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9QQO

Crystal structure of a beta-glycosidase from Prevotella sp.

Summary for 9QQO
Entry DOI10.2210/pdb9qqo/pdb
DescriptorBeta-glycosidase, GLYCEROL (3 entities in total)
Functional Keywordsglycoside hydrolase, hydrolase
Biological sourcePrevotella
Total number of polymer chains12
Total formula weight618921.14
Authors
Schwartz, M.,Neiers, F. (deposition date: 2025-04-01, release date: 2026-01-28, Last modification date: 2026-02-11)
Primary citationMuradova, M.,Proskura, A.,Senty-Segault, V.,Boichot, V.,Ilina, V.,Poirier, N.,Gourrat, K.,Chaloyard, J.,Nadtochii, L.,Baranenko, D.,Heydel, J.M.,Canon, F.,Lirussi, F.,Schwartz, M.,Neiers, F.
A Human Oral Bacterial beta-Glucosidase Involved in Aroma Release from Glycosides.
J.Agric.Food Chem., 74:2941-2950, 2026
Cited by
PubMed Abstract: Flavor perception is driven by the interplay of gustation, olfaction, and somatosensory inputs. Among the factors influencing flavor perception, the enzymatic activity of oral bacterial glycosidases plays a role in modulating taste and aroma, generating aroma molecules from glycosidic precursors. This study investigates the capacity of oral bacterial β-glucosidases to hydrolyze glycosidic aroma precursors. Seven candidate enzymes from oral bacteria were recombinantly produced and screened for glycosidase activity. Among them, only the β-glucosidase from . (PsBG1) showed hydrolytic activity toward chromogenic substrates and the aroma glucosides tested, leading to the release of salicylaldehyde, hexanol, and octanol, as confirmed by GC-MS. Structural analysis of PsBG1 revealed key residues involved in substrate recognition and catalysis. These results identify a specific oral bacterial enzyme capable of releasing aroma-active compounds from glycosides , suggesting a potential contribution of oral microbiota enzymatic activity to in-mouth aroma release.
PubMed: 41549477
DOI: 10.1021/acs.jafc.5c13712
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (2.5 Å)
Structure validation

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PDB entries from 2026-04-08

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