Heavy Enzymes and the Rational Redesign of Protein Catalysts
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Otros documentos de la autoría: Scott, Alan; Luk, Louis Y. P.; Tuñón, Iñaki; Moliner, Vicent; Allemann, Rudolf K.
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INVESTIGACIONMetadatos
Título
Heavy Enzymes and the Rational Redesign of Protein CatalystsFecha de publicación
2019-11-18Editor
WileyISSN
1439-4227; 1439-7633Cita bibliográfica
A. F. Scott, L. Y.-P. Luk, I. Tuñón, V. Moliner, R. K. Allemann, ChemBioChem 2019, 20, 2807Tipo de documento
info:eu-repo/semantics/articleVersión de la editorial
https://chemistry-europe.onlinelibrary.wiley.com/doi/10.1002/cbic.201900134Versión
info:eu-repo/semantics/publishedVersionPalabras clave / Materias
Resumen
An unsolved mystery in biology concerns the link between enzyme catalysis and protein motions. Comparison between isotopically labelled “heavy” dihydrofolate reductases and their natural‐abundance counterparts has ... [+]
An unsolved mystery in biology concerns the link between enzyme catalysis and protein motions. Comparison between isotopically labelled “heavy” dihydrofolate reductases and their natural‐abundance counterparts has suggested that the coupling of protein motions to the chemistry of the catalysed reaction is minimised in the case of hydride transfer. In alcohol dehydrogenases, unnatural, bulky substrates that induce additional electrostatic rearrangements of the active site enhance coupled motions. This finding could provide a new route to engineering enzymes with altered substrate specificity, because amino acid residues responsible for dynamic coupling with a given substrate present as hotspots for mutagenesis. Detailed understanding of the biophysics of enzyme catalysis based on insights gained from analysis of “heavy” enzymes might eventually allow routine engineering of enzymes to catalyse reactions of choice. [-]
Publicado en
ChemBioChem, 2019, vol. 20, no 22Proyecto de investigación
Biotechnology and Biological Sciences Research Council (BBSRC); BB/J005266/1, BB/L020394/1; Spanish Ministerio de Ciencia, Innovacion y Universidades: PGC2018-094852-B_C21, PGC2018-094852-B_C22; Universitat Jaume I: UJI.B2017-31; European Union (EU): PGC2018-094852-B_C21, PGC2018-094852-B_C22Derechos de acceso
info:eu-repo/semantics/openAccess
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