2020/01/31 by Grzegorz Janusz, Anna Pawlik, Urszula Świderska-Burek +4 · 3 citations
Agricultural and Biological Sciences · Biochemistry, Genetics and Molecular Biology · Chemistry · #Enzyme-mediated dye degradation #Microbial Metabolism and Applications #Metal-Catalyzed Oxygenation Mechanisms
paper · pdf · doi:10.3390/ijms21030966
openalex publication_date 2020/01/31 · openalex created_date 2025/10/10 · openalex updated_date 2026/07/31
Discovered in 1883, laccase is one of the first enzymes ever described. Now, after almost 140 years of research, it seems that this copper-containing protein with a number of unique catalytic properties is widely distributed across all kingdoms of life. Laccase belongs to the superfamily of multicopper oxidases (MCOs)-a group of enzymes comprising many proteins with different substrate specificities and diverse biological functions. The presence of cupredoxin-like domains allows all MCOs to reduce oxygen to water without producing harmful byproducts. This review describes structural characteristics and plausible evolution of laccase in different taxonomic groups. The remarkable catalytic abilities and broad substrate specificity of laccases are described in relation to other copper-containing MCOs. Through an exhaustive analysis of laccase roles in different taxa, we find that this enzyme evolved to serve an important, common, and protective function in living systems.