Add time:08/12/2019         Source:sciencedirect.com

Squalene synthetase of pig liver has been solubilized and partially purified. This enzyme has a pH optimum of 7.4 and a Km value of 5 × 10−7M for farnesyl pyrophosphate. A divalent metal ion, Mg++ or Mn++, and NADPH are required for the conversion of farnesyl pyrophosphate to squalene. Inhibition of the reaction is effected in the presence of nerolidyl pyrophosphate and SH inhibitors. Inhibition is also effected by farnesyl pyrophosphate at concentrations greater than 1.0 × 10−4M. Farnesyl pyrophosphate reacts with the enzyme to form an enzyme bound intermediate (C15) with the release of pyrophosphate. A C30-enzyme compound has also been isolated and this compound has been converted to squalene on addition of NADPH and Mg++ to the incubation mixture. A mechanism for the conversion of farnesyl pyrophosphate to squalene has been proposed from these findings.

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