Catalase proper is widespread in both prokaryotes and eukaryotes, including nearly all groups. It has been studied as an activity for over 125 years and as a blood and liver protein since the mid-nineteen thirties. Its mechanism of action is fairly well understood (see Nicholls, P. (2012) Classical catalase: ancient and modern. Arch. Biochem. Biophys. 525, 95-101).
Although also a haem enzyme catalase-peroxidase is not found in mammals and is confined to prokaryotes and a few fungi. There is no homology between the two catalase types. Catalase-peroxidases have a somewhat lower catalase activity and a mechanism different from that of 'classical' catalases. But as the name indicates they have higher peroxidase activity than the classical enzyme family. The clinically significant catalase-peroxidase is the Mycobacterium tuberculosis enzyme that oxidizes the tuberculosis drug isoniazid.
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