Abstract
Four heme peroxidase superfamilies arose independently in evolution that differ in overall fold, active site architecture and enzymatic activities. The peroxidase-cyclooxygenase superfamily shows the highest diversity regarding domain architectures and composition. In contrast to other heme peroxidase (super)families, most of its members have the prosthetic heme group posttranslationally modified. This review focuses on the phylogeny and biochemistry of Family 1 (chordata peroxidases) and Family 2 (peroxidasins) representatives, including myeloperoxidase, eosinophil peroxidase, lactoperoxidase, thyroid peroxidase and peroxidasin 1. We discuss the relevant sequence motifs, overall structures and heme cavity architecture, and the impact of the autocatalytically formed covalent links on spectral and redox properties as well as on catalysis, including Compound I formation and Compound I reduction by one- and two-electron donors.
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