Enzymatic synthesis of ω-carboxy-β-hydroxy-( l)-α-amino acids

Commercially available ω-carboxy-aldehydes and glycine have been subjected to the catalytic action of an l-threonine aldolase from Escherichia coli to give the corresponding β-hydroxy-α-( l)-amino acids as a mixture of erythro/ threo epimers. Specifically, the reaction with glyoxylic acid ( 2) gave...

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Bibliographic Details
Published in:Tetrahedron 2008-05, Vol.64 (22), p.5079-5084
Main Authors: Sagui, Francesca, Conti, Paola, Roda, Gabriella, Contestabile, Roberto, Riva, Sergio
Format: Article
Language:English
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Summary:Commercially available ω-carboxy-aldehydes and glycine have been subjected to the catalytic action of an l-threonine aldolase from Escherichia coli to give the corresponding β-hydroxy-α-( l)-amino acids as a mixture of erythro/ threo epimers. Specifically, the reaction with glyoxylic acid ( 2) gave the epimeric β-hydroxy-( l)-aspartates ( t, e)-9 that could be isolated by ion-exchange chromatography in 67% yield. Following esterification and N-Boc protection, the two epimers could be isolated as pure compounds. Similarly, the aldolase-catalyzed addition of glycine to succinic semialdehyde ( 4) gave the expected mixture of β-hydroxy- l-α-aminoadipic acids ( t)-12 and ( e)-12 in 34% yield. [Display omitted]
ISSN:0040-4020
1464-5416
DOI:10.1016/j.tet.2008.03.070