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Título: | Suppression of Water as a Nucleophile in Candida antarctica Lipase B Catalysis |
Autor: | Larsen, Marianne Wittrup; Zielinska, Dorota F.; Martinelle, Mats; Hidalgo, Aurelio CSIC ORCID; Jensen, Lars Juhl; Bornscheuer, Uwe T.; Hult, Karl | Palabras clave: | Candida antarctica Lipase B Hydrolysis Library screening Mutagenesis Rational design Transacylation |
Fecha de publicación: | 2010 | Editor: | Wiley-VCH | Citación: | ChemBioChem 11 (6): 796–801 (2010) | Resumen: | A water tunnel in Candida antarctica lipase B that provides the active site with substrate water is hypothesized. A small, focused library created in order to prevent water from entering the active site through the tunnel was screened for increased transacylation over hydrolysis activity. A single mutant, S47L, in which the inner part of the tunnel was blocked, catalysed the transacylation of vinyl butyrate to 20 mm butanol 14 times faster than hydrolysis. The single mutant Q46A, which has a more open outer end of the tunnel, showed an increased hydrolysis rate and a decreased hydrolysis to transacylation ratio compared to the wild-type lipase. Mutants with a blocked tunnel could be very useful in applications in which hydrolysis is unwanted, such as the acylation of highly hydrophilic compounds in the presence of water. | Versión del editor: | http://dx.doi.org/10.1002/cbic.200900743 | URI: | http://hdl.handle.net/10261/74747 | DOI: | 10.1002/cbic.200900743 | ISSN: | 1439-4227 |
Aparece en las colecciones: | (CBM) Artículos |
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accesoRestringido.pdf | 15,38 kB | Adobe PDF | Visualizar/Abrir |
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