Technologies enabling new enzyme discovery and efficient protein engineering have spurred intense interest in the development of biocatalytic reactions. In recent years, whole-cell biocatalysis has received attention as a simple, efficient, and scalable biocatalytic reaction platform. Inspired by these developments, we have established a whole-cell protocol for oxidative dearomatization of phenols using the flavin-dependent monooxygenase, TropB. This approach provides a scalable biocatalytic platform for accessing gram-scale quantities of chiral synthetic building blocks.
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| http://www.ncbi.nlm.nih.gov/pmc/articles/PMC6538480 | PMC |
| http://dx.doi.org/10.1111/cbdd.13443 | DOI Listing |
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Article Synopsis
- The study focuses on l-Tryptophan decarboxylase (TDC) and l-3,4-dihydroxyphenylalanine decarboxylase (DDC), which are enzymes that catalyze the decarboxylation of specific amino acids.
- Researchers analyzed the amino acid compositions of the substrate-binding pockets in both enzymes, identifying key amino acids that affect substrate selectivity and catalytic activity.
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