ArticlePloS one2011
Understanding lignin-degrading reactions of ligninolytic enzymes: binding affinity and interactional profile.
Article in PloS one, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.
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Who cites it
17 citing papers in PubMed, 98 citations in OpenAlex.
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- Non-productive binding of cellobiohydrolase i investigated by surface plasmon resonance spectroscopy.Cellulose (London, England) · 2021Article
- Genes Identification, Molecular Docking and Dynamics Simulation Analysis of Laccases fromInternational journal of molecular sciences · 2020Article
- Structure-Function of the High Affinity Substrate Binding Site (S1) of Human Norepinephrine Transporter.Frontiers in pharmacology · 2020Article
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- Unleashing the potential of ligninolytic bacterial contributions towards pulp and paper industry: key challenges and new insights.Environmental science and pollution research international · 2016Review
- Discovery of 12-mer peptides that bind to wood lignin.Scientific reports · 2016Article
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- Diversity of two-domain laccase-like multicopper oxidase genes in Streptomyces spp.: identification of genes potentially involved in extracellular activities and lignocellulose degradation during composting of agricultural waste.Applied and environmental microbiology · 2014Article
- Release of Pleurotus ostreatus versatile-peroxidase from Mn2+ repression enhances anthropogenic and natural substrate degradation.PloS one · 2012Article
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Authors and funding
11 authors at 1 institution in 1 country.
Funding
Abstract
Previous works have demonstrated that ligninolytic enzymes mediated effective degradation of lignin wastes. The degrading ability greatly relied on the interactions of ligninolytic enzymes with lignin. Ligninolytic enzymes mainly contain laccase (Lac), lignin peroxidase (LiP) and manganese peroxidase (MnP). In the present study, the binding modes of lignin to Lac, LiP and MnP were systematically determined, respectively. Robustness of these modes was further verified by molecular dynamics (MD) simulations. Residues GLU460, PRO346 and SER113 in Lac, residues ARG43, ALA180 and ASP183 in LiP and residues ARG42, HIS173 and ARG177 in MnP were most crucial in binding of lignin, respectively. Interactional analyses showed hydrophobic contacts were most abundant, playing an important role in the determination of substrate specificity. This information is an important contribution to the details of enzyme-catalyzed reactions in the process of lignin biodegradation, which can be used as references for designing enzyme mutants with a better lignin-degrading activity.
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