reviewInternational Journal of Molecular SciencesJan 31, 2020GOLD OA

Laccase Properties, Physiological Functions, and Evolution

GJGrzegorz JanuszAPAnna PawlikUŚUrszula Świderska-BurekJPJolanta PolakJSJustyna Sulej

Maria Curie-Skłodowska University · University of Idaho

PubMed
Indexed incrossrefdoajpubmed

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…

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669
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FWCI
76.07
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100%
References
215
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Authors

7

Topics & keywords

Topics
Keywords
  • Laccase
  • Enzyme
  • Substrate specificity
  • Multicopper oxidase
  • Biology
  • SUPERFAMILY
  • Substrate (aquarium)
  • Function (biology)
UN Sustainable Development Goals
  • Clean water and sanitation
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