Enzyme Engineering
Open Access

Abstract

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.