The substrate specificity of the heat-stable stereospecific amidase from Klebsiella oxytoca

Autor:	Nicholas M. Shaw, Andrew B Naughton
Rok vydání:	2004
Předmět:	Trifluoromethyl biology Chemistry Stereochemistry Organic Chemistry Substrate (chemistry) Klebsiella oxytoca biology.organism_classification Biochemistry Amidase chemistry.chemical_compound Stereospecificity Biotransformation Drug Discovery Side chain Substrate specificity
Zdroj:	Tetrahedron. 60:747-752
ISSN:	0040-4020
DOI:	10.1016/j.tet.2003.10.124
Popis:	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 CF 3 group was substituted by CCl 3 , 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.
Databáze:	OpenAIRE
Externí odkaz:	https://explore.openaire.eu/search/publication?articleId=doi_________::9d8dfd5843fec9f160a2e1b14ed54595 https://doi.org/10.1016/j.tet.2003.10.124 Zobrazit plný text záznamu Full Text from ScienceDirect