ArticleThe Journal of biological chemistry2013
The structure of a Streptomyces avermitilis α-L-rhamnosidase reveals a novel carbohydrate-binding module CBM67 within the six-domain arrangement.
Article in The Journal of biological chemistry, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 34 papers.
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34 citing papers in PubMed, 102 citations in OpenAlex.
- Comparative Study on Growth Performance and Rumen Digestive Metabolism Between Cull Beef Cows and Fattening Bulls.Animals : an open access journal from MDPI · 2026Article
- Effects of Dietary Dandelion Supplementation on Ruminal Morphology, Fermentation, Microbiome, and Inflammation in Lambs Under High-Concentrate Feeding.Animals : an open access journal from MDPI · 2026Article
- Microbial α-L-Rhamnosidases: Regioselective Biocatalysts for Flavonoid Biotransformation and Nutraceutical Applications.Current issues in molecular biology · 2026Review
- Genomic diversity, functional differentiation and prophage dynamics in Lactiplantibacillus paraplantarum.NPJ science of food · 2026Article
- A Hyperthermostable Archaeal GH78 Rhamnosidase Efficiently Hydrolyzes Flavonoid Glycosides for Juice Debittering.Journal of agricultural and food chemistry · 2026Article
- Article
- Substrate Selectivities of GH78 α-L-Rhamnosidases from Human Gut Bacteria on Dietary Flavonoid Glycosides.Molecules (Basel, Switzerland) · 2025Article
- Functional and structural insights into α-L-Rhamnosidase: cloning, characterization, and decoding evolutionary constraints through structural motif.Archives of microbiology · 2025Article
- Verrucomicrobia of the FamilyMicroorganisms · 2024Article
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- In vitro evaluation of novel SN-38 prodrug activated by α-rhamnosidase of exogenous enzyme.Analytical sciences : the international journal of the Japan Society for Analytical Chemistry · 2024Article
- Efficient production of icariin and baohuoside I from Epimedium Folium flavonoids by fungal α-L-rhamnosidase hydrolysing regioselectively the terminal rhamnose of epimedin C.Biotechnology for biofuels and bioproducts · 2023Article
- α-L-rhamnosidase: production, properties, and applications.World journal of microbiology & biotechnology · 2023Review
- Insights into glycosidic bond specificity of an engineered selective α-L-rhamnosidase N12-Rha via activity assays and molecular modelling.AMB Express · 2022Article
- Computational design of Lactobacillus Acidophilus α-L-rhamnosidase to increase its structural stability.PloS one · 2022Article
- Metagenomics analysis of the effects ofPeerJ · 2022Article
- Cellulosomes: Highly Efficient Cellulolytic Complexes.Sub-cellular biochemistry · 2021Review
- Multi-omic Directed Discovery of Cellulosomes, Polysaccharide Utilization Loci, and Lignocellulases from an Enriched Rumen Anaerobic Consortium.Applied and environmental microbiology · 2020Article
- Crystal structure of β-L-arabinobiosidase belonging to glycoside hydrolase family 121.PloS one · 2020Article
- A carbohydrate-binding family 48 module enables feruloyl esterase action on polymeric arabinoxylan.The Journal of biological chemistry · 2019Article
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Authors and funding
8 authors at 4 institutions in 3 countries.
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Abstract
α-L-rhamnosidases hydrolyze α-linked L-rhamnosides from oligosaccharides or polysaccharides. We determined the crystal structure of the glycoside hydrolase family 78 Streptomyces avermitilis α-L-rhamnosidase (SaRha78A) in its free and L-rhamnose complexed forms, which revealed the presence of six domains N, D, E, F, A, and C. In the ligand complex, L-rhamnose was bound in the proposed active site of the catalytic module, revealing the likely catalytic mechanism of SaRha78A. Glu(636) is predicted to donate protons to the glycosidic oxygen, and Glu(895) is the likely catalytic general base, activating the nucleophilic water, indicating that the enzyme operates through an inverting mechanism. Replacement of Glu(636) and Glu(895) resulted in significant loss of α-rhamnosidase activity. Domain D also bound L-rhamnose in a calcium-dependent manner, with a KD of 135 μm. Domain D is thus a non-catalytic carbohydrate binding module (designated SaCBM67). Mutagenesis and structural data identified the amino acids in SaCBM67 that target the features of L-rhamnose that distinguishes it from the other major sugars present in plant cell walls. Inactivation of SaCBM67 caused a substantial reduction in the activity of SaRha78A against the polysaccharide composite gum arabic, but not against aryl rhamnosides, indicating that SaCBM67 contributes to enzyme function against insoluble substrates.
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