Journal
CHEMCATCHEM
Volume 13, Issue 19, Pages 4237-4242Publisher
WILEY-V C H VERLAG GMBH
DOI: 10.1002/cctc.202100835
Keywords
aldoxime dehydratase; asymmetric synthesis; biocatalysis; chiral resolution; halohydrin
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Funding
- Japan Society for Promotion of Sciences [17H06169]
- Grants-in-Aid for Scientific Research [17H06169] Funding Source: KAKEN
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A biocatalyst with selective enantioselectivity was developed through mutagenesis on aldoxime dehydratase derived from Pseudomonas chlororaphis B23, resulting in the synthesis of chiral compounds.
A biocatalyst used for selective ring scission of (+/-)-5-(chloromethyl)-4, 5-dihydroisoxazole to synthesize chiral (R)-4-chloro-3-hydroxybutanenitrile (90 % ee, 39 % isolated yield) and (S)-5-(chloromethyl)-4, 5-dihydroisoxazole (99 % ee, 39 % isolated yield) was developed by site-saturated mutagenesis on aldoxime dehydratase derived from Pseudomonas chlororaphis B23 (OxdA). The positive mutant (OxdA-L318I, E=68) improved the enantiomeric ratio E by 6-fold as compared to the wild type enzyme (OxdA-wild, E=11). The racemic precursor of (+/-)-5-(chloromethyl)-4, 5-dihydroisoxazole, used in the reaction, can be synthesized from readily available allyl chloride without utilizing highly toxic cyanide. The enantiopure (S)-5-(chloromethyl)-4, 5-dihydroisoxazole remaining in the kinetic resolution can be transformed into corresponding chiral (S)-4-chloro-3-hydroxybutanenitrile without loss of enantiomeric excess by treating it with triethylamine in acetonitrile (99 % ee, 72 % isolated yield) or catalysis of OxdA-wild enzyme (99 % ee, 88 % isolated yield).
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