Decaprenyl pyrophosphate synthetase from Paracoccus denitrificans

Decaprenyl pyrophosphate synthetase was partially purified from extracts of Paracoccus denitrificans. The enzyme catalyzed the synthesis of all-E-decaprenyl pyrophosphate from isopentenyl pyrophosphate and geranyl pyrophosphate, but it did not catalyze a reaction between isopentenyl pyrophosphate and dimethylallyl pyrophosphate. The Michaelis constants for geranyl, E,E-farnesyl pyrophosphate, and al-E-geranyl-geranyl pyrophosphate were 5.0 0.06, and 2.9 μM, respectively. The enzyme required detergent and Mg²⁺ for its catalytic activity and it was activated by monovalent cations such as K⁺ and NH₄⁺.