In silico and in vitro exploration of a tyrosinase for biocatalytic production of catechols
James Britton, Fang Zhao, Reeta Davis, Meg Walsh, Kevin E O'Connor, David O'Connell, Tanja Narancic · 2026
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Description
James Britton and co-authors explore a bacterial tyrosinase enzyme for making catechols, prized building blocks of fine goods, in 2026. Most such enzymes prefer two ring substrates, yet the Ralstonia enzyme unusually favors single ring phenols. Docking runs on shape models plus bench rate tests covered eleven trade fit feeds.
Three contact residues in the active site explained much of the binding pattern. Bench tests proved wide feed uptake, with resveratrol and tyrosol handled fastest. Side chain branching and end groups steered activity strongly. Knowing the rules helps design greener ways to make antioxidants, drugs, and flavor goods.
Catalog record
| CREATOR | James Britton, Fang Zhao, Reeta Davis, Meg Walsh, Kevin E O'Connor, David O'Connell, Tanja Narancic |
|---|---|
| YEAR | 2026 |
| COLLECTION | PAPERS |
| FORMAT | TXT |
| FILE SIZE | 53 KB |
| LICENSE | https://creativecommons.org/licenses/by/4.0 |
| RIGHTS | CC BY |
| SOURCE | Europe PMC |