Asymmetric synthesis of aliphatic 2-hydroxy ketones by enzymatic carboligation of aldehydes

被引：40

作者：

de Maria, Pablo Dominguez

Pohl, Martina

Gocke, Doerte

Groeger, Harald

Trauthwein, Harald

Stillger, Thomas

Walter, Lydia

Mueller, Michael

机构：

[1] Degussa AG, Serv Ctr Biocatalysis, D-63457 Hanau, Germany

[2] Univ Dusseldorf, Inst Mol Enzymtechnol, D-52426 Julich, Germany

[3] Univ Freiburg, Inst Pharmazeut Wissenschaften, D-79104 Freiburg, Germany

来源：

EUROPEAN JOURNAL OF ORGANIC CHEMISTRY | 2007年 / 2007卷 / 18期

关键词：

enzyme catalysis; carboligation; benzaldehyde lyase; benzoylformate decarboxylase; aldehydes; 2-hydroxy ketones;

D O I：

10.1002/ejoc.200600876

中图分类号：

O62 [有机化学];

学科分类号：

070303 ; 081704 ;

摘要：

Benzaldehyde lyase (BAL) and benzoylformate decarboxylase (BFD) catalyse the asymmetric ligation of aliphatic aldehydes to afford enantiomerically enriched 2-hydroxy ketones. Carboligation of linear aldehydes with both enzymes results in high levels of conversion and in enantioselectivities of up to 80 % ee. In cases involving branched aliphatic aldehydes, BAL enables the carboligation of 3-methylbutanal with a high level of conversion and an enantioselectivity of 89 % ee. ((c) Wiley-VCH Verlag GmbH & Co.

引用

页码：2940 / 2944

页数：5

共 37 条

[1] Synthesis with good enantiomeric excess of both enantiomers of α-ketols and acetolactates by two thiamin diphosphate-dependent decarboxylases [J].