ArticleNature communications2022
Mechanism and biomass association of glucuronoyl esterase: an α/β hydrolase with potential in biomass conversion.
Article in Nature communications, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.
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Who cites it
14 citing papers in PubMed.
- Report of the 5th International Symposium on Frontiers in Molecular Science (ISFMS 2025).International journal of molecular sciences · 2025Article
- Exploring the synergy between fungal CE15 glucuronoyl esterases and xylanases for lignocellulose saccharification.Biotechnology for biofuels and bioproducts · 2025Article
- Structure-based clustering and mutagenesis of bacterial tannases reveals the importance and diversity of active site-capping domains.Protein science : a publication of the Protein Society · 2024Article
- Elucidation of the noncovalent interactions driving enzyme activity guides branching enzyme engineering for α-glucan modification.Nature communications · 2024Article
- Structural, Biochemical, and Phylogenetic Analysis of Bacterial and Fungal Carbohydrate Esterase Family 15 Glucuronoyl Esterases in the Rumen.The protein journal · 2024Article
- Exploration of three Dyadobacter fermentans enzymes uncovers molecular activity determinants in CE15.Applied microbiology and biotechnology · 2024Article
- New Labeled PET Analogues Enable the Functional Screening and Characterization of PET-Degrading Enzymes.ACS sustainable chemistry & engineering · 2024Article
- Transesterification with CE15 glucuronoyl esterase from Cerrena unicolor reveals substrate preferences.Biotechnology letters · 2024Article
- Polysaccharide utilization loci from Bacteroidota encode CE15 enzymes with possible roles in cleaving pectin-lignin bonds.Applied and environmental microbiology · 2024Article
- Crystal structures of herbicide-detoxifying esterase reveal a lid loop affecting substrate binding and activity.Nature communications · 2023Article
- New insights to diversity and enzyme-substrate interactions of fungal glucuronoyl esterases.Applied microbiology and biotechnology · 2023Review
- Structural and functional investigation of a fungal member of carbohydrate esterase family 15 with potential specificity for rare xylans.Acta crystallographica. Section D, Structural biology · 2023Article
- Glucuronoyl esterases - enzymes to decouple lignin and carbohydrates and enable better utilization of renewable plant biomass.Essays in biochemistry · 2023Review
- Molecular mechanism of LIP05 derived fromFrontiers in microbiology · 2022Article
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Authors and funding
9 authors.
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Abstract
Glucuronoyl esterases (GEs) are α/β serine hydrolases and a relatively new addition in the toolbox to reduce the recalcitrance of lignocellulose, the biggest obstacle in cost-effective utilization of this important renewable resource. While biochemical and structural characterization of GEs have progressed greatly recently, there have yet been no mechanistic studies shedding light onto the rate-limiting steps relevant for biomass conversion. The bacterial GE OtCE15A possesses a classical yet distinctive catalytic machinery, with easily identifiable catalytic Ser/His completed by two acidic residues (Glu and Asp) rather than one as in the classical triad, and an Arg side chain participating in the oxyanion hole. By QM/MM calculations, we identified deacylation as the decisive step in catalysis, and quantified the role of Asp, Glu and Arg, showing the latter to be particularly important. The results agree well with experimental and structural data. We further calculated the free-energy barrier of post-catalysis dissociation from a complex natural substrate, suggesting that in industrial settings non-catalytic processes may constitute the rate-limiting step, and pointing to future directions for enzyme engineering in biomass utilization.
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