Lipases A and B from Candida antarctica in the enantioselective acylation of ethyl 3-heteroaryl-3-hydroxypropanoates: aspects on the preparation and enantiopreference

Synthesis of new optically pure tetrabromobenzotriazole derivatives via lipase-catalyzed transesterification

“…The best results are achieved if a large difference in size of the two substituents next to the hydroxyl-attached carbon occurs within the structure of the alcohol [14]. Many factors have an impact on the results of the reaction: lipase type [15][16][17][18], temperature [19], solvent [20][21][22], water content [23] as well as acyl donor [24,25], changing the reaction enantioselectivity factor E [26] or even reversing enantiopreference of the catalyst [23,27]. An enantioselective resolution of similar compounds has been previously reported [19].…”

Lipase-catalyzed synthesis of the chiral tetrahydroisoquinoline (R)-salsolinol

“…Over the last two decades, a new methodology using an enzyme as the resolution catalyst has been intensively developed for the synthesis of enantiomerically pure amines and their derivatives mainly via enzymatic hydrolysis, 11 aminolysis, 12 acylation, 13,14 and alkoxycarbonylation processes. 15 Enzyme-catalyzed methods have also shown their potential in the preparation of secondary amines.…”

Candida antarctica Lipase A-Based Enantiorecognition of a Highly Strained 4-Dibenzocyclooctynol (DIBO) Used for PET Imaging

“…Furthermore, two fused benzene rings with a cyclooctyne ring makes DIBO highly strained and, therefore, the enantiomers of DIBO have so far remained unseparated. Among the few known enzymes acting on this type of substrates, lipase A from Candida antarctica (CAL-A) is known to accept bulky secondary alcohols [6,7] and similar amines [8,9].substrates that are seldom accepted by other lipases.We investigated the ability of lipases and especially CAL-A to separate the enantiomers of DIBO using detailed enzyme-substrate interaction analysis through in silico docking. Additionally, even though CAL-A is not a metalloenzyme [10], Mg 2+ was suspected to interact with CAL-A and potential binding sites for Mg 2+ were predicted.…”

“…">Results and DiscussionSelection of enzyme and solvent: Altogether, 18 hydrolases, mostly lipases (listed in the Materials and Methods section), were screened for the O-acylation of DIBO (rac-1; 5.0 mM) with vinyl acetate (150 mM; R 1 =Me, R 2 = CH=CH2; Scheme 1) in methyl tert-butyl ether (MTBE). The preliminary reaction conditions were based on our earlier works and optimization studies with CAL-A [6,8]. Most of the evaluated hydrolases did not accept DIBO as a substrate.…”

“…Furthermore, two fused benzene rings with a cyclooctyne ring makes DIBO highly strained and, therefore, the enantiomers of DIBO have so far remained unseparated. Among the few known enzymes acting on this type of substrates, lipase A from Candida antarctica (CAL-A) is known to accept bulky secondary alcohols [6,7] and similar amines [8,9].…”