1.11.1.26: NADH-dependent peroxiredoxin
This is an abbreviated version!
For detailed information about NADH-dependent peroxiredoxin, go to the full flat file.
Word Map on EC 1.11.1.26
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1.11.1.26
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peroxiredoxins
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pylori
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helicobacter
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dismutases
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ahpcf
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vancomycin-resistant
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microaerophilic
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thioredoxin-like
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medicine
- 1.11.1.26
- peroxiredoxins
- pylori
-
helicobacter
- dismutases
-
ahpcf
-
vancomycin-resistant
-
microaerophilic
-
thioredoxin-like
- medicine
Reaction
Synonyms
AhpC, AhpC1, AhpCF, AhpF, AhpR, alkyl hydroperoxidase, alkyl hydroperoxide reductase, alkyl hydroperoxide reductase subunit C, alkyl hydroperoxide reductase subunit F, alkyl-hydroperoxide reductase C1, alkylhydroperoxide reductase, alkylhydroperoxide reductase subunit C, EC 1.11.1.15, FTL_1015, FTT_0557, NADH peroxidase, NADH peroxidase alkyl hydroperoxide reductase, peroxiredoxin C, Prx
ECTree
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Subunits
Subunits on EC 1.11.1.26 - NADH-dependent peroxiredoxin
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decamer
dimer
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the redox state of AhpC is a key factor determining the dimer-decamer equilibrium. at 25 °C exists predominantly as a decamer
multimer
oligomer
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heat induces oligomerization of AhpC. At 53°C the oxidized AhpC forms an high-molecular-weight oligomer with a molecular mass of about 2.0-3.0 MDa, corresponding to 100-150 subunits
decamer
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the redox state of AhpC is a key factor determining the dimer-decamer equilibrium. at 25 °C exists predominantly as a decamer