ArticleScientific reports2015
Subsite-specific contributions of different aromatic residues in the active site architecture of glycoside hydrolase family 12.
Article in Scientific reports, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.
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Who cites it
11 citing papers in PubMed, 36 citations in OpenAlex.
- Strategies for GH functional annotation: toward harmonized and predictive CAZymology.Biotechnology for biofuels and bioproducts · 2026Article
- Characterization of Xyloglucanase TpXEG12a fromInternational journal of molecular sciences · 2025Article
- The receptor-like protein RXEG1 confers broad-spectrum resistance in soybean and cotton by recognizing microbial glycoside hydrolase 12 proteins.Plant biotechnology journal · 2025Article
- Dynamics of loops surrounding the active site architecture in GH5_2 subfamily TfCel5A for cellulose degradation.Biotechnology for biofuels and bioproducts · 2023Article
- Roles of Surfactants in Oriented Immobilization of Cellulase on Nanocarriers and Multiphase Hydrolysis System.Frontiers in chemistry · 2022Review
- Synergistic mechanism of GH11 xylanases with different action modes from Aspergillus niger An76.Biotechnology for biofuels · 2021Article
- Genome-based analysis for the bioactive potential of Streptomyces yeochonensis CN732, an acidophilic filamentous soil actinobacterium.BMC genomics · 2020Article
- Carbohydrate active enzyme domains from extreme thermophiles: components of a modular toolbox for lignocellulose degradation.Extremophiles : life under extreme conditions · 2018Review
- Loop 3 of Fungal Endoglucanases of Glycoside Hydrolase Family 12 Modulates Catalytic Efficiency.Applied and environmental microbiology · 2017Article
- Biochemical and structural characterization of a novel halotolerant cellulase from soil metagenome.Scientific reports · 2016Article
- Ligand-binding specificity and promiscuity of the main lignocellulolytic enzyme families as revealed by active-site architecture analysis.Scientific reports · 2016Article
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Authors and funding
9 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The active site architecture of glycoside hydrolase (GH) is a contiguous subregion of the enzyme constituted by residues clustered in the three-dimensional space, recognizing the monomeric unit of ligand through hydrogen bonds and hydrophobic interactions. Mutations of the key residues in the active site architecture of the GH12 family exerted different impacts on catalytic efficiency. Binding affinities between the aromatic amino acids and carbohydrate rings were quantitatively determined by isothermal titration calorimetry (ITC) and the quantum mechanical (QM) method, showing that the binding capacity order of Tyr>Trp>His (and Phe) was determined by their side-chain properties. The results also revealed that the binding constant of a certain residue remained unchanged when altering its location, while the catalytic efficiency changed dramatically. Increased binding affinity at a relatively distant subsite, such as the mutant of W7Y at the -4 subsite, resulted in a marked increase in the intermediate product of cellotetraose and enhanced the reactivity of endoglucanase by 144%; while tighter binding near the catalytic center, i.e. W22Y at the -2 subsite, enabled the enzyme to bind and hydrolyze smaller oligosaccharides. Clarification of the specific roles of the aromatics at different subsites may pave the way for a more rational design of GHs.
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