ArticleThe Journal of biological chemistry2020
A structural and kinetic survey of GH5_4 endoglucanases reveals determinants of broad substrate specificity and opportunities for biomass hydrolysis.
Article in The Journal of biological chemistry, 2020. 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, 27 citations in OpenAlex.
- A minimal cellulosome-like system in Cellulosilyticum lentocellum.FEBS open bio · 2026Article
- Characterization of a novel bifunctional endo-β-1,4-glucanase/mannanase from Aspergillus oryzae.Applied microbiology and biotechnology · 2026Article
- Recent progress in the microbial production of Xylanase.World journal of microbiology & biotechnology · 2025Review
- Characterization of a novel halophilic and thermostable multifunctional cellulase from Ebinur Salt Lake.Scientific reports · 2025Article
- Dissection of an Anaerobic Fungal Cellulosomal Endoglucanase: Impact of the Dockerin Module on Activity, Thermostability, and Flexibility.ACS omega · 2025Article
- Biochemical characterization of a bilfunctional endoglucanase/glucomannanase derived from mountain soil.Biotechnology letters · 2025Article
- Metabolism of hemicelluloses by root-associated Bacteroidota species.The ISME journal · 2025Article
- Expression and characterization of a novel microbial GH9 glucanase, IDSGLUC9-4, isolated from sheep rumen.Animal bioscience · 2024Article
- Dynamics of loops surrounding the active site architecture in GH5_2 subfamily TfCel5A for cellulose degradation.Biotechnology for biofuels and bioproducts · 2023Article
- Structure and enzymatic characterization of CelD endoglucanase from the anaerobic fungus Piromyces finnis.Applied microbiology and biotechnology · 2023Article
- A combinatorial droplet microfluidic device integrated with mass spectrometry for enzyme screening.Lab on a chip · 2023Article
- Enzymatic Characterization of Unused Biomass Degradation Using theMicroorganisms · 2022Article
- Characterization of a novel thermophilic metagenomic GH5 endoglucanase heterologously expressed in Escherichia coli and Saccharomyces cerevisiae.Biotechnology for biofuels and bioproducts · 2022Article
- Expression, characterization, and activity optimization of a novel cellulase from the thermophilic bacteria Cohnella sp. A01.Scientific reports · 2022Article
- The carbohydrate-active enzyme database: functions and literature.Nucleic acids research · 2022Article
- An amateur gut microbial configuration formed in giant panda for striving to digest cellulose in bamboo: Systematic evidence from intestinal digestive enzymes, functional genes and microbial structures.Frontiers in microbiology · 2022Article
- Multifunctional cellulases are potent, versatile tools for a renewable bioeconomy.Current opinion in biotechnology · 2021Review
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Authors and funding
9 authors at 4 institutions in 2 countries.
Funding
Abstract
Broad-specificity glycoside hydrolases (GHs) contribute to plant biomass hydrolysis by degrading a diverse range of polysaccharides, making them useful catalysts for renewable energy and biocommodity production. Discovery of new GHs with improved kinetic parameters or more tolerant substrate-binding sites could increase the efficiency of renewable bioenergy production even further. GH5 has over 50 subfamilies exhibiting selectivities for reaction with β-(1,4)-linked oligo- and polysaccharides. Among these, subfamily 4 (GH5_4) contains numerous broad-selectivity endoglucanases that hydrolyze cellulose, xyloglucan, and mixed-linkage glucans. We previously surveyed the whole subfamily and found over 100 new broad-specificity endoglucanases, although the structural origins of broad specificity remained unclear. A mechanistic understanding of GH5_4 substrate specificity would help inform the best protein design strategies and the most appropriate industrial application of broad-specificity endoglucanases. Here we report structures of 10 new GH5_4 enzymes from cellulolytic microbes and characterize their substrate selectivity using normalized reducing sugar assays and MS. We found that GH5_4 enzymes have the highest catalytic efficiency for hydrolysis of xyloglucan, glucomannan, and soluble β-glucans, with opportunistic secondary reactions on cellulose, mannan, and xylan. The positions of key aromatic residues determine the overall reaction rate and breadth of substrate tolerance, and they contribute to differences in oligosaccharide cleavage patterns. Our new composite model identifies several critical structural features that confer broad specificity and may be readily engineered into existing industrial enzymes. We demonstrate that GH5_4 endoglucanases can have broad specificity without sacrificing high activity, making them a valuable addition to the biomass deconstruction toolset.
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