ArticleThe Journal of biological chemistry2012
Tracing determinants of dual substrate specificity in glycoside hydrolase family 5.
Article in The Journal of biological chemistry, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.
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Who cites it
22 citing papers in PubMed, 44 citations in OpenAlex.
- Deciphering functional diversity and structural determinants of substrate specificity in fungal glycoside hydrolase family 5_5 cellulases.Applied and environmental microbiology · 2026Article
- Characterization of a novel bifunctional endo-β-1,4-glucanase/mannanase from Aspergillus oryzae.Applied microbiology and biotechnology · 2026Article
- Biochemical characterization of a bilfunctional endoglucanase/glucomannanase derived from mountain soil.Biotechnology letters · 2025Article
- Dynamics of loops surrounding the active site architecture in GH5_2 subfamily TfCel5A for cellulose degradation.Biotechnology for biofuels and bioproducts · 2023Article
- Unraveling the roles of coastal bacterial consortia in degradation of various lignocellulosic substrates.mSystems · 2023Article
- Insights into promiscuous chitosanases: the known and the unknown.Applied microbiology and biotechnology · 2022Review
- Biochemical characterization and cleavage pattern analysis of a novel chitosanase with cellulase activity.Applied microbiology and biotechnology · 2022Article
- Multifunctional cellulases are potent, versatile tools for a renewable bioeconomy.Current opinion in biotechnology · 2021Review
- A structural and kinetic survey of GH5_4 endoglucanases reveals determinants of broad substrate specificity and opportunities for biomass hydrolysis.The Journal of biological chemistry · 2020Article
- Enzymatic degradation of plant biomass and synthetic polymers.Nature reviews. Chemistry · 2020Review
- Extent and Origins of Functional Diversity in a Subfamily of Glycoside Hydrolases.Journal of molecular biology · 2019Article
- TheBiotechnology for biofuels · 2017Article
- Functional Trade-Offs in Promiscuous Enzymes Cannot Be Explained by Intrinsic Mutational Robustness of the Native Activity.PLoS genetics · 2016Article
- Ligand-binding specificity and promiscuity of the main lignocellulolytic enzyme families as revealed by active-site architecture analysis.Scientific reports · 2016Article
- Subsite-specific contributions of different aromatic residues in the active site architecture of glycoside hydrolase family 12.Scientific reports · 2015Article
- Novel β-1,4-Mannanase Belonging to a New Glycoside Hydrolase Family in Aspergillus nidulans.The Journal of biological chemistry · 2015Article
- Article
- Structure, dynamics, and specificity of endoglucanase D from Clostridium cellulovorans.Journal of molecular biology · 2013Article
- The evolutionary origins of detoxifying enzymes: the mammalian serum paraoxonases (PONs) relate to bacterial homoserine lactonases.The Journal of biological chemistry · 2013Article
- Article
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Authors and funding
15 authors at 4 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Enzymes are traditionally viewed as having exquisite substrate specificity; however, recent evidence supports the notion that many enzymes have evolved activities against a range of substrates. The diversity of activities across glycoside hydrolase family 5 (GH5) suggests that this family of enzymes may contain numerous members with activities on multiple substrates. In this study, we combined structure- and sequence-based phylogenetic analysis with biochemical characterization to survey the prevalence of dual specificity for glucan- and mannan-based substrates in the GH5 family. Examination of amino acid profile differences between the subfamilies led to the identification and subsequent experimental confirmation of an active site motif indicative of dual specificity. The motif enabled us to successfully discover several new dually specific members of GH5, and this pattern is present in over 70 other enzymes, strongly suggesting that dual endoglucanase-mannanase activity is widespread in this family. In addition, reinstatement of the conserved motif in a wild type member of GH5 enhanced its catalytic efficiency on glucan and mannan substrates by 175 and 1,600%, respectively. Phylogenetic examination of other GH families further indicates that the prevalence of enzyme multispecificity in GHs may be greater than has been experimentally characterized. Single domain multispecific GHs may be exploited for developing improved enzyme cocktails or facile engineering of microbial hosts for consolidated bioprocessing of lignocellulose.
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