2. Academic Validation
  3. Laccase Properties, Physiological Functions, and Evolution

Laccase Properties, Physiological Functions, and Evolution

  • Int J Mol Sci. 2020 Jan 31;21(3):966. doi: 10.3390/ijms21030966.
Grzegorz Janusz 1,  Anna Pawlik 1,  Urszula Świderska-Burek 2,  Jolanta Polak 1,  Justyna Sulej 1,  Anna Jarosz-Wilkołazka 1,  Andrzej Paszczyński 3
Affiliations

Affiliations

  • 1 Department of Biochemistry and Biotechnology, Maria Curie-Skłodowska University, Akademicka 19 Street, 20-033 Lublin, Poland.
  • 2 Department of Botany, Mycology and Ecology, Maria Curie-Skłodowska University, Akademicka 19 Street, 20-033 Lublin, Poland.
  • 3 Professor Emeritus, School of Food Science, University of Idaho, Moscow, ID 83844, USA.
PMID: 32024019 DOI: 10.3390/ijms21030966
Abstract

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.

Keywords

evolution; function; laccase; lignin; melanin; multicopper oxidase; polyphenol oxidase.

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