Characterization and engineering of an o-xylene dioxygenase for biocatalytic applications.
Depending on the size and position of the substituent groups on the aromatic ring, the o-xylene dioxygenase from Rhodococcus sp. strain DK17 possesses the unique ability to perform distinct regioselective hydroxylations via differential positioning of substrates within the active site. The substrate-binding pocket of the DK17 o-xylene dioxygenase is large enough to accommodate bicyclics and can be divided into three regions (distal, central, and proximal), and hydrophobic interactions in the distal position are important for substrate binding. Current molecular and functional knowledge contribute insights into how to engineer this enzyme to create tailor-made properties for chemoenzymatic syntheses.
['Kim|Dockyu|D|', 'Yoo|Miyoun|M|', 'Choi|Ki Young|KY|', 'Kang|Beom Sik|BS|', 'Kim|Eungbin|E|']
D001426:Bacterial Proteins D002384:Catalysis D049308:Dioxygenases D006841:Hydrocarbons, Aromatic D057927:Hydrophobic and Hydrophilic Interactions D006900:Hydroxylation D008958:Models, Molecular D015202:Protein Engineering
Rhodococcus Regioselective hydroxylation Aromatic dioxygenases Biocatalysis cis-Dihydrodiols