Premium
Thiamin‐Diphosphate‐Dependent Enzymes: New Aspects of Asymmetric CC Bond Formation
Author(s) -
Pohl Martina,
Lingen Bettina,
Müller Michael
Publication year - 2002
Publication title -
chemistry – a european journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.687
H-Index - 242
eISSN - 1521-3765
pISSN - 0947-6539
DOI - 10.1002/1521-3765(20021202)8:23<5288::aid-chem5288>3.0.co;2-f
Subject(s) - umpolung , chemistry , catalysis , stereochemistry , bond cleavage , substrate (aquarium) , enzyme , biocatalysis , benzoin , kinetic resolution , combinatorial chemistry , enzyme catalysis , protein engineering , enantioselective synthesis , organic chemistry , reaction mechanism , nucleophile , biology , ecology
Starting from a thorough investigation of mechanistic aspects of ThDP‐dependent (ThDP=thiamin diphosphate) enzymes in combination with mutagenesis studies and a detailed substrate screening, new general synthetic methods have been developed based on Umpolung reactions by thiamin catalysis. A selective donor–acceptor concept was established leading to the first asymmetric cross‐benzoin condensation, and a kinetic racemic resolution through CC bond cleavage was developed. With these tools and in combination with protein engineering, we approached the synthesis of new chiral building blocks on a preparative scale. An outlook is given with respect to the potential of other ThDP‐dependent enzymes as catalysts in asymmetric synthesis.