Laccase Properties, Physiological Functions, and Evolution

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 multicop...

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Published inInternational journal of molecular sciences Vol. 21; no. 3; p. 966
Main Authors Janusz, Grzegorz, Pawlik, Anna, Świderska-Burek, Urszula, Polak, Jolanta, Sulej, Justyna, Jarosz-Wilkołazka, Anna, Paszczyński, Andrzej
Format Journal Article
LanguageEnglish
Published Switzerland MDPI AG 31.01.2020
MDPI
Subjects
Bacteria
Enzymes
Fungi
Genes
Insects
Lignin
Molecular weight
Polymerization
Proteins
Review
laccase
melanin
function
lignin
polyphenol oxidase
evolution
multicopper oxidase
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Summary: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.
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ISSN:1422-0067
1661-6596
1422-0067
DOI:10.3390/ijms21030966