초록
<P>A unique lipase (SpL) from <I>Sphingomonas</I> sp. HXN-200 was discovered as the first intracellular enzyme for the aminolysis of ester or acid to produce amide. Reactions of a series of esters and amines with SpL gave the corresponding amides <B>3a</B>-<B>g</B> in high yield with high activity. SpL also showed high enantioselectivity and high activity for enantioselective ester aminolysis, producing amides (<I>R</I>)-<B>3h</B>-<B>j</B> in high ee from the corresponding racemic ester or amine. Moreover, SpL was found to be highly active for the aminolysis of carboxylic acid, which was generally considered infeasible with the known aminolysis enzymes. The aminolysis of several carboxylic acids afforded the corresponding amides <B>3a</B>, <B>3d</B>, <B>3k</B>, <B>3l</B>, and <B>3n</B> in good yield. The intracellular SpL was expressed in <I>Escherichia coli</I> cells to give an efficient whole-cell biocatalyst for amide synthesis. Remarkably, high catalytic activity was observed in the presence of water at 2-4% (v/v) for free enzyme and 16% (v/v) for whole cells, respectively. Accordingly, <I>E. coli</I> (SpL) wet cells were used as easily available and practical catalysts for the aminolysis of ester or acid, producing a group of useful and valuable amides in high concentration (up to 103 mM) and high yield. The newly discovered intracellular SpL with unique properties is a promising catalyst for green and efficient synthesis of amides.</P><BR>[FIG OMISSION]</BR>