Catalase‐Peroxidase:KatG

Abstract

Even in the absence of the catalase fold , an efficient catalase activity is also found in the heme‐containing catalase‐peroxidase proteins. The structure of these broad substrate range enzymes, reported for the first time less than 10 years ago from the halophilic archaebacterium Haloarcula marismortui ( HmKatG ) and from the bacterium Burkholderia pseudomallei ( BpKatG ), and more recently, from the eukaryotic fungus Magnaporthe grisea ( MgKatG ), showed a heme pocket closely related to that of plant peroxidases, although with a number of unique modifications that enable the catalase reaction.

The catalase‐peroxidase PiCP1 plays a critical role in abiotic stress resistance, pathogenicity and asexual structure development in Phytophthora infestans

“…Catalase‐peroxidases have both the catalase activity and the peroxidase activity, which can convert H 2 O 2 into H 2 O (in peroxidases) or into O 2 and H 2 O (in catalases) (Tehrani & Moosavi‐Movahedi, 2018). Of the two catalytic activities, the catalase activity is the predominant one (Fita et al, 2015). Together with superoxide dismutase and glutathione peroxidase, catalase plays a vital role in the antioxidant system that protect cells against the adverse effects of free radicals (Blackman & Hardham, 2008; Ighodaro & Akinloye, 2018).…”