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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...
Autores principales: | , , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
MDPI
2020
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7036934/ https://www.ncbi.nlm.nih.gov/pubmed/32024019 http://dx.doi.org/10.3390/ijms21030966 |
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author | Janusz, Grzegorz Pawlik, Anna Świderska-Burek, Urszula Polak, Jolanta Sulej, Justyna Jarosz-Wilkołazka, Anna Paszczyński, Andrzej |
author_facet | Janusz, Grzegorz Pawlik, Anna Świderska-Burek, Urszula Polak, Jolanta Sulej, Justyna Jarosz-Wilkołazka, Anna Paszczyński, Andrzej |
author_sort | Janusz, Grzegorz |
collection | PubMed |
description | 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. |
format | Online Article Text |
id | pubmed-7036934 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2020 |
publisher | MDPI |
record_format | MEDLINE/PubMed |
spelling | pubmed-70369342020-03-11 Laccase Properties, Physiological Functions, and Evolution Janusz, Grzegorz Pawlik, Anna Świderska-Burek, Urszula Polak, Jolanta Sulej, Justyna Jarosz-Wilkołazka, Anna Paszczyński, Andrzej Int J Mol Sci Review 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. MDPI 2020-01-31 /pmc/articles/PMC7036934/ /pubmed/32024019 http://dx.doi.org/10.3390/ijms21030966 Text en © 2020 by the authors. Licensee MDPI, Basel, Switzerland. This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution (CC BY) license (http://creativecommons.org/licenses/by/4.0/). |
spellingShingle | Review Janusz, Grzegorz Pawlik, Anna Świderska-Burek, Urszula Polak, Jolanta Sulej, Justyna Jarosz-Wilkołazka, Anna Paszczyński, Andrzej Laccase Properties, Physiological Functions, and Evolution |
title | Laccase Properties, Physiological Functions, and Evolution |
title_full | Laccase Properties, Physiological Functions, and Evolution |
title_fullStr | Laccase Properties, Physiological Functions, and Evolution |
title_full_unstemmed | Laccase Properties, Physiological Functions, and Evolution |
title_short | Laccase Properties, Physiological Functions, and Evolution |
title_sort | laccase properties, physiological functions, and evolution |
topic | Review |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7036934/ https://www.ncbi.nlm.nih.gov/pubmed/32024019 http://dx.doi.org/10.3390/ijms21030966 |
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