Polyphosphate kinase (PPK), which can regenerate ATP from ADP, was utilized in the mevalonate-dependent enzymatic synthesis of amorphadiene. The activity of PPK, cloned from Escherichia coli, was determined by 31P-NMR. The yield from the PPK-catalyzed synthesis was 25%, 2.5 times higher than that without PPK. The 31P-NMR analysis of the final reaction mixture indicated no accumulation of intermediates.
