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
Online AccessGet full text
ISSN1422-0067
1661-6596
1422-0067
DOI10.3390/ijms21030966

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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.
AbstractList 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.
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.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.
Author Świderska-Burek, Urszula
Janusz, Grzegorz
Paszczyński, Andrzej
Pawlik, Anna
Jarosz-Wilkołazka, Anna
Sulej, Justyna
Polak, Jolanta
AuthorAffiliation 1 Department of Biochemistry and Biotechnology, Maria Curie-Skłodowska University, Akademicka 19 Street, 20-033 Lublin, Poland; anna.pawlik@poczta.umcs.lublin.pl (A.P.); jpolak@poczta.umcs.lublin.pl (J.P.); justyna.sulej@poczta.umcs.lublin.pl (J.S.); anna.wilkolazka@poczta.umcs.lublin.pl (A.J.-W.)
3 Professor Emeritus, School of Food Science, University of Idaho, Moscow, ID 83844, USA; andrzej@uidaho.edu
2 Department of Botany, Mycology and Ecology, Maria Curie-Skłodowska University, Akademicka 19 Street, 20-033 Lublin, Poland; urszula.swiderska-burek@poczta.umcs.lublin.pl
AuthorAffiliation_xml – name: 2 Department of Botany, Mycology and Ecology, Maria Curie-Skłodowska University, Akademicka 19 Street, 20-033 Lublin, Poland; urszula.swiderska-burek@poczta.umcs.lublin.pl
– name: 3 Professor Emeritus, School of Food Science, University of Idaho, Moscow, ID 83844, USA; andrzej@uidaho.edu
– name: 1 Department of Biochemistry and Biotechnology, Maria Curie-Skłodowska University, Akademicka 19 Street, 20-033 Lublin, Poland; anna.pawlik@poczta.umcs.lublin.pl (A.P.); jpolak@poczta.umcs.lublin.pl (J.P.); justyna.sulej@poczta.umcs.lublin.pl (J.S.); anna.wilkolazka@poczta.umcs.lublin.pl (A.J.-W.)
Author_xml – sequence: 1
  givenname: Grzegorz
  orcidid: 0000-0002-2046-2806
  surname: Janusz
  fullname: Janusz, Grzegorz
– sequence: 2
  givenname: Anna
  orcidid: 0000-0002-2991-758X
  surname: Pawlik
  fullname: Pawlik, Anna
– sequence: 3
  givenname: Urszula
  surname: Świderska-Burek
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  surname: Polak
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– sequence: 5
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  surname: Sulej
  fullname: Sulej, Justyna
– sequence: 6
  givenname: Anna
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– sequence: 7
  givenname: Andrzej
  surname: Paszczyński
  fullname: Paszczyński, Andrzej
BackLink https://www.ncbi.nlm.nih.gov/pubmed/32024019$$D View this record in MEDLINE/PubMed
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melanin
function
lignin
polyphenol oxidase
evolution
multicopper oxidase
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crossref_primary_10_3390_ijms21030966
ProviderPackageCode CITATION
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PublicationCentury 2000
PublicationDate 20200131
PublicationDateYYYYMMDD 2020-01-31
PublicationDate_xml – month: 1
  year: 2020
  text: 20200131
  day: 31
PublicationDecade 2020
PublicationPlace Switzerland
PublicationPlace_xml – name: Switzerland
– name: Basel
PublicationTitle International journal of molecular sciences
PublicationTitleAlternate Int J Mol Sci
PublicationYear 2020
Publisher MDPI AG
MDPI
Publisher_xml – name: MDPI AG
– name: MDPI
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Snippet 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...
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SubjectTerms Bacteria
Enzymes
Fungi
Genes
Insects
Lignin
Molecular weight
Polymerization
Proteins
Review
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Title Laccase Properties, Physiological Functions, and Evolution
URI https://www.ncbi.nlm.nih.gov/pubmed/32024019
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