Computational Studies of Candida Antarctica Lipase B to Test Its Capability as a Starting Point to Redesing New Diels-Alderases
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http://dx.doi.org/10.1021/acs.jpcb.5b10527 |
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Títol
Computational Studies of Candida Antarctica Lipase B to Test Its Capability as a Starting Point to Redesing New Diels-AlderasesData de publicació
2016-03Editor
American Chemical SocietyCita bibliogràfica
ŚWIDEREK, Katarzyna; MOLINER, Vicent. Computational Studies of Candida Antarctica Lipase B to Test Its Capability as a Starting Point To Redesign New Diels-Alderases. The journal of physical chemistry. B, 2016, vol. 120, no 8, p. 2053.Tipus de document
info:eu-repo/semantics/articleVersió de l'editorial
http://pubmedcentralcanada.ca/pmcc/articles/PMC4777658/Versió
info:eu-repo/semantics/publishedVersionParaules clau / Matèries
Resum
The design of new biocatalysts is a target that is receiving increasing attention. One of the most popular reactions in this regard is the Diels-Alder cycloaddition due to its applications in organic synthesis and the ... [+]
The design of new biocatalysts is a target that is receiving increasing attention. One of the most popular reactions in this regard is the Diels-Alder cycloaddition due to its applications in organic synthesis and the absence of efficient natural enzymes that catalyze it. In this paper, the possibilities of using the highly promiscuous Candida Antarctica lipase B (CALB) as a protein scaffold to re-design a Diels-Alderase has been explored by means of theoretical quantum mechanics/molecular mechanics (QM/MM) molecular dynamics (MD) simulations. Free energy surfaces have been computed for two reactions in the wild-type and in several mutants with hybrid AM1/MM potentials with corrections at M06-2X/MM level. The study of the counterpart reactions in solution has allowed performing comparative analysis that render interesting conclusion. Since the dienophile anchors very well in the oxyanion hole of all tested protein variants, the slight electronic changes from reactant complex to the transition state suggest that mutations should be focused in favoring the formation of reactive conformations of reactant complex that, in turn, would reduce the energy barrier. [-]
Publicat a
J Phys Chem B. 2016 March 3; 120(8)Drets d'accés
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info:eu-repo/semantics/restrictedAccess
info:eu-repo/semantics/restrictedAccess
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