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Abstract
DyP-type peroxidases are a family of heme peroxidases named for their ability to degrade persistent anthraquinone dyes. DyP-type peroxidases are subclassified into three classes: classes P, I and V. Based on its genome sequence, Streptomyces avermitilis, eubacteria, has two genes presumed to encode class V DyP-type peroxidases and two class I genes. We have previously shown that ectopically expressed SaDyP2, a member of class V, indeed has the characteristics of a DyP-type peroxidase. In this study, we analyzed SaDyP1, a member of the same class V as SaDyP2. SaDyP1 showed high amino acid sequence identity to SaDyP2, retaining a conserved GXXDG motif and catalytic aspartate. SaDyP1 degraded anthraquinone dyes, which are specific substrates of DyP-type peroxidases but not azo dyes. In addition to such substrate specificity, SaDyP1 showed other features of DyP-type peroxidases, such as low optimal pH. Furthermore, immunoblotting using an anti-SaDyP2 polyclonal antibody revealed that SaDyP1 and/or SaDyP2 is expressed in mycelia of wild-type S. avermitilis.
Highlights
Using ectopic expression and biochemical characterization, we previously showed that SaDyP2, encoded by SavDyPrx03-2, has features of a Dye-decolorizing peroxidase (DyP)-type peroxidase
Whole-genome sequencing showed that S. avermitilis has four candidate DyP-type peroxidase genes [26]
DyP,than which belongs which belongs the same. These results indicate thattoSaDyP1 class to the same class Vto[33]
Summary
Heme peroxidases are conserved among almost all organisms and catalyze various oxidative reactions using hydrogen peroxide as an electron acceptor They are present in both prokaryotes and eukaryotes and are classified by the peroxidase and oxide-reductase database RedoxiBase (https://peroxibase.toulouse.inra.fr/, accessed on 20 July 2021) into six groups [1,2]: catalases, haloperoxidases, di-heme cytochrome c peroxidases, animal peroxidases, non-animal peroxidases (previously called plant peroxidase [3]) and DyP-type peroxidases. DyP differs from existing heme peroxidases in terms of amino acid sequence, tertiary structure, substrate specificity, catalytic residues and optimum pH. For these reasons, it was originally considered an exceptional peroxidase. DyP and a series of genes phylogenetically similar to DyP were proposed to constitute a novel heme peroxidase family, the DyP-type peroxidase because many genes similar to DyP were found, and for those cases in which the corresponding protein has been purified, their biochemical characterizations have been revealed similar to those of DyP [6,7]
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