- The substrate specificity of the heat-stable stereospecific amidase from Klebsiella oxytoca
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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.
- Shaw, Nicholas M.,Naughton, Andrew B.
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- Chemo-enzymatic synthesis of chiral fluorine-containing building blocks
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Two complementary strategies for the synthesis of optically active fluorine-containing building blocks have been probed. The first strategy involves either the enzymatic resolution of fluorinated α,α- disubstituted-α-amino acid amides, or the asymmetric h
- Blaauw, Richard H.,IJzendoorn, Denis R.,Cremers, Jozef G. O.,Rutjes, Floris P. J. T.,Broxterman, Quirinus B.,Schoemaker, Hans E.
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p. 104 - 107
(2007/10/03)
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- Enzymatic resolution of Cα-fluoroalkyl substituted amino acids
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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
- Koksch, Beate,Quaedflieg, Peter J. L. M.,Michel, Thomas,Burger, Klaus,Broxterman, Quirinus B.,Schoemaker, Hans E.
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p. 1401 - 1407
(2007/10/03)
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