期刊
CHEMBIOCHEM
卷 9, 期 4, 页码 491-498出版社
WILEY-V C H VERLAG GMBH
DOI: 10.1002/cbic.200700688
关键词
enantioselectivity; esterases; lipases; protein engineering; tertiary alcohols
Enantiopure tertiary alcohols are very valuable building blocks for the synthesis of many different natural products and pharmaceuticals. As a consequence, several chemical and enzymatic strategies to afford such chiral structures hove been described. Promising enzymatic approaches with agents such as epoxide hydrolases, dehalogenoses and hydroxynitrile lyases have been reported, as well as dihydroxylation by microorganisms. Apart from those valuable options, the hydrolase-based kinetic resolution of tertiary alcohols has been known for the lost three decodes, as several wild-type enzymes hove been reported to be able to accept these sterically hindered molecules. More recently, the existence of an amino acid motif within an enzyme's active site has been identified as highly relevant for the acceptance of such bulky structures. This discovery clearly facilitates the identification of novel biocatalysts for this application. Although several tertiary alcohols have been successfully resolved with wild-type biocatolysts, enontioselectivities have often been too low for synthetic purposes. These limitations have recently been overcome by accessing enzymes from the metagenome through directed evolution or by rational protein design. This minireview describes the state of the art in this area, highlighting aspects of basic academic research into the practical application of biocatolysts for the synthesis of optically active tertiary alcohols.
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