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. isopropyl 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.
The marine transaminase, P-ω-TA, can be employed for the oxidative deamination of 1-aminotetralins and 1-aminoindanes. While 4-substituents are tolerated on the tetralin core, the presence of 3- or 8- substituents...
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