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Literature summary extracted from

  • Smeets, A.; Marchand, C.; Linard, D.; Knoops, B.; Declercq, J.P.
    The crystal structures of oxidized forms of human peroxiredoxin 5 with an intramolecular disulfide bond confirm the proposed enzymatic mechanism for atypical 2-Cys peroxiredoxins (2008), Arch. Biochem. Biophys., 477, 98-104.
    View publication on PubMed

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
1.11.1.24 the C72S mutant is crystallized by hanging drop vapour diffusion method with sodium cacodylate 0.1 M pH 6.5, PEG8000 20% (w/v), sodium acetate 0.1 M, and 6-aminocaproic acid 3% (w/v), at 18°C Homo sapiens

Protein Variants

EC Number Protein Variants Comment Organism
1.11.1.24 C72S the C72S mutation improves the crystallization in oxidizing conditions Homo sapiens

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
1.11.1.24 benzoate in orthorhombic 1 form, the benzoate ion is present close to the Cp residue in both fully folded subunits the benzoate ion is not observed in the six oxidized subunits in which the disulfide bond is formed Homo sapiens

Organism

EC Number Organism UniProt Comment Textmining
1.11.1.24 Homo sapiens P30044
-
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.11.1.24 H2O2 + reduced thioredoxin
-
Homo sapiens H2O + oxidized thioredoxin
-
?

Synonyms

EC Number Synonyms Comment Organism
1.11.1.24 peroxiredoxin 5 classified in the atypical 2-Cys subfamily, the oxidized form of the enzyme is characterized by the presence of an intramolecular disulfide bridge between the peroxidatic and the resolving cysteine residues Homo sapiens
1.11.1.24 PRDX5
-
Homo sapiens

Cofactor

EC Number Cofactor Comment Organism Structure
1.11.1.24 thioredoxin
-
Homo sapiens