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- W2808041568 abstract "Enzyme catalyzed hydrolysis of glycosidic bonds is undertaken by glycoside hydrolases (GHs) in nature. In addition to a catalytic domain (CD), GHs often have carbohydrate-binding modules (CBMs) attached to the CD through a linker. Allosamidin binding to full-length GH18 Serratia marcescens ChiB and the catalytic domain only yield equal changes in reaction free energy (ΔGro = −38 kJ/mol), enthalpy (ΔHro = 18 kJ/mol), and entropy (−TΔSro = −57 kJ/mol). Interestingly, the change in heat capacity (ΔCp,r) was 3-fold smaller for full-length vs. the CD alone (−263 vs. −695 J/K mol). Allosamidin binding to the full-length isoform and the CD alone of the GH18 human chitotriosidase yielded different ΔGro (−46.9 vs. −38.9 kJ/mol) due to differences in ΔHro (−58.2 vs. −50.2 kJ/mol), while −TΔSro and (11.3 vs. 11.3 kJ/mol) and ΔCp,r (−531 vs. −602 kJ/mol) are similar. The results combined show that the nature of the linker region and CBM affect the thermodynamic signatures of active site ligand binding." @default.
- W2808041568 created "2018-06-21" @default.
- W2808041568 creator A5049307104 @default.
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- W2808041568 date "2018-10-01" @default.
- W2808041568 modified "2023-10-06" @default.
- W2808041568 title "The effect of carbohydrate binding modules and linkers on inhibitor binding to family 18 glycoside hydrolases" @default.
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- W2808041568 doi "https://doi.org/10.1016/j.jct.2018.06.013" @default.
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