ArticleThe Journal of biological chemistry2012
Analysis of keystone enzyme in Agar hydrolysis provides insight into the degradation (of a polysaccharide from) red seaweeds.
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 40 papers.
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Who cites it
40 citing papers in PubMed, 90 citations in OpenAlex.
- Distribution of microbial carrageenan foraging pathways reveals a widespread latent trait within the ruminant intestinal microbiome.Nature communications · 2026Article
- Fructan utilization by members of marine Gammaproteobacteria involves SusC/D-like proteins.The ISME journal · 2026Article
- Effects of neutral detergent fiber levels on apparent nutrient digestibility and intestinal microbiota composition and function in forest musk deer.Frontiers in veterinary science · 2025Article
- An Unusual His/Asp Dyad Operates Catalysis in Agar-Degrading Glycosidases.ACS catalysis · 2024Article
- Odd-Numbered Agaro-Oligosaccharides Produced by α-Neoagaro-Oligosaccharide Hydrolase Exert Antioxidant Activity in Human Dermal Fibroblasts.Marine drugs · 2024Article
- Bifunctional and monofunctional α-neoagarooligosaccharide hydrolases from Streptomyces coelicolor A3(2).Applied microbiology and biotechnology · 2023Article
- Extracellular production of a thermostable Cellvibrio endolytic β-agarase in Escherichia coli for agarose liquefaction.AMB Express · 2023Article
- Enrichment of Agar Gel with Antioxidant Pectin from Fireweed: Mechanical and Rheological Properties, Simulated Digestibility, and Oral Processing.Gels (Basel, Switzerland) · 2022Article
- Glycoside hydrolase from the GH76 family indicates that marine Salegentibacter sp. Hel_I_6 consumes alpha-mannan from fungi.The ISME journal · 2022Article
- Metabolism of a hybrid algal galactan by members of the human gut microbiome.Nature chemical biology · 2022Article
- Diverse events have transferred genes for edible seaweed digestion from marine to human gut bacteria.Cell host & microbe · 2022Article
- Standard Candles for Dating Microbial Lineages.Methods in molecular biology (Clifton, N.J.) · 2022Article
- Biochemical and Structural Characterization of Thermostable GH159 Glycoside Hydrolases Exhibiting α-L-Arabinofuranosidase Activity.Frontiers in molecular biosciences · 2022Article
- Characterization of Agarolytic Pathway in a Terrestrial BacteriumFrontiers in microbiology · 2022Article
- Metabolic and enzymatic elucidation of cooperative degradation of red seaweed agarose by two human gut bacteria.Scientific reports · 2021Article
- Characterization of Neoagarooligosaccharide HydrolaseMarine drugs · 2021Article
- Molecular Characterization of a Novel 1,3-α-3,6-Anhydro-L-Galactosidase, Ahg943, with Cold- and High-Salt-Tolerance fromJournal of microbiology and biotechnology · 2020Article
- Article
- Warming, but Not Acidification, Restructures Epibacterial Communities of the Baltic MacroalgaFrontiers in microbiology · 2020Article
- Inverting family GH156 sialidases define an unusual catalytic motif for glycosidase action.Nature communications · 2019Article
Corrections and comments
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Authors and funding
5 authors at 2 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Agars are abundant polysaccharides from marine red algae, and their chemical structure consists of alternating D-galactose and 3,6-anhydro-L-galactose residues, the latter of which are presumed to make the polymer recalcitrant to degradation by most terrestrial bacteria. Here we study a family 117 glycoside hydrolase (BpGH117) encoded within a recently discovered locus from the human gut bacterium Bacteroides plebeius. Consistent with this locus being involved in agarocolloid degradation, we show that BpGH117 is an exo-acting 3,6-anhydro-α-(1,3)-L-galactosidase that removes the 3,6-anhydrogalactose from the non-reducing end of neoagaro-oligosaccharides. A Michaelis complex of BpGH117 with neoagarobiose reveals the distortion of the constrained 3,6-anhydro-L-galactose into a conformation that favors catalysis. Furthermore, this complex, supported by analysis of site-directed mutants, provides evidence for an organization of the active site and positioning of the catalytic residues that are consistent with an inverting mechanism of catalysis and suggests that a histidine residue acts as the general acid. This latter feature differs from the vast majority of glycoside hydrolases, which use a carboxylic acid, highlighting the alternative strategies that enzymes may utilize in catalyzing the cleavage of glycosidic bonds.
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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.