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DyP-type Peroxidases: A Promising and Versatile Class of Enzymes

Marco W. Fraaije and Edwin van Bloois*

Peroxidases (EC1.11.1.x) represent a large family of oxidoreductases that typically use hydrogen peroxide as an electron acceptor to catalyze the oxidation of substrate molecules. The vast majority of these enzymes contain heme as a cofactor [1], and are ubiquitously present in prokaryotes and eukaryotes. Peroxidases take center stage in a variety of biochemical processes, ranging from the biosynthesis of cell wall material to immunological host-defense responses [2,3]. Hemecontaining peroxidases were originally classified into two superfamilies: the plant peroxidases and animal peroxidases [4]. Remarkably, some members of the peroxidase superfamily have been studied for more than a century like, for example, Horseradish Peroxidase (HRP) [5], and in this respect, it was highly fascinating that the first member of a newly discovered peroxidase superfamily, the group of DyP-type peroxidases, was described in the late 90’s [6]. Here, we will discuss the biochemical and structural features of DyP-type peroxidases, as well as their promising biotechnological potential.