Revealing the Origin of the Efficiency of the De Novo Designed Kemp Eliminase HG-3.17 by Comparison with the Former Developed HG-3
Impacto
Scholar |
Otros documentos de la autoría: Świderek, Katarzyna; Tuñón, Iñaki; Moliner, Vicent; Bertrán, Juan
Metadatos
Mostrar el registro completo del ítemcomunitat-uji-handle:10234/9
comunitat-uji-handle2:10234/7013
comunitat-uji-handle3:10234/8638
comunitat-uji-handle4:
INVESTIGACIONMetadatos
Título
Revealing the Origin of the Efficiency of the De Novo Designed Kemp Eliminase HG-3.17 by Comparison with the Former Developed HG-3Fecha de publicación
2017-05Editor
WileyCita bibliográfica
ŚWIDEREK, Katarzyna, et al. Revealing the Origin of the Efficiency of the De Novo Designed Kemp Eliminase HG‐3.17 by Comparison with the Former Developed HG‐3. Chemistry-A European Journal, 2017, vol. 23, no 31, p. 7582-7589.Tipo de documento
info:eu-repo/semantics/articleVersión de la editorial
http://onlinelibrary.wiley.com/doi/10.1002/chem.201700807/fullVersión
info:eu-repo/semantics/draftinfo:eu-repo/semantics/acceptedVersion
Palabras clave / Materias
Resumen
The design of new biocatalysts is a goal in biotechnology to improve the rate, selectivity and environmental impact of industrial chemical processes. In this regard, the use of computational techniques has provided ... [+]
The design of new biocatalysts is a goal in biotechnology to improve the rate, selectivity and environmental impact of industrial chemical processes. In this regard, the use of computational techniques has provided valuable assistance in the design of new enzymes with remarkable catalytic activity. In this paper, hybrid QM/MM molecular dynamics simulations have allowed insights to be gained on the origin of the limited efficiency of a computationally designed enzyme for the Kemp elimination; the HG-3. Comparison of results derived from this enzyme with those of a more evolved protein containing additional point mutations, HG-3.17, rendered important information that should be taken into account in the design of new enzymes. For this Kemp eliminase reaction, higher reactivity has been demonstrated to be related to a better electrostatic preorganisation of an environment that creates a more favourable electrostatic potential for the reaction to proceed. The limitations of HG-3 can be related to a lack of flexibility, a not well-fitted active site, and a lack of protein electrostatic preorganisation, which decrease the reorganisation around the oxyanion hole. [-]
Proyecto de investigación
Spanish Ministerio de Economía y Competitividad (project CTQ2015-66223-C2) ; Universitat Jaume I (project P1⋅1B2014-26) ; Generalitat Valenciana (PROMETEOII/2014/022) ; Polish Ministry of Science and Higher Education (“Iuventus Plus” program project no. 0478/IP3/2015/73, 2015–2016)Derechos de acceso
Copyright © 2017 John Wiley & Sons, Inc. All Rights Reserved
http://rightsstatements.org/vocab/InC/1.0/
info:eu-repo/semantics/openAccess
http://rightsstatements.org/vocab/InC/1.0/
info:eu-repo/semantics/openAccess
Aparece en las colecciones
- QFA_Articles [812]