Abstract
The prenyl transferase, farnesyl pyrophosphate (FPP) synthase, which catalyzes the head-to-tail couplings of dimethylallyl pyrophosphate (DMAPP) and geranyl pyrophosphate (GPP) with isopentenyl pyrophosphate (IPP), is a key enzyme in juvenile hormone (JH) biosynthesis. While moderate FPP synthase activity has been found in whole-body insect preparations, enzymatic activity in the corpus allatum, the gland responsible for JH biosynthesis, has been elusive. A new procedure for examining corpora allata prenyl transferase activity in the lepidopteran Manduca sexta is described. In contrast to most other short-chain prenyl transferases, the larval enzyme requires detergent for activity. Optimum conversion of DMAPP and GPP to FPP is obtained with corpora allata homogenates containing 2% Triton X-100, 0.15% bovine serum albumin, and 25% glycerol. The enzyme is activated in the presence of Mn2+ or Mg2+ and is inactivated by the addition of N-ethylmaleimide. Keywords: Insect prenyl transferase; farnesyl pyrophosphate synthase; juvenile hormone biosynthesis; Manduca sexta; corpora allata
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