作者:Toshiki FURUYA、Kuniki KINO
DOI:10.1271/bbb.90624
日期:2009.12.23
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.
CYP199A2是来自水稻假单胞菌的细菌P450单氧化酶,发现其对三种羟基萘酸具有氧化活性。表达CYP199A2的重组大肠杆菌全细胞有效催化了1-、3-和6-羟基-2-萘酸的区域选择性氧化,分别生成1,7-、3,7-和6,7-二羟基萘酸。这些结果表明,CYP199A2可能是合成二羟基萘酸的有用氧化生物催化剂。