References
- Boutaud O, Ceruti M, Cattel L, Schuber F. Retention of the label during the conversion of [3-3H] squalene into (3S)-2,3-oxidosqualene catalyzed by mammalian squalene oxidase. Biochem Biophys Res Commun 1995; 208: 42–47
- Chugh A, Ray A, Gupta JB. Review squalene epoxidase as hypocholesterolemic drug target revisited. Prog Lipid Res 2003; 42: 37–50
- Collart FR, Huberman E. Cloning and sequence analysis of the human and Chinese hamster inosine-5′-monophosphate dehydrogenase cDNAs. J Biochem 1988; 263: 15769–15772
- Dubey VS, Bhalla R, Luthra R. An overview of the non-mevalonate pathway for terpenoid biosynthesis in plants. Indian Acad Sci 2003; 9: 637–646
- Gomelsky M, Klug G. A novel FAD-binding domain involved in sensory transduction in microorganisms. Trends Biochem Sci 2002; 27: 497–500
- Hong DY, Lau AJ, Yeo CL, Liu XK, Yang CR, Koh HL, et al. Genetic diversity and variation of saponin contents in Panax notoginseng roots from a single farm. Agric Food Chem 2005; 53: 8465–8467
- Jandrositz A, Turnowsky F, Hogenauer G. The gene encoding squalene epoxidase from Saccharomyces cerevisiae: Cloning and characterization. Gene 1991; 107: 155–160
- Kosuga K, Hata S, Osumi T, Sakakibara J. Nucleotide sequence of a cDNA for mouse sequalene epoxidase. Biochim Biophys Acta 1995; 1260: 345–348
- Lau AJ, Woo SO, Koh HL. Analysis of saponins in raw and steamed Panax notoginseng using high-performance liquid chromatography with diode array detection. J Chromatogr A 2003; 1011: 77–78
- Miyano M, Fukui K, Watanabe F, Takahashi S, Tada M, Kanashiro M, Miyake Y. Studies on Phe-228 and Leu-307 recombinant mutants of porcine kidney d-amino acid oxidase: Expression, purification, and characterization. J Biochem 1991; 109: 171–177
- Negri A, Ceciliani F, Tedeschi G, Simonic T, Ronchi S. The primary structure of the flavoprotein d-aspartate oxidase from beef kidney. J Biochem 1992; 267: 11865–11871
- Ruckenstuh C, Eidenberger A, Lang S, Turnowsky F. Single amino acid exchanges in FAD-binding domains of squalene epoxidase of Saccharomyces cerevisiae lead to either loss of functionality or terbinafine sensitivity. Biochem Soc 2005; 33: 1197–2010
- Sakakibara J, Watanabe R, Kanai Y. Molecular cloning and expression of rat squalene epoxidase. J Biochem 1995; 270: 17–20
- Satoh T, Horie M, Watanabe H, Tsuchiya Y, Kamei T. Enzymatic properties of squalene epoxidase from Saccharomyces cerevisiae. Biol Pharm Bull 1993; 6: 349–352