Structural highlights
FunctionPublication Abstract from PubMedSaponins are natural glycosides widely used in medicine and the food industry. Although saponin metabolism in human is dependent on intestinal microbes, few involving bacteria enzymes have been identified. We cloned BlBG3, a GH3 beta-glucosidase from Bifidobacterium longum, from human stool. We found that BlBG3 catalyzes the hydrolysis of glycoside furostanol and ginsenoside Rb1 at higher efficiency than other microbial beta-glucosidases. Structural analysis of BlBG3 in complex with d-glucose revealed its three unique loops, which form a deep pocket and participate in substrate binding. To understand how substrate is bound to the pocket, molecular docking was performed and the binding interactions of protobioside with BlBG3 were revealed. Mutational study suggested that R484 and H642 are critical for enzymatic activity. Our study presents the first structural and functional analysis of a saponin-processing enzyme from human microbiota. Functional and structural characterization of a beta-glucosidase involved in saponin metabolism from intestinal bacteria.,Yan S, Wei PC, Chen Q, Chen X, Wang SC, Li JR, Gao C Biochem Biophys Res Commun. 2018 Feb 19;496(4):1349-1356. doi:, 10.1016/j.bbrc.2018.02.018. Epub 2018 Feb 5. PMID:29421652[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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