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.

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.

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.