Download MendeleyCharacterization of a New DyP-Peroxidase from the Alkaliphilic Cellulomonad, Cellulomonas bogoriensis.
Habib, M.H., Rozeboom, H.J., Fraaije, M.W.(2019) Molecules 24
- PubMed: 30934796
- DOI: https://doi.org/10.3390/molecules24071208
- Primary Citation of Related Structures:
6QZO - PubMed Abstract:
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 ( Cbo DyP) 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 Cbo DyP was solved which revealed atomic details of the dimeric heme-containing enzyme. A peculiar feature of Cbo DyP 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 Cbo DyP 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.
Organizational Affiliation:
Molecular Enzymology, Groningen Biomolecular Sciences and Biotechnology Institute, University of Groningen, Nijenborgh 4, 9747AG Groningen, The Netherlands. m.habib@rug.nl.
