Is Promiscuous CALB a Good Scaffold for Designing New Epoxidases?
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Otros documentos de la autoría: Bordes, Isabel; Recatalá, José; Świderek, Katarzyna; Moliner, Vicent
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Título
Is Promiscuous CALB a Good Scaffold for Designing New Epoxidases?Fecha de publicación
2015Editor
MDPIISSN
1420-3049; 1420-3049Cita bibliográfica
BORDES, Isabel, et al. Is Promiscuous CALB a Good Scaffold for Designing New Epoxidases?. Molecules, 2015, vol. 20, no 10, p. 17789-17806.Tipo de documento
info:eu-repo/semantics/articleVersión de la editorial
http://www.mdpi.com/1420-3049/20/10/17789/htmVersión
info:eu-repo/semantics/publishedVersionPalabras clave / Materias
Resumen
Candida Antarctica lipase B (CALB) is a well-known enzyme, especially because of its promiscuous activity. Due to its properties, CALB was widely used as a benchmark for designing new catalysts for important organic ... [+]
Candida Antarctica lipase B (CALB) is a well-known enzyme, especially because of its promiscuous activity. Due to its properties, CALB was widely used as a benchmark for designing new catalysts for important organic reactions. The active site of CALB is very similar to that of soluble epoxide hydrolase (sEH) formed by a nucleophile-histidine-acid catalytic triad and an oxyanion hole typical for molecular structures derived from processes of α/β hydrolases. In this work we are exploring these similarities and proposing a Ser105Asp variant of CALB as a new catalyst for epoxide hydrolysis. In particular, the hydrolysis of the trans-diphenylpropene oxide (t-DPPO) is studied by means of quantum cluster models mimicking the active site of both enzymes. Our results, based on semi-empirical and DFT calculations, suggest that mutant Ser105Asp CALB is a good protein scaffold to be used for the bio-synthesis of chiral compounds. [-]
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Molecules, 2015, vol. 20, no 10Derechos de acceso
© MDPI AG
info:eu-repo/semantics/openAccess
info:eu-repo/semantics/openAccess
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