23434-95-9

Upstream product

• 3617-01-4 β-(4-chlorophenyl)pyruvic acid 
• 1431505-85-9 (E/Z)-methyl 3-(4-chlorophenyl)-2-dimethylaminoacrylate 
• 80540-56-3 methyl 3-(4-chlorophenyl)-2-hydroxyacrylate 
• 104-88-1 4-chlorobenzaldehyde 
• 93634-55-0 (Z)-4-(4-chlorobenzylidene)-2-methyloxazol-5(4H)-one 
• 7424-00-2 DL-Phe(4Cl) 

Downstream Products

• 186700-30-1 methyl 3-(4-chlorophenyl)-2-hydroxypropanoate 

Relevant academic research and scientific papers

METHODS FOR PRODUCTION OF PF1022A DERIVATIVES

Provided are processes for the production of PF1022A derivative compounds, including incubating a microorganism strain capable of producing such compounds in a culture medium to produce a resulting culture, said culture medium containing carbon and nitrog

Enantioselective reduction of 3-aryl-2-oxo-propanoic acids: A comparison of enzymatic and transition-metal-catalyzed methods

Phenyllactic acids are important constituents of depsipeptides, which are a large class of natural products expressing a wide range of biological activities. Despite there being several methods for the enantioselective synthesis of α-hydroxy acids, almost no studies are available addressing the substrate selectivity of transition-metal and enzyme-catalyzed methods for the preparation of substituted phenyllactic or more general aryllactic acids. We report herein comparative results for Rh-DiPAMP (DiPAMP = 1,2-ethandiylbis[(o- methoxyphenyl)phenylphosphane]) and lactate dehydrogenase catalyzed enantioselective reductions of several 3-aryl-2-oxopropanoic acids. Phenyllactic acids are important constituents of depsipeptides, which are a large class of natural products expressing a wide range of biological activities. A comparative study of transition-metal and lactate dehydrogenase catalyzed enantioselective reductions of several 3-aryl-2-oxopropanoic acids as valuable sources for enantiomerically pure phenyllactic acids is described. Copyright

SUBSTITUTED BETA-PHENYL-ALPHA-HYDROXY PROPANOIC ACID, SYNTHESIS METHOD AND USE THEREOF

The present invention relates to a compound of the formula (I), wherein R1, R2 and R3 are each independently selected from H, OH, F, Cl, Br, methoxy and ethoxy; or alternatively, R1 and R2 together form -OCH2O-, R3 is selected from H, OH, methoxy, ethoxy and halogens; R4 is OH or acyloxy; R5 is cycloalkoxyl, amino and substituted amino, and when R5 is selected from amino, at least one of R1, R2 and R3 is not H. The present invention further relates to a process for synthesizing a compound of the formula (I), and use of the compound of the formula (I) in the manufacture of a medicament for the prevention or treatment of cardiovascular or cerebrovascular diseases.

Biocatalytic racemization of aliphatic, arylaliphatic, and aromatic α-hydroxycarboxylic acids

Biocatalytic racemization of a range of aliphatic, (aryl)aliphatic, and aromatic α-hydroxycarboxylic acids was accomplished by using whole resting cells of a range of Lactobacillus spp. The mild (physiological) reaction conditions ensured an essentially "clean" isomerization in the absence of side reactions, such as elimination or decomposition. Whereas straight-chain aliphatic 2-hydroxy-carboxylic acids were racemized with excellent rates (up to 85% relative to lactate), steric hindrance was observed for branched-chain analogues. Good rates were observed for aryl-alkyl derivatives, such as 3-phenyllactic acid (up to 59%) and 4-phenyl-2-hydroxybutanoic acid (up to 47%). In addition, also mandelate and its o-chloro analogue were accepted at a fair rate (45%). This biocatalytic racemization represents an important tool for the deracemization of a number of pharmaceutically important building blocks.

Deracemisation of aryl substituted α-hydroxy esters using Candida parapsilosis ATCC 7330: Effect of substrate structure and mechanism

Candida parapsilosis ATCC 7330 was found to be an efficient biocatalyst for the deracemisation of aryl α-hydroxy esters (65-85% yield and 90-99% ee). A variety of aryl and aryl substituted α-hydroxy esters were synthesized to reflect steric and electronic effects on biocatalytic deracemisation. The mechanism of this biocatalytic deracemisation was found to be stereoinversion.