Characterization of Class V DyP-Type Peroxidase SaDyP1 from Streptomyces avermitilis and Evaluation of SaDyPs Expression in Mycelium |
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| Authors: | Kanako Sugawara Toru Yoshida Rena Hirashima Ryoko Toriumi Hotaka Akiyama Yurika Kakuta Yuki Ishige Yasushi Sugano |
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| Affiliation: | 1.Department of Chemical and Biological Sciences, Faculty of Science, Japan Women’s University, 2-8-1 Mejirodai, Bunkyo-Ku, Tokyo 112-8681, Japan; (K.S.); (T.Y.); (R.H.); (R.T.); (H.A.); (Y.K.); (Y.I.);2.Department of Clinical Laboratory Sciences, Faculty of Health Sciences, Nihon Institute of Medical Science, 1276 Shimogawara, Moroyamamachi, Irumagun, Saitama 350-0435, Japan |
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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. |
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| Keywords: | heme peroxidase dye-decolorizing peroxidase DyP-type peroxidase Streptomyces |
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