Functional analyses and application of microbial lactonohydrolases |
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| Authors: | Kohsuke Honda Michihiko Kataoka Sakayu Shimizu |
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| Affiliation: | (1) Division of applied Life Sciences, Graduate School of Agriculture, Kyoto University, Kitashirakawa-Oiwakecho, Sakyo-ku, 606-8502 Kyoto, Japan |
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| Abstract: | Microbial lactonohydrolases (intramolecular ester bond-hydrolyzing enzymes) with unique properties were found. The lactonohydrolase fromFusarium oxysporum catalyzes enantioselective hydrolysis of aldonate lactones andd-pantoyl lactone (d-PL). This enzyme is useful for the large-scale optical resolution of racemic PL. TheAgrobacterium tumefaciens enzyme catalyzes asymmetric hydrolysis of PL, but the stereospecificity is opposite to that of theFusarium enzyme. Dihydrocoumarin hydrolase (DHase) fromAcinetobacter calcoaceticus is a bifunctional enzyme, which catalyzes not only hydrolysis of aromatic lactones but also bromination of monochlorodimedon in the presence of H2O2 and dihydrocoumarin. DHase also hydrolyzes several linear esters, and is useful for enantioselective hydrolysis of methyldl-β-acetylthioisobutyrate and regioselective hydrolysis of methyl cetraxate. |
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| Keywords: | lactonohydrolase lactone stereospecific hydrolysis resio selective hydrolysis |
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