Abstract
Peroxidase enzymes can oxidize a multitude of substrates in diverse biological processes. According to the latest phylogenetic analysis, there are four major heme peroxidase superfamilies. In this review, we focus on certain members of the cyclooxygenase-peroxidase superfamily (also labeled as animal heme peroxidases) and their connection to specific NADPH oxidase enzymes which provide H2O2 for the one- and two-electron oxidation of various peroxidase substrates. The family of NADPH oxidases is a group of enzymes dedicated to the production of superoxide and hydrogen peroxide. There is a handful of known and important physiological functions where one of the seven known human NADPH oxidases plays an essential role. In most of these functions NADPH oxidases provide H2O2 for specific heme peroxidases and the concerted action of the two enzymes is indispensable for the accomplishment of the biological function. We discuss human and other metazoan examples of such cooperation between oxidases and peroxidases and analyze the biological importance of their functional interaction. We also review those oxidases and peroxidases where this kind of partnership has not been identified yet.
Highlights
Heme peroxidases comprise a large number of heme-containing proteins
The eosinophil peroxidase (EPO) and myeloperoxidase are highly homologous at the amino acid level their biochemical properties and biological role differ significantly
Coimmunoprecipitation studies revealed a molecular interaction between thyroid peroxidase (TPO) and dual oxidase 2 (Duox2) in the membrane fractions of isolated thyroid tissue lysates and of transfected COS-7 cells as well [47]
Summary
Heme peroxidases comprise a large number of heme-containing proteins. Families of these enzymes display distinct structural and biochemical properties and play a role in highly specialized biological processes. The numerous members of each of these families are expressed in all different kingdoms of life. It had been recently suggested that the denomination of heme peroxidases should happen according to their characteristic enzymatic activities and structural properties instead of their animal, plant or fungal origin [1]. The unique feature of the peroxidase-cyclooxygenase superfamily is the presence of a post-translationally modified heme group which is covalently linked to the peroxidase protein via two covalent bonds [2]. Myeloperoxidase (MPO) is unique in this superfamily because of having three covalent linkages to the heme group
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