Efficient Enzymatic Synthesis of Amide with(Aminomethyl)trimethylsilane
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概要
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Hydrolase-catalyzed amide synthesis using a silicon-containing amine, (aminomethyl)trimethylsilane, as the substrate was studied. Six hydrolases(lipase OF 360, lipase Novo, lipase KLIP-001, lipoprotein lipase Type A, cholesterol esterase Type A, and cholesterol esterase III)were capable of forming the amide of(aminomethyl)trimethylsilane with octanoic acid in 2, 2, 4-trimethylpentane. Lipoprotein lipase Type A and cholesterol esterase Type A showed particularly the high levels of activity. From a comparative study of(aminomethyl)trimethylsilane and its carbon analog, 2, 2-dimethylpropylamine, the former was found to be a better substrate for the hydrolases than the carbon analog. This difference is considered to arise from the specific properties of the silicon atom. (Aminomethyl)trimethylsilane exhibited a homotropic effect at concentration under 100 mM in amide synthesis by lipoprotein lipase Type A, while the carbon analog showed no such effect.
- 公益社団法人日本生物工学会の論文
- 1999-05-25
著者
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Kawamoto Takuo
Laboratory Of Applied Biological Chemistry Department Of Synthetic Chemistry And Biological Chamistr
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Tanaka Atsuo
Laboratory Of Applied Biological Chemistry Department Of Synthetic Chemistry And Biological Chamistr
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SO ROSARIO
Laboratory of Applied Biological Chemistry, Department of Synthetic Chemistry and Biological Chamist
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MASUDA YOSHIHISA
Laboratory of Applied Biological Chemistry, Department of Synthetic Chemistry and Biological Chamist
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So Rosario
Laboratory Of Applied Biological Chemistry Department Of Synthetic Chemistry And Biological Chamistr
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Masuda Yoshihisa
Laboratory Of Applied Biological Chemistry Department Of Synthetic Chemistry And Biological Chamistr
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