Chapter 14: Structure and Reactivity of the Dye-decolorizing Peroxidase (DyP) Family
Published:26 Oct 2015
The dye-decolorizing peroxidases are a recently discovered family of bacterial and fungal peroxidases that are structurally unrelated to the previously studied mammalian and plant peroxidases, but show novel reactivity for oxidation of anthraquinone dyes, phenolic substrates, Mn(ii) and in some cases polymeric lignin. The chapter discusses the discovery of this family of peroxidases, their classification into four sub-families via phylogenetic analysis, and the crystal structures of members of each sub-family. The reactivity of each sub-family is discussed, and the catalytic mechanism of the DyP peroxidases, which differ from conventional peroxidases in having an active site aspartic acid as a proton donor, in place of histidine. Possible applications of the novel reactivities of the DyP enzymes are discussed.