216872-00-3Relevant academic research and scientific papers
Purification, properties and reactivity of the esterase from Micrococcus sp.
Imura, Akihiro,Itoh, Motohiro,Miyadera, Akihiko
, p. 654 - 656 (2007/10/03)
The esterase from Micrococcus sp., which hydrolyzes n-propyl-2- fluorocyclopropanecarboxylate (3) enantioselectively, was highly purified by three types of chromatography. The purified enzyme was inactivated by Hg and diisopropyl fluorophosphate (DFP). It was a monomer with a molecular weight of about 35000. The enzyme exhibits esterase activity towards many aliphatic propyl esters. The enantioselectivity for substrate (3) using purified enzyme did not differ from that of crude enzyme.
Resolution of cis-2-fluorocyclopropanecarboxylic acid by a microbial enantioselective hydrolysis
Imura, Akihiro,Itoh, Motohiro,Miyadera, Akihiko
, p. 3047 - 3052 (2007/10/03)
The important key intermediate of quinolone analogue synthesis, (1S,2S)- 2-fluorocyclopropanecarboxylic acid, was prepared enantioselectively by a microbial resolution. One of the strains with the highest enzymatic specificity was selected from soil and when lyophilized cells were treated with corresponding ester, the remaining (1S,2S)-ester was obtained with high enantiomeric purity (98% e.e.).
