Gavin, DP;Murphy, EJ;Foley, AM;Castilla, IA;Reen, FJ;Woods, DF;Collins, SG;O'Gara, F;Maguire, AR

2019

June

Advanced Synthesis and Catalysis

Identification of an Esterase Isolated Using Metagenomic Technology which Displays an Unusual Substrate Scope and its Characterisation as an Enantioselective Biocatalyst

Validated

Altmetric: 12 ()

CHEMOENZYMATIC SYNTHESIS MARINE DISCOVERY ASPARAGINASE BIODISCOVERY RESOLUTIONS EFFICIENCY TETRALONES STRATEGIES LIBRARIES

361

2466

2474

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 beta-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 beta-carbon.

WEINHEIM

1615-4150

10.1002/adsc.201801691