ArticleThe Journal of biological chemistry2011
α-Galactosidase/sucrose kinase (AgaSK), a novel bifunctional enzyme from the human microbiome coupling galactosidase and kinase activities.
Article in The Journal of biological chemistry, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.
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Who cites it
15 citing papers in PubMed, 37 citations in OpenAlex.
- Activity-based metaproteomics driven discovery and enzymological characterization of potential α-galactosidases in the mouse gut microbiome.Communications chemistry · 2024Article
- Microbiota alters the metabolome in an age- and sex- dependent manner in mice.Nature communications · 2023Article
- Ruminococcus gnavus: friend or foe for human health.FEMS microbiology reviews · 2023Review
- Molecular advances in microbial α-galactosidases: challenges and prospects.World journal of microbiology & biotechnology · 2022Review
- Heterologous Expression of a Thermostable α-Galactosidase fromJournal of microbiology and biotechnology · 2022Article
- The Intestinal Barrier and Its Dysfunction in Patients with Metabolic Diseases and Non-Alcoholic Fatty Liver Disease.International journal of molecular sciences · 2022Review
- RadA, a MSCRAMM Adhesin of the Dominant SymbioteBiomolecules · 2021Article
- α-Galactosidase and Sucrose-Kinase Relationships in a Bi-functional AgaSK Enzyme Produced by the Human Gut SymbiontFrontiers in microbiology · 2020Article
- Sucrose 6Microbial genomics · 2019Article
- A β-mannan utilization locus in Bacteroides ovatus involves a GH36 α-galactosidase active on galactomannans.FEBS letters · 2016Article
- Genetically modified proteins: functional improvement and chimeragenesis.Bioengineered · 2015Review
- Microbiota and gut-liver axis: their influences on obesity and obesity-related liver disease.Journal of pediatric gastroenterology and nutrition · 2013Review
- The molecular mechanism of thermostable α-galactosidases AgaA and AgaB explained by x-ray crystallography and mutational studies.The Journal of biological chemistry · 2012Article
- Functional analysis of family GH36 α-galactosidases from Ruminococcus gnavus E1: insights into the metabolism of a plant oligosaccharide by a human gut symbiont.Applied and environmental microbiology · 2012Article
- Structural elucidation of dextran degradation mechanism by streptococcus mutans dextranase belonging to glycoside hydrolase family 66.The Journal of biological chemistry · 2012Article
Corrections and comments
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Authors and funding
11 authors at 4 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
α-Galactosides are non-digestible carbohydrates widely distributed in plants. They are a potential source of energy in our daily food, and their assimilation by microbiota may play a role in obesity. In the intestinal tract, they are degraded by microbial glycosidases, which are often modular enzymes with catalytic domains linked to carbohydrate-binding modules. Here we introduce a bifunctional enzyme from the human intestinal bacterium Ruminococcus gnavus E1, α-galactosidase/sucrose kinase (AgaSK). Sequence analysis showed that AgaSK is composed of two domains: one closely related to α-galactosidases from glycoside hydrolase family GH36 and the other containing a nucleotide-binding motif. Its biochemical characterization showed that AgaSK is able to hydrolyze melibiose and raffinose to galactose and either glucose or sucrose, respectively, and to specifically phosphorylate sucrose on the C6 position of glucose in the presence of ATP. The production of sucrose-6-P directly from raffinose points toward a glycolytic pathway in bacteria, not described so far. The crystal structures of the galactosidase domain in the apo form and in complex with the product shed light onto the reaction and substrate recognition mechanisms and highlight an oligomeric state necessary for efficient substrate binding and suggesting a cross-talk between the galactose and kinase domains.
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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.