ArticleJournal of bacteriology2010
Functional diversity of four glycoside hydrolase family 3 enzymes from the rumen bacterium Prevotella bryantii B14.
Article in Journal of bacteriology, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 27 papers.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
27 citing papers in PubMed, 66 citations in OpenAlex.
- Synthesis and Glycosidase Inhibition Studies of Novel Exoglycals Targeting GH3 Family Enzymes: Insights from Comparative Analysis with Macrolide Antibiotics.Chemistry (Weinheim an der Bergstrasse, Germany) · 2026Article
- Multiomic Analysis Provided Insights into the Responses of Carbon Sources by Wood-Rotting FungiJournal of fungi (Basel, Switzerland) · 2025Article
- Use of xylosidase 3C from Segatella baroniae to discriminate xylan non-reducing terminus substitution characteristics.BMC research notes · 2024Article
- Transcriptomic analysis of polysaccharide utilization loci reveals substrate preferences in ruminal generalists Segatella bryantii TF1-3 and Xylanibacter ruminicola KHP1.BMC genomics · 2024Article
- A novel GH3-β-glucosidase from soda lake metagenomic libraries with desirable properties for biomass degradation.Scientific reports · 2024Article
- Tutorial: Microbiome studies in drug metabolism.Clinical and translational science · 2022Article
- Functional and Phylogenetic Characterization of Bacteria in Bovine Rumen Using Fractionation of Ruminal Fluid.Frontiers in microbiology · 2022Article
- PUL-Mediated Plant Cell Wall Polysaccharide Utilization in the Gut Bacteroidetes.International journal of molecular sciences · 2021Review
- Characterization and diversity of the complete set of GH family 3 enzymes from Rhodothermus marinus DSM 4253.Scientific reports · 2020Article
- Multiple cellobiohydrolases and cellobiose phosphorylases cooperate in the ruminal bacterium Ruminococcus albus 8 to degrade cellooligosaccharides.Scientific reports · 2016Article
- Functional and modular analyses of diverse endoglucanases from Ruminococcus albus 8, a specialist plant cell wall degrading bacterium.Scientific reports · 2016Article
- Identification of the nucleophile catalytic residue of GH51 α-L-arabinofuranosidase from Pleurotus ostreatus.AMB Express · 2015Article
- The N-Terminal GH10 Domain of a Multimodular Protein from Caldicellulosiruptor bescii Is a Versatile Xylanase/β-Glucanase That Can Degrade Crystalline Cellulose.Applied and environmental microbiology · 2015Article
- Characterization of five β-glycoside hydrolases from Cellulomonas fimi ATCC 484.Journal of bacteriology · 2014Article
- Two new xylanases with different substrate specificities from the human gut bacterium Bacteroides intestinalis DSM 17393.Applied and environmental microbiology · 2014Article
- Reconstitution of a thermostable xylan-degrading enzyme mixture from the bacterium Caldicellulosiruptor bescii.Applied and environmental microbiology · 2013Article
- Article
- Biochemical and structural insights into xylan utilization by the thermophilic bacterium Caldanaerobius polysaccharolyticus.The Journal of biological chemistry · 2012Article
- Molecular and biochemical analyses of the GH44 module of CbMan5B/Cel44A, a bifunctional enzyme from the hyperthermophilic bacterium Caldicellulosiruptor bescii.Applied and environmental microbiology · 2012Article
- Quantitative comparisons of select cultured and uncultured microbial populations in the rumen of cattle fed different diets.Journal of animal science and biotechnology · 2012Article
Corrections and comments
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Authors and funding
4 authors at 2 institutions in 2 countries.
Funding
Abstract
Prevotella bryantii B(1)4 is a member of the phylum Bacteroidetes and contributes to the degradation of hemicellulose in the rumen. The genome of P. bryantii harbors four genes predicted to encode glycoside hydrolase (GH) family 3 (GH3) enzymes. To evaluate whether these genes encode enzymes with redundant biological functions, each gene was cloned and expressed in Escherichia coli. Biochemical analysis of the recombinant proteins revealed that the enzymes exhibit different substrate specificities. One gene encoded a cellodextrinase (CdxA), and three genes encoded beta-xylosidase enzymes (Xyl3A, Xyl3B, and Xyl3C) with different specificities for either para-nitrophenyl (pNP)-linked substrates or substituted xylooligosaccharides. To identify the amino acid residues that contribute to catalysis and substrate specificity within this family of enzymes, the roles of conserved residues (R177, K214, H215, M251, and D286) in Xyl3B were probed by site-directed mutagenesis. Each mutation led to a severely decreased catalytic efficiency without a change in the overall structure of the mutant enzymes. Through amino acid sequence alignments, an amino acid residue (E115) that, when mutated to aspartic acid, resulted in a 14-fold decrease in the k(cat)/K(m) for pNP-beta-d-xylopyranoside (pNPX) with a concurrent 1.1-fold increase in the k(cat)/K(m) for pNP-beta-d-glucopyranoside (pNPG) was identified. Amino acid residue E115 may therefore contribute to the discrimination between beta-xylosides and beta-glucosides. Our results demonstrate that each of the four GH3 enzymes has evolved to perform a specific role in lignopolysaccharide hydrolysis and provide insight into the role of active-site residues in catalysis and substrate specificity for GH3 enzymes.
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Registered trials
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