Prenyltransferases of Bacillus subtilis: Undecaprenyl Pyrophosphate Synthetase and Geranylgeranyl Pyrophosphate Synthetase1

Abstract

Undecaprenyl pyrophosphate synthetase and geranylgeranyl pyrophosphate synthe-tase were partially purified and characterized from Bacillus subtilis, from which heptaprenyl pyrophosphate synthetase and farnesyl pyrophosphate synthetase had previously been obtained [Takahashi et al. (1980) J. Biol. Chem. 255, 4539; (1981) J. Biochem. 89, 1581]. The undecaprenyl pyrophosphate synthetase catalyzed the Z-oligomerization of isopentenyl units with farnesyl pyrophosphate as a priming substrate to give C₅₀ and C₅₅ prenyl pyrophosphates with Z, E mixed stereochemistry. Various geometric isomers of C₁₀, C₁₅, C₂₀, and C₂₅ prenyl pyrophosphates also acted as priming substrates to give the corresponding isomeric products with chain lengths of C₅₀ and C₅₅, including unnatural products. In addition to absolute requirements for Mg²⁺ and detergent, the enzyme activity was further stimulated markedly by monovalent cations such as K⁺ and NH₄⁺. The geranylgeranyl pyrophosphate synthetase catalyzed C₅→ C₁₀→ C₁₅→ C₂₀ reactions to give E,E-farnesyl and E,E,E-geranylgeranyl pyrophosphates. This enzyme was not affected by monovalent cations or detergent.