151716-73-3

Upstream product

• 90919-32-7 α-methoxy-p-chloropropiophenone 
• 877-37-2 2-bromo-1-(4-chlorophenyl)-1-propanone 
• 49656-24-8 1-(4-chlorophenyl)-2-hydroxypropan-1-one 
• 6285-05-8 4'-chloropropiophenone 
• 104-88-1 4-chlorobenzaldehyde 
• 75-07-0 acetaldehyde 
• 169295-49-2 α-acetoxy-p-chloropropiophenone 

Relevant academic research and scientific papers

Biocatalytic route to chiral acyloins: P450-catalyzed regio- and enantioselective α-hydroxylation of ketones

P450-BM3 and mutants of this monooxygenase generated by directed evolution are excellent catalysts for the oxidative α-hydroxylation of ketones with formation of chiral acyloins with high regioselectivity (up to 99%) and enantioselectivity (up to 99% ee). This constitutes a new route to a class of chiral compounds that are useful intermediates in the synthesis of many kinds of biologically active compounds.

Enantioselective Synthesis of α-Hydroxy Ketones via Benzaldehyde Lyase-Catalyzed C-C Bond Formation Reaction

(R)-Benzoins and (R)-2-hydroxypropiophenone derivatives are formed on a preparative scale by benzaldehyde lyase (BAL)-catalyzed C-C bond formation from aromatic aldehydes and acetaldehyde in aqueous buffer/ DMSO solution with remarkable ease in high chemical yield and high optical purity. The substrate range of this thiamin diphosphate-dependent enzyme was examined with respect to a broad applicability of this benzoin condensation-type reaction in stereoselective synthesis.

Benzoylformate decarboxylase from Pseudomonas putida as stable catalyst for the synthesis of chiral 2-hydroxy ketones

The thiamin diphosphate-and Mg2+-dependent enzyme benzoylformate decarboxylase (BFD) from Pseudomonas putida was characterized with respect to its suitability to catalyze the formation of chiral 2-hydroxy ketones in a benzoin-condensation type reaction. Carboligation constitutes a side reaction of BFD, whereas the predominant physiological task of the enzyme is the non-oxidative decarboxylation of benzoylformate. For this purpose the enzyme was obtained in sufficient purity from Pseudomonas putida cells in a one-step purification using anion-exchange chromatography. To facilitate the access to pure BFD for kinetical studies, stability investigations, and synthetical applications, the coding gene was cloned into a vector allowing the expression of a hexahistidine fusion protein. The recombinant enzyme shows distinct activity maxima for the decarboxylation and the carboligation beside a pronounced stability in a broad pH and temperature range. The enzyme accepts a wide range of donor aldehyde substrates which are ligated to acetaldehyde as an acceptor in mostly high optical purities. The enantioselectivity of the carboligation was found to be a function of the reaction temperature, the substitution pattern of the donor aldehyde and, most significantly, of the concentration of the donor aldehyde substrate. Our data are consistent with a mechanistical model based on the X-ray crystallographic data of BFD. Furthermore we present a simple way to increase the enantiomeric excess of (S)-2-hydroxy-1-phenyl-propanone from 90% to 95% by skillful choice of the reaction parameters. Enzymatic synthesis with BFD are performed best in a continuously operated enzyme membrane reactor. Thus, we have established a new enzyme tool comprising a vast applicability for stereoselective synthesis.

Resolution of Secondary α-Ketoalcohols Catalyzed by Lipase and Inversioon of Stereochemistry

Several α-ketoalcohols of synthetic value were resolved using lipase as a catalyst.Lipoprotein lipase (LPL) provided the best rate of hydrolysis and kinetic differentiation.One of these optically pure α-ketoalcohol was converted to (S)-ibuprofen in good optical purity.The stereospecific inversion of (R)-alcohol to (S)-alcohol is described.Key Words Enzymatic resolution; α-Ketoalcohol; (S)-Ibuprofen

Enzymes in Organic Synthesis: Lipase Catalyzed Resolution of Secondary α-Ketoalcohols

Resolution of several α-ketoalcohols of synthetic value using lipase as a catalyst is described.