172585-58-9Relevant articles and documents
Palladium-catalyzed γ -selective and stereospecific allyl-aryl coupling between allylic acetates and arylboronic acids
Ohmiya, Hirohisa,Makida, Yusuke,Tanaka, Tatsunori,Sawamura, Masaya
supporting information; experimental part, p. 17276 - 17277 (2009/07/19)
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Enantioselective acylation of primary and secondary alcohols catalyzed by lipase QL from Alcaligenes sp.: A predictive active site model for lipase QL to identify which enantiomer of an alcohol reacts faster in this acylation
Naemura, Koichiro,Murata, Masaki,Tanaka, Rie,Yano, Masashi,Hirose, Keiji,Tobe, Yoshito
, p. 3285 - 3294 (2007/10/03)
Lipase QL (from Alcaligenes sp.)-catalyzed acylation of alcohols using isopropenyl acetate as the acylating agent in diisopropyl ether converted preferentially primary alcohols with an S configuration and secondary alcohols with an R configuration into the corresponding homochiral acetates. On the basis of observed enantiomer selectivities, a predictive active site model for lipase QL is proposed for identifying which enantiomer of a primary or a secondary alcohol reacts faster in this acylation. Copyright (C) 1996 Published by Elsevier Science Ltd.
Lipase YS-catalysed Acylation of Alcohols: a Predictive Active Site Model for Lipase YS to Identify which Enantiomer of a Primary or a Secondary Alcohol Reacts Faster in this Acylation
Naemura, Koichiro,Fukuda, Ritsuko,Konishi, Masayoshi,Hirose, Keiji,Tobe, Yoshito
, p. 1253 - 1256 (2007/10/02)
Primary alcohols having a hydroxymethyl group at an S chiral centre and secondary alcohols with an R configuration are preferentially acylated to give the corresponding acetates by lipase YS-catalysed acylation in diisopropyl ether; a predictive cubic-spaced active site model for lipase YS is proposed for identifying which enantiomer of a primary or a secondary alcohol reacts faster in this acylation.