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α,β‐Unsaturated Aldehydes as Substrates for Asymmetric CC Bond Forming Reactions with Thiamin Diphosphate (ThDP)‐Dependent Enzymes
Author(s) -
Cosp Anabel,
Dresen Carola,
Pohl Martina,
Walter Lydia,
Röhr Caroline,
Müller Michael
Publication year - 2008
Publication title -
advanced synthesis and catalysis
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.541
H-Index - 155
eISSN - 1615-4169
pISSN - 1615-4150
DOI - 10.1002/adsc.200700550
Subject(s) - chemistry , pyruvate decarboxylase , pseudomonas fluorescens , benzaldehyde , enzyme , pseudomonas putida , stereochemistry , lyase , reactivity (psychology) , organic chemistry , catalysis , medicine , alternative medicine , pathology , biology , bacteria , genetics , alcohol dehydrogenase
The enzymes benzaldehyde lyase (BAL) from Pseudomonas fluorescens, benzoylformate decarboxylase (BFD) from Pseudomonas putida and pyruvate decarboxylase (PDC) from Saccharomyces cerevisiae provide different CC bond forming possibilities of α,β‐unsaturated aldehydes with aliphatic and aromatic aldehydes. Structure elucidation and determination of the absolute configuration of the products, which were obtained with high regio‐ and stereoselectivity were carried out. Selective 1,2‐reactivity with yields of 75% and >98% ee , for one single isomer ( A ) were obtained, by choosing the suitable enzyme in combination with the appropriate substrates. By varying enzymes or substrates the regioisomeric hydroxy ketones C , with up to >99% ee , can be obtained. The application of these new chiral building blocks in the synthesis of natural products or biological active substances is considerably facilitated by applying the different ThDP‐dependent enzymes as catalysts. Abbreviations: BAL, benzaldehyde lyase; BFD, benzoylformate decarboxylase; PDC, pyruvate decarboxylase; His, hexahistidine; 2‐HPP, 2‐hydroxy‐1‐phenylpropan‐1‐one; PAC, phenylacetylcarbinol; NTA, nitrilotriacetic acid; ThDP, thiamin diphosphate; wt, wild‐type.