DyP-Type Peroxidases: Recent Advances and Perspectives

Autor: Toru Yoshida, Yasushi Sugano
Rok vydání: 2021
Předmět:
0301 basic medicine
Anthraquinones
Review
Bacillus subtilis
Lignin
chemistry.chemical_compound
life cycle
Biology (General)
Heme
Phylogeny
Spectroscopy
chemistry.chemical_classification
Oxidase test
biology
antifungal anthraquinone compounds
oxidase
General Medicine
Streptomyces
Computer Science Applications
Chemistry
Peroxidases
Biochemistry
DyP
structure-based sequence alignments
Oxidation-Reduction
Peroxidase
Staphylococcus aureus
QH301-705.5
Iron
Catalysis
Fungal Proteins
Inorganic Chemistry
03 medical and health sciences
Bacterial Proteins
Hydrolase
lignin degradation
Escherichia coli
encapsulin
DyP-type peroxidase
Physical and Theoretical Chemistry
QD1-999
Molecular Biology
030102 biochemistry & molecular biology
iron uptake
Organic Chemistry
Fungi
biology.organism_classification
nano compartment
cargo protein
030104 developmental biology
Enzyme
chemistry
biology.protein
hydrolase
Function (biology)
Zdroj: International Journal of Molecular Sciences
International Journal of Molecular Sciences, Vol 22, Iss 5556, p 5556 (2021)
ISSN: 1422-0067
Popis: In this review, we chart the major milestones in the research progress on the DyP-type peroxidase family over the past decade. Though mainly distributed among bacteria and fungi, this family actually exhibits more widespread diversity. Advanced tertiary structural analyses have revealed common and different features among members of this family. Notably, the catalytic cycle for the peroxidase activity of DyP-type peroxidases appears to be different from that of other ubiquitous heme peroxidases. DyP-type peroxidases have also been reported to possess activities in addition to peroxidase function, including hydrolase or oxidase activity. They also show various cellular distributions, functioning not only inside cells but also outside of cells. Some are also cargo proteins of encapsulin. Unique, noteworthy functions include a key role in life-cycle switching in Streptomyces and the operation of an iron transport system in Staphylococcus aureus, Bacillus subtilis and Escherichia coli. We also present several probable physiological roles of DyP-type peroxidases that reflect the widespread distribution and function of these enzymes. Lignin degradation is the most common function attributed to DyP-type peroxidases, but their activity is not high compared with that of standard lignin-degrading enzymes. From an environmental standpoint, degradation of natural antifungal anthraquinone compounds is a specific focus of DyP-type peroxidase research. Considered in its totality, the DyP-type peroxidase family offers a rich source of diverse and attractive materials for research scientists.
Databáze: OpenAIRE
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