Cited by 1,007Enzyme-mediated dye degradationMetal-Catalyzed Oxygenation MechanismsEnzyme Catalysis and Immobilization

Laccases: a never-ending story

Open access
Giardina, Paola, Faraco, Vincenza, Pezzella, Cinzia, Piscitelli, Alessandra, Vanhulle, Sophie, Sannia, Giovanni·2010·Cellular and Molecular Life Sciences

Abstract

Laccases (benzenediol:oxygen oxidoreductases, EC 1.10.3.2) are blue multicopper oxidases that catalyze the oxidation of an array of aromatic substrates concomitantly with the reduction of molecular oxygen to water. In fungi, laccases carry out a variety of physiological roles during their life cycle. These enzymes are being increasingly evaluated for a variety of biotechnological applications due to their broad substrate range. In this review, the most recent studies on laccase structural features and catalytic mechanisms along with analyses of their expression are reported and examined with the aim of contributing to the discussion on their structure-function relationships. Attention has also been paid to the properties of enzymes endowed with unique characteristics and to fungal laccase multigene families and their organization.

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Crossref · 10.1007/s00018-009-0169-1

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1 of 1 references verified0 citation errors · 0 not checkable

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  • The variations in the redox potential of CuT1 observed among laccases cannot be attributed to a single structural characteristic; it is the sum of factors such as CuT1 coordination geometry and the nature of the waste that influence solvent accessibility, hydrogen bonds and dielectric anisotropy.

    “Overall, the variations in the redox potential of CuT1 observed among laccases cannot be attributed to a single structural characteristic; it is the sum of factors such as the CuT1 coordination geometry and the nature of the waste that influence the accessibility of the solvent, the hydrogen bonds and the dielectric anisotropy [199].”

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Authors
Giardina, P., Faraco, V., Pezzella, C., Piscitelli, A., Vanhulle, S., & Sannia, G.
Affiliations
  • University of Naples Federico II (IT)
  • UCLouvain (BE)
Corresponding author
Giardina, Paola
Venue
Cellular and Molecular Life Sciences
Published
2009-10-22
Volume
67
Issue
3
Pages
369-385
ISSN
  • 1420-682X (ISSN-L)
  • 1420-9071
OpenAlex
W1996350754
Cited by
1,007
References
1
Citations by year
2026: 31 · 2025: 54 · 2024: 62 · 2023: 70 · 2022: 74 · 2021: 79 · 2020: 70 · 2019: 86 · 2018: 49 · 2017: 59 · 2016: 69 · 2015: 81 · 2014: 60 · 2013: 53 · 2012: 47
FWCI
3.14
Type
journal article
Language
en
Open access
Locations
  • Cellular and Molecular Life Sciences (publishedVersion)
  • PubMed Central (publishedVersion)
  • PubMed (publishedVersion)
  • Digital Access to Libraries (submittedVersion)
Funders
Ministero dell'Università e della Ricerca
Topics
  • Life Sciences › Agricultural and Biological Sciences › Plant Science › Enzyme-mediated dye degradation
  • Physical Sciences › Chemistry › Inorganic Chemistry › Metal-Catalyzed Oxygenation Mechanisms
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Enzyme Catalysis and Immobilization
Keywords
laccase, fungal laccase
MeSH terms
Amino Acid Sequence, Copper, Fungi, Molecular Sequence Data, Oxidation-Reduction, Structure-Activity Relationship, Sequence Alignment, Sequence Homology, Amino Acid, Catalytic Domain, Laccase

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