A study towards efficient L-threonine aldolase-catalyzed enantio- and diastereoselective aldol reactions of glycine with substituted benzaldehydes: biocatalyst production and process development

被引：16

作者：

Baer, Katrin ^{[1
]}

Dueckers, Nina ^{[2
]}

Rosenbaum, Thorsten ^{[3
]}

Leggewie, Christian ^{[2
]}

Simon, Sabine ^{[1
]}

Krausser, Marina ^{[1
]}

Osswald, Steffen ^{[4
]}

Hummel, Werner ^{[3
]}

Groeger, Harald ^{[1
]}

机构：

[1] Univ Erlangen Nurnberg, Dept Chem & Pharm, D-91054 Erlangen, Germany

[2] Evocatal GmbH, D-40225 Dusseldorf, Germany

[3] Univ Dusseldorf, Inst Mol Enzyme Technol, Res Ctr Julich, D-52426 Julich, Germany

[4] Evon Degussa GmbH, Hlth & Nutr, D-63457 Hanau, Germany

来源：

TETRAHEDRON-ASYMMETRY | 2011年 / 22卷 / 09期

关键词：

ALPHA-AMINO ACIDS; ESCHERICHIA-COLI; GENE;

D O I：

10.1016/j.tetasy.2011.04.016

中图分类号：

O61 [无机化学];

学科分类号：

070301 ; 081704 ;

摘要：

The development of aldol reactions of glycine with substituted benzaldehydes in the presence of recombinant L-threonine aldolases from Escherichia coli or Saccharomyces cerevisiae, which were obtained with excellent overexpression data, has been carried out. When using glycine and ortho-chlorobenzaldehyde, a high conversion of >95%, an enantioselectivity of >99% ee, and a diastereoselectivity with d.r.(syn/anti) = 80:20 was obtained for the resulting beta-hydroxy alpha-amino acid in such a biotransformation. It should be noted that this enzymatic process can be conducted at an elevated substrate concentration of 250 mM. (C) 2011 Elsevier Ltd. All rights reserved.

引用

页码：925 / 928

页数：4

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