194922-79-7Relevant academic research and scientific papers
Synthesis of Chiral Cyclic Alcohols from Chiral Epoxides by H or N Substitution with Frontside Displacement
Da Silva Gomes, Roberto,Reddy, Karla Mahender,Corey
supporting information, p. 6310 - 6313 (2018/10/09)
Diverse examples are provided of enantioselective sequences for the transformation of cycloalkenes to either chiral trans-β-substituted cycloalkanols or chiral α-amino ketones.
Conformational effects on lipase-mediated acylations of 2-substituted cyclohexanols
Tanikaga, Rikuhei,Matsumoto, Yoshimasa,Sakaguchi, Maki,Koyama, Yohei,Ono, Kentaro
, p. 6781 - 6783 (2007/10/03)
Lipase-mediated acetylations of trans- and cis-2-substituted cyclohexanols gave the corresponding (1R)-cyclohexyl acetates and (1S)-cyclohexanols in high yields and ee, but c-4-tert-butyl-c-2-ethenyl-r-1-cyclohexanol was unreactive owing to the steric interaction between the axial OH group and the axial H atoms at the 3- and 5-positions. In the cis-isomer the OH group occupies an equatorial position to bind to the lipase, and less bulky axial alkenyl and alkynyl groups might not so much prevent acetylations than an alkyl group.
ENZYMATIC "IN VITRO" REDUCTION OF KETONES VII. (1) Reduction rates and stereochemistry of the HLAD catalyzed reduction of 2-alkyl cyclohexanones, dimethyl cyclohexanones, cycloalkanones and bicycloalkanones.
Osselaer, T. A. Van,Lemiere, G. L.,Lepoivre, J. A.,Alderweireldt, F. C.
, p. 389 - 398 (2007/10/02)
Values for the rate constants of the catalytic step HLAD-NADH + ketone -> HLAD-NAD1+ + alcohol in the HLAD catalyzed reduction of some 2-alkyl cyclohexanones, geminal dimethyl cyclohexanones, cycloalkanones and bicyclic ketones are presented.Also the thermodynamic parameters of activation are given and they are compared with the activation parameters of the NaBH4 reduction leading to a better understanding of some forces at work in enzymatic catalysis.The results are rationalized in the same way as was previously done for the 3-alkyl and 4-alkyl cyclohexanones.A reaction model is obtained in which steric hindrances and hydrophobic zones are responsible for rate decreasing, respectively increasing interactions between enzyme and substrates.
