8 hydrazine + phenazine methosulfate
-
 Candidatus Jettenia caeni ? + reduced phenazine methosulfate
-
 ?
1.7.2.8 additional information hydrazine-oxidizing enzyme (HZO, wich has no activity with hydroxylamine) and hydroxylamine oxidoreductase (HAO, which oxidizes hydroxylamine and hydrazine) occur both in planctomycete KSU-1 Candidatus Jettenia caeni ?
-
 ?
1.7.2.8 additional information no activity with NAD+, hydroxylamine is not a substrate for hydrazine-oxidizing enzyme HZOB Candidatus Jettenia caeni ?
-
 ?

Subunits

EC Number Subunits Comment Organism
1.7.2.8 dimer 2 * 62000, SDS-PAGE Candidatus Jettenia caeni

Synonyms

EC Number Synonyms Comment Organism
1.7.2.8 hydrazine-oxidizing enzyme
-
 Candidatus Jettenia caeni
1.7.2.8 hzoB
-
 Candidatus Jettenia caeni

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
1.7.2.8 35
-
 assay at Candidatus Jettenia caeni

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
1.7.2.8 7.5 8.5
-
 Candidatus Jettenia caeni

pH Stability

EC Number pH Stability pH Stability Maximum Comment Organism
1.7.2.8 6 9 35°C, 10 min, stable Candidatus Jettenia caeni

Cofactor

EC Number Cofactor Comment Organism Structure
1.7.2.8 heme the 62000 Da subunits contains eight heme Candidatus Jettenia caeni

Ki Value [mM]

EC Number Ki Value [mM] Ki Value maximum [mM] Inhibitor Comment Organism Structure
1.7.2.8 0.0024
-
 hydroxylamine pH 8.0, 35°C Candidatus Jettenia caeni