772-14-5Relevant articles and documents
Asymmetric Hydrogenation of ?-Aryl Alkylidene Malonate Esters: Installing an Ester Group Significantly Increases the Efficiency
Zhao, Qian-Kun,Wu, Xiong,Li, Lin-Ping,Yang, Fan,Xie, Jian-Hua,Zhou, Qi-Lin
supporting information, p. 1675 - 1680 (2021/03/08)
Herein, we report a practical method for efficient asymmetric hydrogenation of β-aryl alkylidene malonates. With a site-specifically tailored chiral spiro iridium catalyst, a series of β-aryl alkylidene malonate esters were hydrogenated to afford chiral m
Folding Assessment of Incorporation of Noncanonical Amino Acids Facilitates Expansion of Functional-Group Diversity for Enzyme Engineering
Drienovská, Ivana,Gajdo?, Matú?,Kindler, Alexia,Takhtehchian, Mahsa,Darnhofer, Barbara,Birner-Gruenberger, Ruth,D?rr, Mark,Bornscheuer, Uwe T.,Kourist, Robert
supporting information, p. 12338 - 12342 (2020/09/07)
Protein design is limited by the diversity of functional groups provided by the canonical protein ?building blocks“. Incorporating noncanonical amino acids (ncAAs) into enzymes enables a dramatic expansion of their catalytic features. For this, quick identification of fully translated and correctly folded variants is decisive. Herein, we report the engineering of the enantioselectivity of an esterase utilizing several ncAAs. Key for the identification of active and soluble protein variants was the use of the split-GFP method, which is crucial as it allows simple determination of the expression levels of enzyme variants with ncAA incorporations by fluorescence. Several identified variants led to improved enantioselectivity or even inverted enantiopreference in the kinetic resolution of ethyl 3-phenylbutyrate.
Identification of an Esterase Isolated Using Metagenomic Technology which Displays an Unusual Substrate Scope and its Characterisation as an Enantioselective Biocatalyst
Gavin, Declan P.,Murphy, Edel J.,Foley, Aoife M.,Castilla, Ignacio Abreu,Reen, F. Jerry,Woods, David F.,Collins, Stuart G.,O'Gara, Fergal,Maguire, Anita R.
, p. 2466 - 2474 (2019/03/11)
Evaluation of an esterase annotated as 26D isolated from a marine metagenomic library is described. Esterase 26D was found to have a unique substrate scope, including synthetic transformations which could not be readily effected in a synthetically useful manner using commercially available enzymes. Esterase 26D was more selective towards substrates which had larger, more sterically demanding substituents (i. e. iso-propyl or tert-butyl groups) on the β-carbon, which is in contrast to previously tested commercially available enzymes which displayed a preference for substrates with sterically less demanding substituents (e.g. methyl group) at the β-carbon. (Figure presented.).
