Abstract
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.
Highlights
In most cases, dye decolorizing peroxidase (DyP)-type peroxidases show typical peroxidase activity, such as that shown by horseradish peroxidase (HRP)
DyP-type peroxidases show a broad range of substrate specificities, and several active sites have been proposed [31,43,49,65]
In 2009, Létoffé et al reported that EfeB, a DyP-type peroxidase from Escherichia coli, functions as a deferrochelatase [70]
Summary
Publisher’s Note: MDPI stays neutral with regard to jurisdictional claims in published maps and institutional affiliations. DyP-type peroxidases have been found in a variety of organisms (Figure 1) These enzymes exhibit a varied distribution, functioning inside and outside of cells. Reside in the periplasmic space and outside of the cell, respectively They are homologs of each other and are inferred to play similar physiological roles [8,11]. Secreted DyP-type peroxidases likely serve a function independent of removal of intracellular H2 O2 or construct the cell tissues. It appears that some DyP-type peroxidases exist as a cargo protein in encapsulin [12,13]. Research performed over the past decade has clarified the unique characteristics of DyP-type peroxidases, converging on the view that they do not exist solely to remove H2 O2 but instead have more important specific roles
Sign-in/Register to view highlights & summary Sign-in/Register to access full text options 
Talk to us
Join us for a 30 min session where you can share your feedback and ask us any queries you have
Schedule a call
