Literature summary for 1.11.1.24 extracted from

Park, J.W.; Piszczek, G.; Rhee, S.G.; Chock, P.B.
Glutathionylation of peroxiredoxin I induces decamer to dimers dissociation with concomitant loss of chaperone activity (2011), Biochemistry, 50, 3204-3210.

Search for more literature for 1.11.1.24

Cloned(Commentary)

Cloned (Comment)	Organism
expression in Escherichia coli	Homo sapiens

Protein Variants

Protein Variants	Comment	Organism
C52S/C173S	glutathionylation of isoform PrxI wild-type or its C52S/C173S double mutant shifts its oligomeric status from decamers to a population consisting mainly of dimers. Glutathionylation of both the wild-type and C52S/C173S mutant greatly reduces their molecular chaperone activity in protecting citrate synthase from thermally induced aggregation	Homo sapiens
C83S	residue Cys83 is not essential for the formation of high molecular weight complexes, it affects the dimer/decamer equilibrium. Glutathionylation of the C83S mutant leads to accumulation of dimers and monomers	Homo sapiens

Organism

Organism	UniProt	Comment	Textmining
Homo sapiens	-	-	-

Posttranslational Modification

Posttranslational Modification	Comment	Organism
additional information	glutathionylation of isoform PrxI wild-type or its C52S/C173S double mutant shifts its oligomeric status from decamers to a population consisting mainly of dimers. Glutathionylation of both the wild-type and C52S/C173S mutant greatly reduces their molecular chaperone activity in protecting citrate synthase from thermally induced aggregation	Homo sapiens

Subunits

Subunits	Comment	Organism
More	glutathionylation of isoform PrxI wild-type or its C52S/C173S double mutant shifts its oligomeric status from decamers to a population consisting mainly of dimers. Glutathionylation of both the wild-type and C52S/C173S mutant greatly reduces their molecular chaperone activity in protecting citrate synthase from thermally induced aggregation	Homo sapiens

Synonyms

Synonyms	Comment	Organism
Prx1	-	Homo sapiens

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Release 2023.1 (January 2023)