Promiscuous zinc-dependent acylase-mediated carbon?carbon bond formation in organic media
Department of Chemistry, Zhejiang University, Hangzhou 310027, People's Republic of China. Chemical Communications
(Impact Factor: 6.83).
06/2007; 20(20):2078-80. DOI: 10.1039/B700327G
A zinc-dependent acylase, D-aminoacylase from Escherichia. Coli, displays a promiscuous activity to catalyze the carbon-carbon bond formation reaction of 1,3-dicarbonyl compounds to methyl vinyl ketone in organic media.
Available from: Chao Li
- "Although it is well known that a given enzyme is able to catalyze a specific reaction efficiently, some unexpected experimental results have indicated that many enzymes are catalytically promiscuous; i.e., they have the ability to catalyze distinctly different reactions (Copley, 2003; Khersonsky et al., 2006; Hult and Berglund, 2007). Many instances of this phenomenon have recently been reported (Babtie et al., 2009; Feng et al., 2009; Hasnaoui-Dijoux et al., 2008; Lou et al., 2008; Olguin et al., 2008; Sharma et al., 2009; Svedendahl et al., 2008; Taglieber et al., 2007; Xu et al., 2007). "
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ABSTRACT: Several proteases, especially pepsin, were observed to directly catalyze asymmetric aldol reactions. Pepsin, which displays well-documented proteolytic activity under acidic conditions, exhibited distinct catalytic activity in a crossed aldol reaction between acetone and 4-nitrobenzaldehyde with high yield and moderate enantioselectivity. Fluorescence experiments indicated that under neutral pH conditions, pepsin maintains its native conformation and that the natural structure plays an important role in biocatalytic promiscuity. Moreover, no significant loss of enantioselectivity was found even after four cycles of catalyst recycling, showing the high stability of pepsin under the selected aqueous reaction conditions. This case of biocatalytic promiscuity not only expands the application of proteases to new chemical transformations, but also could be developed into a potentially valuable method for green organic synthesis.
Journal of Biotechnology 10/2010; 150(4):539-45. DOI:10.1016/j.jbiotec.2010.10.004 · 2.87 Impact Factor
Available from: Maria Svedendahl Humble
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ABSTRACT: A novel strategy to perform Michael additions between 1,3-dicarbonyl compounds and α,β-unsaturated compounds was developed by the catalysis of hydrolase. We found that 11 hydrolase could catalyze the enzymatic Michael addition reaction to form the carbon–carbon bond. In 2-methyl-2-butanol d-aminoacylase showed high Michael addition activity. The influence of substrate and Michael acceptor structure on Michael addition was evaluated systematically. Some control experiments demonstrated that the active site of d-aminoacylase was responsible for the enzymatic Michael addition reaction. This novel Michael addition activity of hydrolase is of practical significance in expanding the application of enzymes and in the evolution of new biocatalysts.
Journal of Molecular Catalysis B Enzymatic 11/2007; 49(1):50-54. DOI:10.1016/j.molcatb.2007.08.004 · 2.13 Impact Factor
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