title: Characterization and engineering of an o-xylene dioxygenase for biocatalytic applications.
abstract: 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.
authors.affiliation: Department of Systems Biology, Yonsei University, Seoul 120-749, Republic of Korea.
authors.forename: Dockyu
authors.initials: D
authors.lastname: Kim
authors.forename: Miyoun
authors.initials: M
authors.lastname: Yoo
authors.forename: Ki Young
authors.initials: KY
authors.lastname: Choi
authors.forename: Beom Sik
authors.initials: BS
authors.lastname: Kang
authors.forename: Eungbin
authors.initials: E
authors.lastname: Kim
mesh_terms: D001426:Bacterial Proteins / Q000096:biosynthesis* / Q000235:genetics* / Q000378:metabolism*; D002384:Catalysis; D049308:Dioxygenases / Q000096:biosynthesis* / Q000235:genetics* / Q000378:metabolism*; D006841:Hydrocarbons, Aromatic / Q000378:metabolism*; D057927:Hydrophobic and Hydrophilic Interactions; D006900:Hydroxylation; D008958:Models, Molecular; D015202:Protein Engineering / Q000379:methods*
chemical_list: D001426:Bacterial Proteins; D006841:Hydrocarbons, Aromatic; D049308:Dioxygenases; C551337:o-xylene dioxygenase, Rhodococcus
keywords: Aromatic dioxygenases; Biocatalysis; Regioselective hydroxylation; Rhodococcus; cis-Dihydrodiols