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Studies on enantioselective hydrolysis of the acetic ester of a secondary alcohol with Arthrobacter lipase

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Summary

Characteristics of the enantioselective hydrolysis of the acetic ester of 4-hydroxy-3-methyl-2-(2-propynyl)-2-cyclopentenone (HMPC) by Arthrobacter lipase were investigated in a water/oil biphasic reaction mixture. Kinetic studies revealed that the strict enantioselectivity was entirely due to a difference in the catalytic constants for the enantiomeric substrates and that (S)-HMPC acetate acted as a competitive inhibitor. The comparison of enantioselectivity for the acetates of HMPC analogues indicated that hydrophobic substituents in the HMPC molecule were essential for the strict enantioselectivity.

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Authors and Affiliations

  1. Takarazuka Research Center, Sumitomo Chemical Co. Ltd., 4-2-1 Takatsukasa, 665, Takarazuka, Hyogo, Japan

    Satoshi Mitsuda, Shigeyasu Nabeshima & Hideo Hirohara

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  1. Satoshi Mitsuda
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  2. Shigeyasu Nabeshima
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  3. Hideo Hirohara
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Additional information

Biological preparation of an optically active alcohol. Part II

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Mitsuda, S., Nabeshima, S. & Hirohara, H. Studies on enantioselective hydrolysis of the acetic ester of a secondary alcohol with Arthrobacter lipase. Appl Microbiol Biotechnol 31, 334–337 (1989). https://doi.org/10.1007/BF00257599

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  • DOI: https://doi.org/10.1007/BF00257599

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