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Literature summary for 1.11.1.26 extracted from

  • Logan, C.; Mayhew, S.G.
    Cloning, overexpression, and characterization of peroxiredoxin and NADH peroxiredoxin reductase from Thermus aquaticus (2000), J. Biol. Chem., 275, 30019-30028.
    View publication on PubMed
Search for more literature for 1.11.1.26

Cloned(Commentary)

Cloned (Comment) Organism
-
 Thermus aquaticus

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
21000
-
 x * 21000, SDS-PAGE Thermus aquaticus
235000
-
 gel filtration Thermus aquaticus

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
additional information Thermus aquaticus peroxiredoxin and NADH:peroxiredoxin oxidoreductase together catalyze the anaerobic reduction of H2O2 ?
-
 ?
additional information Thermus aquaticus YT-1 peroxiredoxin and NADH:peroxiredoxin oxidoreductase together catalyze the anaerobic reduction of H2O2 ?
-
 ?

Organism

Organism UniProt Comment Textmining
Thermus aquaticus
-
 YT-1
-
Thermus aquaticus YT-1
-
 YT-1
-

Purification (Commentary)

Purification (Comment) Organism
-
 Thermus aquaticus

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
additional information peroxiredoxin and NADH:peroxiredoxin oxidoreductase together catalyze the anaerobic reduction of H2O2 Thermus aquaticus ?
-
 ?
additional information peroxiredoxin and NADH:peroxiredoxin oxidoreductase together catalyze the anaerobic reduction of H2O2 Thermus aquaticus YT-1 ?
-
 ?

Subunits

Subunits Comment Organism
multimer x * 21000, SDS-PAGE Thermus aquaticus

Synonyms

Synonyms Comment Organism
Prx
-
 Thermus aquaticus