62247-44-3Relevant articles and documents
Discovery and Design of Family VIII Carboxylesterases as Highly Efficient Acyltransferases
Müller, Henrik,Godehard, Simon P.,Palm, Gottfried J.,Berndt, Leona,Badenhorst, Christoffel P. S.,Becker, Ann-Kristin,Lammers, Michael,Bornscheuer, Uwe T.
supporting information, p. 2013 - 2017 (2020/11/30)
Promiscuous acyltransferase activity is the ability of certain hydrolases to preferentially catalyze acyl transfer over hydrolysis, even in bulk water. However, poor enantioselectivity, low transfer efficiency, significant product hydrolysis, and limited substrate scope represent considerable drawbacks for their application. By activity-based screening of several hydrolases, we identified the family VIII carboxylesterase, EstCE1, as an unprecedentedly efficient acyltransferase. EstCE1 catalyzes the irreversible amidation and carbamoylation of amines in water, which enabled the synthesis of the drug moclobemide from methyl 4-chlorobenzoate and 4-(2-aminoethyl)morpholine (ca. 20 % conversion). We solved the crystal structure of EstCE1 and detailed structure–function analysis revealed a three-amino acid motif important for promiscuous acyltransferase activity. Introducing this motif into an esterase without acetyltransferase activity transformed a “hydrolase” into an “acyltransferase”.
The Candida antarctica lipase B catalysed kinetic resolution of seudenol in non-aqueous media of controlled water activity
Orrenius,Norin,Hult,Carrea
, p. 3023 - 3030 (2007/10/03)
For further ivestigation of the kinetic resolutions in transesterification reactions with the highly enantioselective Candida antarctica lipase B, an easy to study model reaction with one typical substrate, the Douglas Fir Beetle pheromone 3-methyl-2-cycl
Pheromone Synthesis, CXI. - An Enzyme-Mediated Synthesis of Both Enantiomers of Seudenol and 1-Methyl-2-cyclohexen-1-ol, the Aggregation Pheromones of Dendroctonus pseudotsugae
Mori, Kenji,Ogoche, Jondiko I.J.
, p. 903 - 906 (2007/10/02)
Enzymatic resolution of seudenol acetate by pig liver esterase has led to an efficient preparation of both the enantiomers of seudenol and 1-methyl-2-cyclohexen-1-ol, the aggregation pheromones of the Douglas-fir beetle Dendroctonus pseudotsugae Hopkins.