Isotope Substitution of Promiscuous Alcohol Dehydrogenase Reveals the Origin of Substrate Preference in the Transition State
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Otros documentos de la autoría: Behiry, Enas; Ruiz-Pernía, José Javier; Luk, Louis Y. P.; Tuñón, Iñaki; Moliner, Vicent; Allemann, Rudolf K.
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Título
Isotope Substitution of Promiscuous Alcohol Dehydrogenase Reveals the Origin of Substrate Preference in the Transition StateAutoría
Fecha de publicación
2018-03-12Editor
WileyISSN
1433-7851; 1521-3773Cita bibliográfica
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. 3182-3185Tipo de documento
info:eu-repo/semantics/articleVersión de la editorial
https://onlinelibrary.wiley.com/doi/full/10.1002/ange.201712826Versión
info:eu-repo/semantics/publishedVersionPalabras clave / Materias
Resumen
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 ... [+]
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. [-]
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Angewandte Chemie, 2018, vol. 130, no 12Proyecto de investigación
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/2014/022Derechos de acceso
info:eu-repo/semantics/openAccess
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