223464-67-3Relevant articles and documents
The substrate specificity of the heat-stable stereospecific amidase from Klebsiella oxytoca
Shaw, Nicholas M.,Naughton, Andrew B.
, p. 747 - 752 (2004)
The substrate specificity of the heat-stable stereospecific amidase from Klebsiella oxytoca was investigated. In addition to the original substrate, 3,3,3-trifluoro-2-hydroxy-2-methylpropanamide, the amidase accepted 2-hydroxy-2-(trifluoromethyl)-butanamide and 3,3,3-trifluoro-2-amino-2- methylpropanamide as substrates. Compounds with larger side chains and compounds where the hydroxyl group was substituted with a methoxy group, or in which the CF3 group was substituted by CCl3, were not accepted. The biotransformation is a new synthetic route to (R)-(+)-3,3,3- trifluoro-2-amino-2-methylpropanoic acid, and its related (S)-(-)-amide, and to (R)-(+)-2-hydroxy-2-(trifluoromethyl)-butanoic acid and its related (S)-(-)-amide.
Enzymatic resolution of Cα-fluoroalkyl substituted amino acids
Koksch, Beate,Quaedflieg, Peter J. L. M.,Michel, Thomas,Burger, Klaus,Broxterman, Quirinus B.,Schoemaker, Hans E.
, p. 1401 - 1407 (2007/10/03)
A methodology for the enzymatic resolution of sterically constrained C α-fluoroalkyl substituted amino acids has been developed. Racemic H-(αTfm)Ala-NH2, H-(αCF2Cl)Ala-NH 2 and H-(αCF2Br)Ala-NH2