143292-80-2Relevant academic research and scientific papers
Directed evolution of an enantioselective lipase with broad substrate scope for hydrolysis of α-substituted esters
Engstroem, Karin,Nyhlen, Jonas,Sandstroem, Anders G.,Baeckvall, Jan-E.
supporting information; experimental part, p. 7038 - 7042 (2010/07/05)
A variant of Candida antarctica lipase A (CalA) was developed for the hydrolysis of α-substituted p-nitrophenyl esters by directed evolution. The E values of this variant for 7 different esters was 45-276, which is a large improvement compared to 2-20 for the wild type. The broad substrate scope of this enzyme variant is of synthetic use, and hydrolysis of the tested substrates proceeded with an enantiomeric excess between 95-99%. A 30-fold increase in activity was also observed for most substrates. The developed enzyme variant shows (R)-selectivity, which is reversed compared to the wild type that is (S)-selective for most substrates.
Nitrogen Participation in the Deacylation of D-Glucosamine and α-Chymotrypsin Derivatives. Explanation of the Stereospecificity of Acyl-α-Chymotrypsin Hydrolysis
Oetvoes, Laszlo,Kraicsovits, Ferenc
, p. 5009 - 5014 (2007/10/02)
The hydrolysis of ethyl 3,4,6-tri-O-acetyl-2-deoxy-2-amino-β-D-glucopyranoside and acylated α-chymotrypsins has been investigated.Both transformations are catalyzed by neighbouring nitrogen atom participation.The stereospecificity of acylated enzyme hydrolysis can be explained by the specific steric hindrance of nitrogen participation.Keywords: selective deacylation, stereospezific ester hydrolysis, acylated derivatives of α-chymotrypsin, 2-amino-2-deoxy-glucose
