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DyP-Type Peroxidases: Recent Advances and Perspectives
Yasushi Sugano1, Toru Yoshida1
1Department of Chemical and Biological Sciences, Faculty of Science, Japan Women's University, Tokyo 112-8681, Japan.
International Journal of Molecular Sciences
|June 2, 2021
Summary
The DyP-type peroxidase family, found in bacteria and fungi, shows diverse structures and functions beyond simple peroxidase activity. Research highlights their unique roles in iron transport and lignin degradation.
Area of Science:
- Biochemistry
- Enzymology
- Molecular Biology
Background:
- DyP-type peroxidases are a diverse enzyme family primarily found in bacteria and fungi.
- Recent research has uncovered their widespread distribution and varied structural features.
Purpose of the Study:
- To review research progress on DyP-type peroxidases over the past decade.
- To highlight their structural diversity, catalytic mechanisms, and diverse physiological roles.
Main Methods:
- Tertiary structural analyses of DyP-type peroxidases.
- Review of literature on their enzymatic activities and cellular functions.
- Comparison with other heme peroxidases.
Main Results:
- DyP-type peroxidases exhibit unique catalytic cycles distinct from other heme peroxidases.
- They possess additional hydrolase or oxidase activities and varied cellular localization.
- Key roles identified in Streptomyces life-cycle switching and iron transport systems in bacteria.
Conclusions:
- The DyP-type peroxidase family is a rich source of diverse enzymes with significant research potential.
- Their functions extend beyond lignin degradation, including environmental roles like degrading anthraquinones.
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