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+.
|Number of pages||7|
|Journal||Biochimica et Biophysica Acta (BBA)/Lipids and Lipid Metabolism|
|Publication status||Published - 1985 Jul 9|
- (P. denitrificans)
- Decaprenyl pyrophosphate synthetase
ASJC Scopus subject areas