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Título: | Redesign of the Phosphate Binding Site of L-Rhamnulose- 1-Phosphate Aldolase towards a Dihydroxyacetone Dependent Aldolase |
Autor: | Garrabou, Xavier CSIC ORCID; Joglar Tamargo, Jesús CSIC ORCID; Parella, Teodor; Crehuet, Ramón CSIC ORCID ; Bujons, Jordi CSIC ORCID; Clapés Saborit, Pere CSIC ORCID | Palabras clave: | Aldol reaction Amino aldehydes Enzyme catalysis L-rhamnulose-1-phosphate aldolase Mutagenesis |
Fecha de publicación: | 2011 | Editor: | Wiley-VCH | Citación: | Advanced Synthesis and Catalysis | Resumen: | The aldol addition of unphosphorylated dihydroxyacetone (DHA) to aldehydes catalyzed by L-rhamnulose-1-phosphate aldolase (RhuA), a dihydroxyacetone phosphate-dependent aldolase, is reported. Moreover, a single point mutation in the phosphate binding site of the RhuA wild type, that is, substitution of aspartate for asparagine at position N29, increased by 3-fold the equation image of aldol addition reactions of DHA to other aldehyde acceptors rather than the natural L-lactaldehyde. The RhuA N29D mutant modified the optimum enzyme design for the natural substrate and changed its catalytic properties making the aldolase more versatile to other aldol additions of DHA. | Versión del editor: | http://dx.doi.org/10.1002/adsc.201000719 | URI: | http://hdl.handle.net/10261/46451 | DOI: | 10.1002/adsc.201000719 | ISSN: | 1615-4150 | E-ISSN: | 1615-4169 |
Aparece en las colecciones: | (IQAC) Artículos |
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