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Characterization of a New DyP-Peroxidase from the Alkaliphilic Cellulomonad, Cellulomonas bogoriensis

Molecular Enzymology, Groningen Biomolecular Sciences and Biotechnology Institute, University of Groningen, Nijenborgh 4, 9747AG Groningen, The Netherlands
Department of Microbiology and Immunology, Faculty of Pharmacy, Cairo University, Kasr El Aini 11562, Cairo, Egypt
Author to whom correspondence should be addressed.
Molecules 2019, 24(7), 1208;
Received: 7 March 2019 / Revised: 23 March 2019 / Accepted: 25 March 2019 / Published: 27 March 2019
(This article belongs to the Special Issue Biocatalysis in Organic Synthesis)
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DyP-type peroxidases are heme-containing enzymes that have received increasing attention over recent years with regards to their potential as biocatalysts. A novel DyP-type peroxidase (CboDyP) was discovered from the alkaliphilic cellulomonad, Cellulomonas bogoriensis, which could be overexpressed in Escherichia coli. The biochemical characterization of the recombinant enzyme showed that it is a heme-containing enzyme capable to act as a peroxidase on several dyes. With the tested substrates, the enzyme is most active at acidic pH values and is quite tolerant towards solvents. The crystal structure of CboDyP was solved which revealed atomic details of the dimeric heme-containing enzyme. A peculiar feature of CboDyP is the presence of a glutamate in the active site which in most other DyPs is an aspartate, being part of the DyP-typifying sequence motif GXXDG. The E201D CboDyP mutant was prepared and analyzed which revealed that the mutant enzyme shows a significantly higher activity on several dyes when compared with the wild-type enzyme. View Full-Text
Keywords: biocatalysis; protein structure; peroxidases; signal sequence; structure-inspired mutagenesis biocatalysis; protein structure; peroxidases; signal sequence; structure-inspired mutagenesis

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Habib, M.H.; Rozeboom, H.J.; Fraaije, M.W. Characterization of a New DyP-Peroxidase from the Alkaliphilic Cellulomonad, Cellulomonas bogoriensis. Molecules 2019, 24, 1208.

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