119067-75-3Relevant academic research and scientific papers
Engineering the promiscuous racemase activity of an arylmalonate decarboxylase
Kourist, Robert,Miyauchi, Yusuke,Uemura, Daisuke,Miyamoto, Kenji
experimental part, p. 557 - 563 (2011/03/21)
Variant G74C of arylmalonate decarboxylase (AMDase) from Bordatella bronchoseptica has a unique racemising activity towards profens. By protein engineering, variant G74C/V43A with a 20-fold shift towards promiscuous racemisation was obtained, based on a reduced activity in the decarboxylation reaction and a two-fold increase in the racemisation activity. The mutant showed an extended substrate range, with a 30-fold increase in the reaction rate towards ketoprofen. Molecular dynamics simulations and the substrate profile of the racemase indicate that the steric and polar effects of the substrate structure play a more dominant role on catalysis than mere kinetic α-proton acidity. The observation that the conversion of β,γ-unsaturated carboxylic acids does not lead to a rearrangement to form their α,β isomers indicates a concerted rather than a stepwise mechanism. Interestingly, a substrate bearing a nitro group instead of the carboxylic acid group on the α-carbon atom was also converted by the racemase.
An efficient laboratory synthesis of α-deuteriated profens
Coumbarides, Gregory S.,Dingjan, Marco,Eames, Jason,Flinn, Anthony,Northen, Julian
, p. 903 - 914 (2008/02/09)
An efficient and practical laboratory synthesis of a series of 2-deuterio-2-arylpropionic acids (α-deuterioprofens) is described. The levels of deuterium incorporation are high and the products are synthetically useful. Copyright
