ArticleThe Journal of biological chemistry2012
Structural enzymology of Cellvibrio japonicus Agd31B protein reveals α-transglucosylase activity in glycoside hydrolase family 31.
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 20 papers.
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Who cites it
20 citing papers in PubMed, 45 citations in OpenAlex.
- Fungal Rutinosidase─Engineering of a Side Tunnel Steers Its Transglycosylation Potential.Journal of agricultural and food chemistry · 2026Article
- 1,6-Journal of the American Chemical Society · 2022Article
- Structural basis of the strict specificity of a bacterial GH31 α-1,3-glucosidase for nigerooligosaccharides.The Journal of biological chemistry · 2022Article
- Stereoselective synthesis of a 4-⍺-glucoside of valienamine and its X-ray structure in complex with Streptomyces coelicolor GlgE1-V279S.Scientific reports · 2021Article
- Structure-function analysis of silkworm sucrose hydrolase uncovers the mechanism of substrate specificity in GH13 subfamily 17The Journal of biological chemistry · 2020Article
- Crystal Structure of α-Xylosidase fromACS sustainable chemistry & engineering · 2020Article
- Development of a strategy for the screening of α-glucosidase-producing microorganisms.Journal of microbiology (Seoul, Korea) · 2020Article
- Division of labor in honey bee gut microbiota for plant polysaccharide digestion.Proceedings of the National Academy of Sciences of the United States of America · 2019Article
- Target highlights in CASP13: Experimental target structures through the eyes of their authors.Proteins · 2019Article
- Synthesis of Human Milk Oligosaccharides: Protein Engineering Strategies for Improved Enzymatic Transglycosylation.Molecules (Basel, Switzerland) · 2019Review
- 1,6-Cyclophellitol Cyclosulfates: A New Class of Irreversible Glycosidase Inhibitor.ACS central science · 2017Article
- Eliminating hydrolytic activity without affecting the transglycosylation of a GH1 β-glucosidase.Applied microbiology and biotechnology · 2017Article
- Article
- α-Glucosidases and α-1,4-glucan lyases: structures, functions, and physiological actions.Cellular and molecular life sciences : CMLS · 2016Review
- Structural dissection of a complex Bacteroides ovatus gene locus conferring xyloglucan metabolism in the human gut.Open biology · 2016Article
- Polysaccharide degradation systems of the saprophytic bacterium Cellvibrio japonicus.World journal of microbiology & biotechnology · 2016Review
- Detection of Active Mammalian GH31 α-Glucosidases in Health and Disease Using In-Class, Broad-Spectrum Activity-Based Probes.ACS central science · 2016Article
- An Aspergillus nidulans β-mannanase with high transglycosylation capacity revealed through comparative studies within glycosidase family 5.Applied microbiology and biotechnology · 2014Article
- Structural insight into how Streptomyces coelicolor maltosyl transferase GlgE binds α-maltose 1-phosphate and forms a maltosyl-enzyme intermediate.Biochemistry · 2014Article
- Crystal structure of α-1,4-glucan lyase, a unique glycoside hydrolase family member with a novel catalytic mechanism.The Journal of biological chemistry · 2013Article
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Authors and funding
5 authors at 3 institutions in 3 countries.
Funding
Abstract
The metabolism of the storage polysaccharides glycogen and starch is of vital importance to organisms from all domains of life. In bacteria, utilization of these α-glucans requires the concerted action of a variety of enzymes, including glycoside hydrolases, glycoside phosphorylases, and transglycosylases. In particular, transglycosylases from glycoside hydrolase family 13 (GH13) and GH77 play well established roles in α-glucan side chain (de)branching, regulation of oligo- and polysaccharide chain length, and formation of cyclic dextrans. Here, we present the biochemical and tertiary structural characterization of a new type of bacterial 1,4-α-glucan 4-α-glucosyltransferase from GH31. Distinct from 1,4-α-glucan 6-α-glucosyltransferases (EC 2.4.1.24) and 4-α-glucanotransferases (EC 2.4.1.25), this enzyme strictly transferred one glucosyl residue from α(1→4)-glucans in disproportionation reactions. Substrate hydrolysis was undetectable for a series of malto-oligosaccharides except maltose for which transglycosylation nonetheless dominated across a range of substrate concentrations. Crystallographic analysis of the enzyme in free, acarbose-complexed, and trapped 5-fluoro-β-glucosyl-enzyme intermediate forms revealed extended substrate interactions across one negative and up to three positive subsites, thus providing structural rationalization for the unique, single monosaccharide transferase activity of the enzyme.
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