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Propanedioic acid, methyl(4-methylphenyl)-, dimethyl ester is a chemical with a specific purpose. Lookchem provides you with multiple data and supplier information of this chemical.

127047-04-5

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127047-04-5 Usage

Check Digit Verification of cas no

The CAS Registry Mumber 127047-04-5 includes 9 digits separated into 3 groups by hyphens. The first part of the number,starting from the left, has 6 digits, 1,2,7,0,4 and 7 respectively; the second part has 2 digits, 0 and 4 respectively.
Calculate Digit Verification of CAS Registry Number 127047-04:
(8*1)+(7*2)+(6*7)+(5*0)+(4*4)+(3*7)+(2*0)+(1*4)=105
105 % 10 = 5
So 127047-04-5 is a valid CAS Registry Number.

127047-04-5Relevant articles and documents

Microbial asymmetric decarboxylation of fluorine-containing arylmalonic acid derivatives

Miyamoto, Kenji,Tsuchiya, Shigeo,Ohta, Hiromichi

, p. 225 - 232 (2007/10/02)

α-Methyl-α-(trifluoromethylphenyl)malonic acids have been incubated with Alcaligenes bronchisepticus to afford optically active α-arylpropionic acids.Generally, the chemical and optical yields of the reaction products were higher when the substituents on the aromatic ring were strongly electron-withdrawing.Decarboxylation of α-fluoro-α-phenylmalonic acid with the aid of the same bacterium afforded optically active α-fluoro-α-phenylacetic acid.

Asymmetric Construction of Quaternary Carbons from Chiral Malonates: Selective and Versatile Total Syntheses of the Enantiomers of α- and β-Cuparenones from a Common Optically Active Precursor

Canet, Jean-Louis,Fadel, Antoine,Salauen, Jacques

, p. 3463 - 3473 (2007/10/02)

From a single chiron (R)-4, available with high enantiomeric purity (96percent) by simple enzymatic hydrolysis (PLE) of a prochiral malonate, were prepared convenient precursors of the two enantiomers of α- and β-cuparenones (1a,b and 2a,b).This versatile

Enzymes in organic synthesis 50. Probing the dimensions of the large hydrophobic binding region of the active site of pig liver esterase using substituted aryl malonate substrates

Toone,Jones

, p. 1041 - 1052 (2007/10/02)

The active side model reported recently for the synthetically useful enzyme pig liver esterase (PLE) permits the structural specificity and stereoselectivity of the enzyme to be interpreted and predicted for a wide range of substrates. The specifications

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