Because the binding of phenolic compounds to the cell wall is mediated by peroxidases and, during plant-pathogen interactions, this binding occurs at the expense of a massive generation of H2O2 [ 27], we monitored peroxidase activity.
P. australis is also capable of degrading organo-chlorine compounds such as DDT and polychlorinated biphenyls (PCBs), which is partially mediated by enzymes like peroxidase and plant P-450 system (Chu et al. 2006).
The removal of H2O2 in cells is mediated by catalase (CAT), glutathione peroxidase and peroxiredoxin (PRDX) [ 73].
The active site architecture of Leishmania major peroxidase (LmP) is very similar with both cytochrome c peroxidase and ascorbate peroxidase.
Catalase-peroxidases (KatGs) exhibit peroxidase and substantial catalase activities similar to monofunctional catalases.
It is comprised of seven families with the chordata peroxidases forming the latest evolutionary descendants including thyroid peroxidase, lactoperoxidase (LPO), eosinophil peroxidase and myeloperoxidase (MPO).
Enzyme activities for lignin peroxidase, versatile peroxidase and dye-decolorizing peroxidase were not detected under the culturing conditions employed.
Cytosolic glutathione peroxidase and catalase activities are 42 and 153% of control values, respectively.
Similar to other heme-peroxidases such cytochrome c peroxidase and horseradish peroxidase, the catalytic cycle of LiP and MnP have three reactions [32,36 39].
The released H2O2 can activate the lignin peroxidases, manganese peroxidase and versatile peroxidase, which in turn are able to oxidize the lignin components in the plant cell wall.
