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+.
|ジャーナル||Biochimica et Biophysica Acta (BBA)/Lipids and Lipid Metabolism|
|出版ステータス||Published - 1985 7 9|
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