ENZYMATIC 10-HYDROXYLATION AND 10-O-METHYLATION OF DIHYDROSANGUINARINE IN DIHYDROCHELIRUBINE FORMATION BY ESCHSCHOLTZIA
ENZYMATIC 10-HYDROXYLATION AND 10-O-METHYLATION OF DIHYDROSANGUINARINE IN DIHYDROCHELIRUBINE FORMATION BY ESCHSCHOLTZIA
复制标题
DOI：
10.1016/0031-9422(92)83617-8
复制
发表时间：
1992-08-01
期刊：
影响因子：
3.8
通讯作者：
ZENK, MH
中科院分区：
文献类型：
--
作者：
DEEKNAMKUL, W;TANAHASHI, T;ZENK, MH
从加州石杉细胞悬浮培养物的无细胞提取物中发现了两种参与苯并菲啶生物碱生物合成的新酶：二氢血根碱-10-羟化酶和10-羟基二氢血根碱-10-O-甲基转移酶。羟化酶是一种微粒体相关的细胞色素P-450依赖性单加氧酶，特异性作用于二氢血根碱的C-10。甲基转移酶，富集60倍和部分特征，甲基化只有羟基部分在C-10形成二氢chelirubine。这两种酶被发现是高度底物特异性。
Two new enzymes involved in benzophenanthridine alkaloid biosynthesis, dihydrosanguinarine-10-hydroxylase and 10-hydroxydihydrosanguinarine-10-O-methyltransferase, have been found in cell-free extracts derived from Eschscholtzia californica cell suspension cultures. The hydroxylase is a microsome-associated, cytochrome P-450-dependent monooxygenase which acts specifically at C-10 of dihydrosanguinarine. The methyltransferase, enriched 60-fold and partially characterized, methylates only the hydroxyl moiety at C-10 to form dihydrochelirubine. Both enzymes were found to be highly substrate specific.