1. Enzyme-mediated enantioselective hydrolysis of 1,2-diol monotosylate derivatives bearing an unsaturated substituent
- Author
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K. Oohana, Kazutsugu Matsumoto, M. Hashimoto, Y. Suzuki, H. Ohshima, T. Togawa, K. Usuda, and T. Shimoda
- Subjects
chemistry.chemical_classification ,biology ,Double bond ,010405 organic chemistry ,Organic Chemistry ,Diol ,Enantioselective synthesis ,Substituent ,010402 general chemistry ,Triple bond ,01 natural sciences ,Biochemistry ,0104 chemical sciences ,chemistry.chemical_compound ,Hydrolysis ,chemistry ,Enzymatic hydrolysis ,Drug Discovery ,biology.protein ,Organic chemistry ,Lipase - Abstract
We have succeeded in the easy preparation of optically active 1,2-diol monotosylates bearing an unsaturated substituent via enzymatic hydrolysis. Lipase PS quickly catalyzes the hydrolyses of 2-acetoxybut-3-enyl tosylate, which has a double bond, and 2-acetoxybut-3-ynyl tosylate, which has a triple bond, with excellent enantioselectivity to afford the corresponding optically active compounds. The reaction is also applicable to acetates with a longer chain, which has a double bond at the terminus. To demonstrate the applicability of this method, enantiomerically pure (R)-massoialactone, a natural coconut flavor, has been synthesized from racemic 2-acetoxypent-4-enyl tosylate in several steps. Furthermore, the enzyme can recognize the stereochemistry of olefins, and the (Z)-alkenyl structure is more suitable for the enantioselective hydrolysis than the (E)-isomer.
- Published
- 2018