Characterization of a novel DyP-type peroxidase from Streptomyces avermitilis

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 anth...

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Bibliographic Details
Published in:Journal of bioscience and bioengineering 2017-04, Vol.123 (4), p.425-430
Main Authors: Sugawara, Kanako, Nishihashi, Yuriko, Narioka, Tomomi, Yoshida, Toru, Morita, Mifumi, Sugano, Yasushi
Format: Article
Language:English
Subjects:
Amino Acid Sequence
Anthraquinone degradation
Anthraquinones - metabolism
Class V
Coloring Agents - metabolism
DyP-type peroxidase
Enzyme Stability
Heme - metabolism
Hydrogen-Ion Concentration
Kinetics
Oxidation-Reduction
Peroxidase - chemistry
Peroxidase - classification
Peroxidase - isolation & purification
Peroxidase - metabolism
Sequence Alignment
Streptomyces
Streptomyces - enzymology
Structure-based sequence alignment
Substrate Specificity
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Summary: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.
ISSN:1389-1723
1347-4421
DOI:10.1016/j.jbiosc.2016.12.001