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Biocatalytic Access to α,α‐Dialkyl‐α‐amino Acids by a Mechanism‐Based Approach
Author(s) -
Fesko Kateryna,
Uhl Michael,
Steinreiber Johannes,
Gruber Karl,
Griengl Herfried
Publication year - 2010
Publication title -
angewandte chemie international edition
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 5.831
H-Index - 550
eISSN - 1521-3773
pISSN - 1433-7851
DOI - 10.1002/anie.200904395
Subject(s) - serine , aldol reaction , chemistry , cysteine , glycine , threonine , alanine , pyridoxal phosphate , combinatorial chemistry , mechanism (biology) , pyridoxal 5 phosphate , amino acid , stereochemistry , pyridoxal , organic chemistry , biochemistry , phosphate , enzyme , catalysis , philosophy , cofactor , epistemology
New donors—new products : Threonine aldolases ( L ‐TA, D ‐TA) have now been found to accept donors other than glycine. In a simple asymmetric biocatalytic aldol reaction alanine, serine, and cysteine reacted with a range of simple acceptor aldehydes to yielded α‐substituted serine derivatives (see scheme; PLP=pyridoxal phosphate).
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