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Isotope Substitution of Promiscuous Alcohol Dehydrogenase Reveals the Origin of Substrate Preference in the Transition State
dc.contributor.author | Behiry, Enas | |
dc.contributor.author | Ruiz-Pernía, José Javier | |
dc.contributor.author | Luk, Louis Y. P. | |
dc.contributor.author | Tuñón, Iñaki | |
dc.contributor.author | Moliner, Vicent | |
dc.contributor.author | Allemann, Rudolf K. | |
dc.date.accessioned | 2018-06-26T10:03:38Z | |
dc.date.available | 2018-06-26T10:03:38Z | |
dc.date.issued | 2018-03-12 | |
dc.identifier.citation | BEHIRY, Enas M., et al. Isotope Substitution of Promiscuous Alcohol Dehydrogenase Reveals the Origin of Substrate Preference in the Transition State. Angewandte Chemie, 2018, vol. 130, no 12, p. 3182-3185 | ca_CA |
dc.identifier.issn | 1433-7851 | |
dc.identifier.issn | 1521-3773 | |
dc.identifier.uri | http://hdl.handle.net/10234/175337 | |
dc.description.abstract | The origin of substrate preference in promiscuous enzymes was investigated by enzyme isotope labelling of the alcohol dehydrogenase from Geobacillus stearothermophilus (BsADH). At physiological temperature, protein dynamic coupling to the reaction coordinate was insignificant. However, the extent of dynamic coupling was highly substrate-dependent at lower temperatures. For benzyl alcohol, an enzyme isotope effect larger than unity was observed, whereas the enzyme isotope effect was close to unity for isopropanol. Frequency motion analysis on the transition states revealed that residues surrounding the active site undergo substantial displacement during catalysis for sterically bulky alcohols. BsADH prefers smaller substrates, which cause less protein friction along the reaction coordinate and reduced frequencies of dynamic recrossing. This hypothesis allows a prediction of the trend of enzyme isotope effects for a wide variety of substrates. | ca_CA |
dc.format.extent | 4 p. | ca_CA |
dc.format.mimetype | application/pdf | ca_CA |
dc.language.iso | eng | ca_CA |
dc.publisher | Wiley | |
dc.relation.isPartOf | Angewandte Chemie, 2018, vol. 130, no 12 | ca_CA |
dc.rights | Atribución 4.0 Internacional | * |
dc.rights.uri | http://creativecommons.org/licenses/by-sa/4.0/ | * |
dc.subject | alcohol dehydrogenase | ca_CA |
dc.subject | enzymes | ca_CA |
dc.subject | enzyme catalysis | ca_CA |
dc.subject | enzyme models | ca_CA |
dc.subject | isotope effects | ca_CA |
dc.title | Isotope Substitution of Promiscuous Alcohol Dehydrogenase Reveals the Origin of Substrate Preference in the Transition State | ca_CA |
dc.type | info:eu-repo/semantics/article | ca_CA |
dc.identifier.doi | https://doi.org/10.1002/ange.201712826 | |
dc.relation.projectID | Cardiff University through the UK's Biotechnology and Biological Sciences Research Council: BB/J005266/1, BB/L020394/1; Spanish Ministerio de Economia y Competitividad and FEDER funds: CTQ2015-66223-C2, CTQ2015-74523-JIN Universitat Jaume I: UJI.B2017-31; Generalitat Valenciana: PROMETEOII/2014/022 | ca_CA |
dc.rights.accessRights | info:eu-repo/semantics/openAccess | ca_CA |
dc.relation.publisherVersion | https://onlinelibrary.wiley.com/doi/full/10.1002/ange.201712826 | ca_CA |
dc.contributor.funder | This work was supported by Cardiff University through the UK's Biotechnology and Biological Sciences Research Council through grants BB/J005266/1 and BB/L020394/1 to R.K.A., by the Spanish Ministerio de Economía y Competitividad and FEDER funds (projects CTQ2015‐66223‐C2 and CTQ2015‐74523‐JIN), Universitat Jaume I (UJI⋅B2017‐31) and Generalitat Valenciana (PROMETEOII/2014/022). We would like to thank Nydia Robayo Churque for her technical help. | ca_CA |
dc.type.version | info:eu-repo/semantics/publishedVersion | ca_CA |
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