ArticleNature communications2020
The structural basis of fungal glucuronoyl esterase activity on natural substrates.
Article in Nature communications, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.
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Who cites it
12 citing papers in PubMed, 31 citations in OpenAlex.
- Glucuronoyl Esterase Expressed in Aspen Xylem Affects γ-Ester Linkages Between Lignin and Glucuronoxylan Reducing Recalcitrance and Accelerating Growth.Plant biotechnology journal · 2025Article
- Exploring the synergy between fungal CE15 glucuronoyl esterases and xylanases for lignocellulose saccharification.Biotechnology for biofuels and bioproducts · 2025Article
- 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
- Transesterification with CE15 glucuronoyl esterase from Cerrena unicolor reveals substrate preferences.Biotechnology letters · 2024Article
- 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
- Mechanism and biomass association of glucuronoyl esterase: an α/β hydrolase with potential in biomass conversion.Nature communications · 2022Article
- Structural and Functional Analysis of a Multimodular Hyperthermostable Xylanase-Glucuronoyl Esterase fromBiochemistry · 2021Article
- The coordinated action of glucuronoyl esterase and α-glucuronidase promotes the disassembly of lignin-carbohydrate complexes.FEBS letters · 2021Article
- Enzymatic processing of lignocellulosic biomass: principles, recent advances and perspectives.Journal of industrial microbiology & biotechnology · 2020Review
Corrections and comments
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Authors and funding
7 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Structural and functional studies were conducted of the glucuronoyl esterase (GE) from Cerrena unicolor (CuGE), an enzyme catalyzing cleavage of lignin-carbohydrate ester bonds. CuGE is an α/β-hydrolase belonging to carbohydrate esterase family 15 (CE15). The enzyme is modular, comprised of a catalytic and a carbohydrate-binding domain. SAXS data show CuGE as an elongated rigid molecule where the two domains are connected by a rigid linker. Detailed structural information of the catalytic domain in its apo- and inactivated form and complexes with aldouronic acids reveal well-defined binding of the 4-O-methyl-a-D-glucuronoyl moiety, not influenced by the nature of the attached xylo-oligosaccharide. Structural and sequence comparisons within CE15 enzymes reveal two distinct structural subgroups. CuGE belongs to the group of fungal CE15-B enzymes with an open and flat substrate-binding site. The interactions between CuGE and its natural substrates are explained and rationalized by the structural results, microscale thermophoresis and isothermal calorimetry.
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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.