Literature summary for 1.11.1.24 extracted from

Rouhier, N.; Gelhaye, E.; Jacquot, J.P.
Glutaredoxin-dependent peroxiredoxin from poplar protein-protein interaction and catalytic mechanism (2002), J. Biol. Chem., 277, 13609-13614 .

Search for more literature for 1.11.1.24

Cloned(Commentary)

Cloned (Comment)	Organism
-	Populus trichocarpa

Protein Variants

Protein Variants	Comment	Organism
C51A	mutation abolishes catalysis	Populus trichocarpa
C76A	mutant enzyme retains about 25% of the wild type peroxiredoxin activity	Populus trichocarpa
V152C	the mutant enzyme is inactive with glutaredoxin as a proton donor, it is catalytically active with thioredoxin	Populus trichocarpa

Organism

Organism	UniProt	Comment	Textmining
Populus trichocarpa	A9PCL4	-	-

Purification (Commentary)

Purification (Comment)	Organism
-	Populus trichocarpa

Source Tissue

Source Tissue	Comment	Organism	Textmining

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
thioredoxin + H2O2	peroxiredoxin Cys51 and glutaredoxin Cys27 are involved in the catalytic mechanism. The enzyme also accepts glutaredoxin as electron donor	Populus trichocarpa	thioredoxin disulfide + 2 H2O	-	?

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Release 2023.1 (January 2023)