Literature summary for 1.11.1.24 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.

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Crystallization (Commentary)

Crystallization (Comment)	Organism
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

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

Metals/Ions

Metals/Ions	Comment	Organism	Structure
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

Organism	UniProt	Comment	Textmining
Homo sapiens	P30044	-	-

Substrates and Products (Substrate)

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

Synonyms

Synonyms	Comment	Organism
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
PRDX5	-	Homo sapiens

Cofactor

Cofactor	Comment	Organism	Structure
thioredoxin	-	Homo sapiens

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Release 2023.1 (January 2023)