ArticleThe Journal of biological chemistry2020
The structure of a family 110 glycoside hydrolase provides insight into the hydrolysis of α-1,3-galactosidic linkages in λ-carrageenan and blood group antigens.
Article in The Journal of biological chemistry, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.
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7 citing papers in PubMed, 17 citations in OpenAlex.
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- Akkermansia muciniphila exoglycosidases target extended blood group antigens to generate ABO-universal blood.Nature microbiology · 2024Article
- Crystal Structure ofJournal of applied glycoscience · 2024Article
- Three novel marine species of the genusFrontiers in microbiology · 2023Article
- Toward Understanding the Alginate Catabolism inFrontiers in bioengineering and biotechnology · 2022Article
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6 authors at 2 institutions in 1 country.
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Abstract
α-Linked galactose is a common carbohydrate motif in nature that is processed by a variety of glycoside hydrolases from different families. Terminal Galα1-3Gal motifs are found as a defining feature of different blood group and tissue antigens, as well as the building block of the marine algal galactan λ-carrageenan. The blood group B antigen and linear α-Gal epitope can be processed by glycoside hydrolases in family GH110, whereas the presence of genes encoding GH110 enzymes in polysaccharide utilization loci from marine bacteria suggests a role in processing λ-carrageenan. However, the structure-function relationships underpinning the α-1,3-galactosidase activity within family GH110 remain unknown. Here we focus on a GH110 enzyme (PdGH110B) from the carrageenolytic marine bacterium
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