title: Efficient enzymatic synthesis of amide with (aminomethyl)trimethylsilane.
abstract: 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.
authors.affiliation: Laboratory of Applied Biological Chemistry, Department of Synthetic Chemistry and Biological Chemistry, Graduate School of Engineering, Kyoto University, Yoshida, Sakyo-ku, Kyoto 606-8501, Japan.
authors.forename: T
authors.initials: T
authors.lastname: Kawamoto
authors.forename: R S
authors.initials: RS
authors.lastname: So
authors.forename: Y
authors.initials: Y
authors.lastname: Masuda
authors.forename: A
authors.initials: A
authors.lastname: Tanaka