ReviewMolecules (Basel, Switzerland)2023
Laccase Engineering: Redox Potential Is Not the Only Activity-Determining Feature in the Metalloproteins.
Review in Molecules (Basel, Switzerland), 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
8 citing papers in PubMed, 24 citations in OpenAlex.
- Deciphering the Catalytic Mechanism of Oxidoreductase-Like Nanozymes Along the Reaction Pathway: Activity, Specificity and Sustainability.Advanced materials (Deerfield Beach, Fla.) · 2026Review
- Mechanistic and Structural Analysis of Aflatoxin B1 Degradation byFoods (Basel, Switzerland) · 2026Article
- Enhanced Inhibition ofInternational journal of molecular sciences · 2026Article
- Influence of mutations at different distances from the active center on the activity and stability of laccase 13B22.Bioresources and bioprocessing · 2025Article
- Altering the Properties of Laccases fromBiomolecules · 2025Article
- The research progress of LACC1.Frontiers in immunology · 2025Review
- Evaluation of Antibiotic Biodegradation by a Versatile and Highly Active Recombinant Laccase from the Thermoalkaliphilic BacteriumBiomolecules · 2024Article
- Increasing Reduction Potentials of Type 1 Copper Center and Catalytic Efficiency of Small Laccase from Streptomyces coelicolor through Secondary Coordination Sphere Mutations.Angewandte Chemie (International ed. in English) · 2023Article
Corrections and comments
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Authors and funding
5 authors at 3 institutions in 3 countries.
Funding
Abstract
Laccase, one of the metalloproteins, belongs to the multicopper oxidase family. It oxidizes a wide range of substrates and generates water as a sole by-product. The engineering of laccase is important to broaden their industrial and environmental applications. The general assumption is that the low redox potential of laccases is the principal obstacle, as evidenced by their low activity towards certain substrates. Therefore, the primary goal of engineering laccases is to improve their oxidation capability, thereby increasing their redox potential. Even though some of the determinants of laccase are known, it is still not entirely clear how to enhance its redox potential. However, the laccase active site has additional characteristics that regulate the enzymes' activity and specificity. These include the electrostatic and hydrophobic environment of the substrate binding pocket, the steric effect at the substrate binding site, and the orientation of the binding substrate with respect to the T1 site of the laccase. In this review, these features of the substrate binding site will be discussed to highlight their importance as a target for future laccase engineering.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.