Abstract：
:8-dimethylallylnaringenin (8-DMAN) 2'-hydroxylase, which is indispensable for the formation of a lavandulylated flavanone, sophoraflavanone G, was detected in cell suspension cultures of Sophora flavescens. The enzyme catalyzes the 2'-hydroxylation of 8-DMAN to leachianone G, and is tightly bound to the membrane. It required NADPH and molecular oxygen as cofactors, and was inhibited by several cytochrome P450 inhibitors such as carbon monoxide and cytochrome c, indicating that the reaction is mediated by a cytochrome P450 monooxygenase. The optimum pH of 8-DMAN 2'-hydroxylase was 8.5, and the enzyme hydroxylated only 8-DMAN. Apparent Km values for 8-DMAN and NADPH of the enzyme were 55 and 34 microM, respectively.
journal_name
Phytochemistryjournal_title
Phytochemistryauthors
Yamamoto H,Yatou A,Inoue Kdoi
10.1016/s0031-9422(01)00270-9subject
Has Abstractpub_date
2001-11-01 00:00:00pages
671-6issue
5eissn
0031-9422issn
1873-3700pii
S0031942201002709journal_volume
58pub_type
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