DyP-Type Peroxidases: Recent Advances and Perspectives

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.

Evidence for Lignocellulose-Decomposing Enzymes in the Genome and Transcriptome of the Aquatic Hyphomycete Clavariopsis aquatica

“…This class also contains peroxidases known to be involved in lignin degradation in Basidiomycota such as LiP, MnP, and VP [4][5][6]. Other fungal heme peroxidases such as DyP-type peroxidases were also implicated in lignin degradation, although a possibly related function has not yet been finally clarified [61]. The peroxidases identified from the C. aquatica genome, however, are more similar to the Ascomycota class II family [62].…”

Functional and protective hole hopping in metalloenzymes

“…Enzymes known as dye-decolorizing peroxidases (DyPs) also utilize protein radicals for substrate reactions. 84 Although the natural substrates are difficult to identify, DyPs can oxidize high potential substrates and are of interest for their role in lignin degradation. Both bacterial and fungal enzymes contain much higher levels of Trp and Tyr in their amino acid sequences than LP and VP.…”

Dye Decoloring Peroxidase Structure, Catalytic Properties and Applications: Current Advancement and Futurity

“…Reactive Blue 5 and Reactive Blue 19 are typical structures of anthraquinone dye sand. BAD DyP can degrade Reactive Blue 5 by cleaving an anthraquinone framework [56,57]. A unique hydrolase mechanism has been proposed, which uses H 2 O released by peroxidase function to exert hydrolase activity during the degradation of anthrone (Figure 5A) [58].…”

“…The construction of a gene database and phylogenetic analysis revealed the omics relationship between DyPs, and gene functions have been elucidated. It indicated that the research on DyPs could reach a new stage using molecular biology [57,63]. DyPs can maintain a high activity in acidic conditions and tend to express high activity at an acidic pH to degrade lignin substrates.…”