Abstract
Heme peroxidases contain the well-known heme b as prosthetic group and use hydrogen peroxide as electron acceptor to catalyze the oxidation of a large number of substrates [1]. On the basis of sequence homology they can be categorized into two super-families (I and II) and are present in (I) bacteria, fungi, plants, and (II) animals [2, 3]. The superfamily of animal peroxidases includes myeloperoxidase (MPO), eosinophil peroxidase (EPO), lactoperoxidase (LPO), thyroid peroxidase (TPO), and prostaglandin-endoperoxide synthase (PGHS). These proteins are related members of the same gene superfamily (Table 15.1). The phylogenetic tree of these related members of animal peroxidases, as derived from ProtoMap [4] on the basis of known sequences, predicts some distinguishing divergences among members of the superfamily (Table 15.2).
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