1.7.2.6: hydroxylamine dehydrogenase
This is an abbreviated version!
For detailed information about hydroxylamine dehydrogenase, go to the full flat file.
Word Map on EC 1.7.2.6
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1.7.2.6
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ammonia
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monooxygenase
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nitrification
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metagenomic
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nitrify
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nitrospira
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europaea
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no2
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nitrosomonas
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comammox
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phenylhydrazine
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ammonium-oxidizing
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genome-centric
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analysis
- 1.7.2.6
- ammonia
- monooxygenase
-
nitrification
-
metagenomic
-
nitrify
- nitrospira
- europaea
- no2
- nitrosomonas
-
comammox
- phenylhydrazine
-
ammonium-oxidizing
-
genome-centric
- analysis
Reaction
+ + 4 ferricytochrome c = + 4 ferrocytochrome c + 5 H+
Synonyms
EC 1.7.3.4, HAO, haoA, HCR, HOA, hydroxylamine cytochrome c554 oxidoreductase, hydroxylamine oxidase, hydroxylamine oxidoreductase, hydroxylamine-cytochrome c reductase, hydroxylamine:oxygen oxidoreductase, mHAO, NeHAO, NirK, NoHAO
ECTree
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Subunits
Subunits on EC 1.7.2.6 - hydroxylamine dehydrogenase
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dimer
hexamer
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3 * 63000 + 3 * 11000, (alpha,beta)3 subunit structure, SDS-PAGE, 200000 MW enzyme forms a 63000 MW monomer after heme removal, hydroxylamine oxidoreductase probably consists of 3 molecules of monoheme c-type cytochrome with a MW of 11000 and 3 tightly complexed molecules of a catalytically active MW 63000 protein containing 6 c-type hemes and one P-460 heme, SDS-PAGE
homotrimer
oligomer
trimer
additional information
dimer
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hypothesis that the enzyme is functionally a dimer in which electrons rapidly equilibrate between the c-hemes of each subunit but not between oligomers
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alpha2 or alpha3 oligomeric structure with a subunit of 63 kDa, SDS-PAGE
the enzyme is composed of a homotrimer of subunits with molecular weight of 62000 Da covalently bound to each other. The bonds are mediated by prosthetic heme c molecules
additional information
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the enzyme is composed of a homotrimer of subunits with molecular weight of 62000 Da covalently bound to each other. The bonds are mediated by prosthetic heme c molecules
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