Oliver Boutaud

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Squalene epoxidase is the only known flavoprotein that catalyzes the epoxidation of an olefin. In order to test the possibility of a catalytic non-heme metal-based mechanism, the conversion of chemically synthesized [3-3H]squalene into [3H]2,3-oxidosqualene, by partially purified pig liver squalene epoxidase, was studied. No exchange of the labeled hydrogen(More)
Small intestinal ulcers are frequent complications of therapy with nonsteroidal anti-inflammatory drugs (NSAIDs). We present here a genetic deficiency of eicosanoid biosynthesis that illuminates the mechanism of NSAID-induced ulcers of the small intestine. Eicosanoids and metabolites were measured by isotope dilution with mass spectrometry. cDNA was(More)
The inhibition of 2,3-oxidosqualene-lanosterol cyclase (EC 5.4.99.7) (OSC) by new azasqualene derivatives, mimicking the proC-8 and proC-20 carbocationic high-energy intermediates of the cyclization of 2,3-oxidosqualene to lanosterol, was studied using pig liver microsomes, partially purified preparations of OSC, and yeast microsomes. The azasqualene(More)
Kinetic studies on the cyclization of 2,3(S)-oxido and 2,3(S):22(S),23-dioxido[14C]squalene catalyzed by liver oxidosqualene-lanosterol cyclase revealed a specificity (in terms of V/Km) of the enzyme for the diepoxide. The specificity ratio was dependent on the enzyme preparation, i.e. purified or microsomal, and was highest (about 5) with the microsomal(More)
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