https://pure.rug.nl/ws/files/49577911/Bacterial_enzymes_involved_in_lignin_degradation.pdf

Bacterial enzymes involved in lignin degradation.

DyP peroxidases comprise a novel superfamily of heme-containing peroxidases, which is unrelated to the superfamilies of plant and animal peroxidases. These enzymes have so far been identified in the genomes of fungi, bacteria, as well as archaea, although their physiological function is still unclear. DyPs are bifunctional enzymes displaying not only oxidative activity but also hydrolytic activity. Moreover, these enzymes are able to oxidize a variety of organic compounds of which some are poorly converted by established peroxidases, including dyes, β-carotene, and aromatic sulfides. Interestingly, accumulating evidence shows that microbial DyP peroxidases play a key role in the degradation of lignin. Owing to their unique properties, these enzymes are potentially interesting for a variety of biocatalytic applications. In this review, we deal with the biochemical and structural features of DyP-type peroxidases as well as their promising biotechnological potential.

/pdf/dyp-type-peroxidases-a-promising-and-versatile-class-of-2cos612hza.pdf

DyP‑type peroxidases: a promising and versatile class of enzymes

https://www.pure.ed.ac.uk/ws/files/19850465/1_s2.0_S1871678414022067_main.pdf

Ferritin family proteins and their use in bionanotechnology

Cells organize and regulate their metabolism via membrane- or protein-bound organelles. In this way, incompatible processes can be spatially separated and controlled. In prokaryotes, protein-based compartments are used to sequester harmful reactions and store useful compounds. These protein compartments play key roles in various metabolic and ecological processes, ranging from iron homeostasis to carbon fixation. One of the newest types of protein organelle are encapsulin nanocompartments. They are able to encapsulate specific protein cargo and are proposed to be involved in redox-related processes. We identified more than 900 putative encapsulin systems in bacterial and archaeal genomes. Encapsulins can be found in fifteen bacterial and two archaeal phyla. Our analysis reveals one new capsid type and nine previously unknown cargo proteins targeted to the interior of encapsulins. We experimentally characterize three newly identified encapsulin systems and illustrate their probable involvement in iron mineralization, oxidative and nitrosative stress resistance and anaerobic ammonium oxidation, a process responsible for 30% of the nitrogen lost from the oceans. Bioinformatics analysis identifies 900 encapsulin nanocompartments in prokaryotes that are associated with cargo proteins carrying out diverse functions.

Vincent P. Le

Papers

Characterization of a Mycobacterium tuberculosis Nanocompartment and Its Potential Cargo Proteins