2022
DOI: 10.3390/catal12030343
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Systematic Functional and Computational Analysis of Glucose-Binding Residues in Glycoside Hydrolase Family GH116

Abstract: Glycoside hydrolases (GH) bind tightly to the sugar moiety at the glycosidic bond being hydrolyzed to stabilize its transition state conformation. We endeavored to assess the importance of glucose-binding residues in GH family 116 (GH116) β-glucosidases, which include human β-glucosylceramidase 2 (GBA2), by mutagenesis followed by kinetic characterization, X-ray crystallography, and ONIOM calculations on Thermoanaerobacterium xylanolyticum TxGH116, the structural model for GH116 enzymes. Mutations of residues … Show more

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Cited by 7 publications
(3 citation statements)
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“…The second member, SSO3039, was proposed as a bifunctional exo-β-glucosidase/N-acetyl-β-glucosaminidase [58]. Finally, TxGH116 was proposed as a β-glucosidase [61] (although no activity was observed towards this compound in [62]). On the other hand, no activity was detected with ExoMA2 towards pNP-β-D-Glcp or pNP-β-D-Xylp, suggesting a high specificity for pNP-β-D-Araf [59].…”
Section: Structural Comparison Of Gh52 and Gh116 Familymentioning
confidence: 99%
“…The second member, SSO3039, was proposed as a bifunctional exo-β-glucosidase/N-acetyl-β-glucosaminidase [58]. Finally, TxGH116 was proposed as a β-glucosidase [61] (although no activity was observed towards this compound in [62]). On the other hand, no activity was detected with ExoMA2 towards pNP-β-D-Glcp or pNP-β-D-Xylp, suggesting a high specificity for pNP-β-D-Araf [59].…”
Section: Structural Comparison Of Gh52 and Gh116 Familymentioning
confidence: 99%
“…Instead of hydrolyzing glucosylceramide like GBA2, Tx GH116 exhibits high activity toward 4-nitrophenyl β- D -glucopyranoside (4NPGlc), and β-1,3- and β-1,4-linked glucooligosaccharides. , The Tx GH116 structure contains an N-terminal domain, formed by a two-sheet β-sandwich, tightly associated with a C-terminal (α/α) 6 solenoid domain that contains the catalytic nucleophile, E441, and general acid/base, D593, residues, which were verified by chemical rescue of alanine mutants . In addition, extensive kinetic and structural studies have elucidated the functions of glucose-binding active site residues. , The Tx GH116 structure is most similar to a Geobacillus thermoglucosidasius β-xylosidase from family GH52, whereas it has no structural similarity to other retaining β-glucosidases. Based on this similarity, the GH52 and GH116 families were designated to a new GH clan, Clan O.…”
Section: Introductionmentioning
confidence: 99%
“… 8 In addition, extensive kinetic and structural studies have elucidated the functions of glucose-binding active site residues. 22 , 23 The Tx GH116 structure is most similar to a Geobacillus thermoglucosidasius β-xylosidase from family GH52, 24 whereas it has no structural similarity to other retaining β-glucosidases. Based on this similarity, the GH52 and GH116 families were designated to a new GH clan, Clan O.…”
Section: Introductionmentioning
confidence: 99%