Characterization of a novel DyP-type peroxidase from Streptomyces avermitilis
| Autor: | Tomomi Narioka, Mifumi Morita, Toru Yoshida, Yasushi Sugano, Kanako Sugawara, Yuriko Nishihashi |
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| Rok vydání: | 2016 |
| Předmět: |
0301 basic medicine
Bioengineering Anthraquinones Heme Applied Microbiology and Biotechnology Anthraquinone Cofactor Substrate Specificity 03 medical and health sciences chemistry.chemical_compound Enzyme Stability Enzyme kinetics Amino Acid Sequence Coloring Agents Peroxidase chemistry.chemical_classification ABTS biology Hydrogen-Ion Concentration biology.organism_classification Streptomyces Kinetics 030104 developmental biology Enzyme chemistry Biochemistry biology.protein Streptomyces avermitilis Oxidation-Reduction Sequence Alignment Biotechnology |
| Zdroj: | Journal of bioscience and bioengineering. 123(4) |
| ISSN: | 1347-4421 |
| Popis: | DyP-type peroxidases are a heme peroxidase family with unique properties whose members are widely distributed from prokaryotes to eukaryotes. DyP-type peroxidases are subdivided into class P, I and V based on structure-based sequence alignment. Class V enzymes possess degradation activities for anthraquinone dyes, and include extra sequences compared with class P and I. Class V enzymes are mainly found in fungi, with only two such proteins, AnaPX and DyP2, reported in bacteria. Here, we heterologously expressed, purified and biochemically characterized SaDyP2 protein, predicted to belong to class V. SaDyP2 was purified as a ∼50 kDa enzyme containing a heme cofactor and was found to oxidize the typical peroxidase substrates, ABTS and DMP. SaDyP2 was generally thermostable and exhibited a lower optimal pH, a feature typical of DyP-type peroxidases. It also degraded anthraquinone dyes, a specific substrate of DyP-type peroxidases, although the kcat for SaDyP2 was lower than that for other class V enzymes. The Km value of SaDyP2 for anthraquinone dye was similar to that of other enzymes of this class. Homology modeling revealed that the structure of SaDyP2 best fit that of class V enzymes. |
| Databáze: | OpenAIRE |
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