dc.contributor.author | Eide, Kristine Bistrup | |
dc.contributor.author | Sørlie, Morten | |
dc.date.accessioned | 2021-03-18T14:21:06Z | |
dc.date.available | 2021-03-18T14:21:06Z | |
dc.date.created | 2018-10-18T13:25:04Z | |
dc.date.issued | 2018 | |
dc.identifier.citation | Journal of Chemical Thermodynamics. 2018, 125 220-224. | en_US |
dc.identifier.issn | 0021-9614 | |
dc.identifier.uri | https://hdl.handle.net/11250/2734291 | |
dc.description.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 (DGrº = -38 kJ/mol), enthalpy (DHrº = 18 kJ/mol), and entropy (-TDSrº = -57 kJ/mol).
Interestingly, the change in heat capacity (DCp,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 DGrº (-46.9 vs. -38.9 kJ/mol) due to differences in DHrº (-58.2 vs. -50.2 kJ/mol), while -TDSrº and (11.3 vs. 11.3 kJ/mol) and DCp,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. | en_US |
dc.language.iso | eng | en_US |
dc.rights | Attribution-NonCommercial-NoDerivatives 4.0 Internasjonal | * |
dc.rights.uri | http://creativecommons.org/licenses/by-nc-nd/4.0/deed.no | * |
dc.title | The effect of carbohydrate binding modules and linkers on inhibitor binding to family 18 glycoside hydrolases | en_US |
dc.type | Peer reviewed | en_US |
dc.type | Journal article | en_US |
dc.description.version | acceptedVersion | en_US |
dc.source.pagenumber | 220-224 | en_US |
dc.source.volume | 125 | en_US |
dc.source.journal | Journal of Chemical Thermodynamics | en_US |
dc.identifier.doi | 10.1016/j.jct.2018.06.013 | |
dc.identifier.cristin | 1621405 | |
cristin.unitcode | 192,12,0,0 | |
cristin.unitname | Kjemi, bioteknologi og matvitenskap | |
cristin.ispublished | true | |
cristin.fulltext | postprint | |
cristin.qualitycode | 1 | |