A soluble Bacillus cereus cytochrome P-450cin system catalyzes 1,4-cineole hydroxylations.
AUTOR(ES)
Liu, W
RESUMO
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.
ACESSO AO ARTIGO
http://www.pubmedcentral.nih.gov/articlerender.fcgi?artid=182545Documentos Relacionados
- Microbial Hydroxylation of 1,4-Cineole
- A Role of the Putidaredoxin COOH-terminus in P-450cam (Cytochrome m) Hydroxylations*
- Plant Expression of a Bacterial Cytochrome P450 That Catalyzes Activation of a Sulfonylurea Pro-Herbicide.
- Nucleotide sequence of cytochrome P450 L1A1 (lanosterol 14 alpha-demethylase) from Candida albicans.
- InvestigaÃÃo dos mecanismos de aÃÃo da atividade gastroprotetora de 1,4-cineol em modelos de Ãlcera gÃstrica em camundongos.
