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Literature summary 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 .
    View publication on PubMed

Cloned(Commentary)

EC Number Cloned (Comment) Organism
1.11.1.24
-
Populus trichocarpa
1.11.1.25
-
Populus trichocarpa

Protein Variants

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

Organism

EC Number Organism UniProt Comment Textmining
1.11.1.24 Populus trichocarpa A9PCL4
-
-
1.11.1.25 Populus trichocarpa A9PCL4
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
1.11.1.24
-
Populus trichocarpa
1.11.1.25
-
Populus trichocarpa

Source Tissue

EC Number Source Tissue Comment Organism Textmining

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.11.1.24 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
-
?
1.11.1.25 glutaredoxin + H2O2 peroxiredoxin Cys51 and glutaredoxin Cys27 are involved in the catalytic mechanism. The enzyme also accepts thioredoxin as electron donor Populus trichocarpa glutaredoxin disulfide + 2 H2O
-
?