Liu W, Rosazza J P
Division of Medicinal and Natural Product Chemistry, University of Iowa, Iowa City 52242.
Appl Environ Microbiol. 1993 Nov;59(11):3889-93. doi: 10.1128/aem.59.11.3889-3893.1993.
A cytochrome P-450-dependent monooxygenase system that catalyzes the stereospecific hydroxylation of the monoterpene substrate 1,4-cineole was demonstrated in cell-free preparations of Bacillus cereus UI-1477. 1,4-Cineole hydroxylations were catalyzed by a 100,000 x g (1-h)-centrifuging soluble, hexane-inducible enzyme that activated and incorporated molecular oxygen into hydroxylated products; required NADH; was inhibited by SKF-525A, imidazole, metyrapone, and octylamine; and displayed a 452-nm peak in the carbon monoxide difference absorption spectrum. The constant 7:1 ratio of endo/exo alcohol products formed when 1,4-cineole was hydroxylated by normal cells, hexane-induced cells, and cell extracts suggested that a single enzyme designated cytochrome P-450cin was responsible for both reactions.
在蜡样芽孢杆菌UI - 1477的无细胞制剂中,证实了一种细胞色素P - 450依赖性单加氧酶系统,该系统催化单萜底物1,4 - 桉叶素的立体特异性羟基化反应。1,4 - 桉叶素的羟基化反应由一种经100,000×g(1小时)离心的可溶性、己烷诱导型酶催化,该酶能激活分子氧并将其掺入羟基化产物中;需要NADH;受SKF - 525A、咪唑、甲吡酮和辛胺抑制;并且在一氧化碳差示吸收光谱中显示出452 nm的峰。当正常细胞、己烷诱导细胞和细胞提取物对1,4 - 桉叶素进行羟基化反应时,形成的内/外型醇产物的恒定7:1比例表明,一种名为细胞色素P - 450cin的单一酶负责这两种反应。