Retention of the label during the conversion of [3-3H] squalene into (3S)-2,3-oxidosqualene catalyzed by mammalian squalene oxidase.
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 could be observed, ruling out a mechanism involving, e.g., an iron carbene type species at C-3.
Boutaud
O
O
Laboratoire de Chimie Bioorganique (URA CNRS 1386), Faculté de Pharmacie, Strasbourg-Illkirch, France.
Ceruti
M
M
Cattel
L
L
Schuber
F
F
D000818:Animals; D001711:Biotransformation; D007810:Lanosterol / Q000378:metabolism; D008862:Microsomes, Liver / Q000201:enzymology*; D009251:NADPH-Ferrihemoprotein Reductase / Q000302:isolation & purification / Q000378:metabolism; D010105:Oxygenases / Q000302:isolation & purification / Q000378:metabolism*; D011865:Radioisotope Dilution Technique; D013185:Squalene / Q000031:analogs & derivatives / Q000032:analysis / Q000378:metabolism*; D050603:Squalene Monooxygenase; D013552:Swine; D014316:Tritium
C002821:2,3-oxidosqualene; D014316:Tritium; D007810:Lanosterol; D013185:Squalene; D010105:Oxygenases; D050603:Squalene Monooxygenase; D009251:NADPH-Ferrihemoprotein Reductase