Biocatalytic synthesis of dihydroxynaphthoic acids by cytochrome P450 CYP199A2.
CYP199A2, a bacterial P450 monooxygenase from Rhodopseudomonas palustris, was found to exhibit oxidation activity towards three hydroxynaphthoic acids. Whole cells of the recombinant Escherichia coli strain expressing CYP199A2 efficiently catalyzed the regioselective oxidation of 1-, 3-, and 6-hydroxy-2-naphthoic acids to produce 1,7-, 3,7-, and 6,7-dihydroxynaphthoic acid respectively. These results suggest that CYP199A2 might be a useful oxidation biocatalyst for the synthesis of dihydroxynaphthoic acids.
Furuya
Toshiki
T
Department of Applied Chemistry, Faculty of Science and Engineering, Waseda University, Tokyo, Japan.
Kino
Kuniki
K
D055162:Biocatalysis; D002851:Chromatography, High Pressure Liquid; D003577:Cytochrome P-450 Enzyme System / Q000378:metabolism*; D009284:Naphthols / Q000737:chemistry / Q000378:metabolism*; D012241:Rhodopseudomonas / Q000201:enzymology
D009284:Naphthols; D003577:Cytochrome P-450 Enzyme System