127047-08-9Relevant articles and documents
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
Reverse chemoselective borane reduction of an optically active malonic acid ester
Fadel,Canet,Salaun
, p. 6687 - 6690 (2007/10/02)
Reduction of the 2-methyl-2-p-tolylmalonic monoester (+)-2 with the borane-dimethylsulfide complex took place unexpectedly on the ester function, providing the β-hydroxy-acid (-)-3. This chemoselective reaction proceeded likely through formation of a six-