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ABSTRACT: 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 (31)P-NMR. The yield from the PPK-catalyzed synthesis was 25%, 2.5 times higher than that without PPK. The (31)P-NMR analysis of the final reaction mixture indicated no accumulation of intermediates.
Bioscience Biotechnology and Biochemistry 08/2012; 76(8):1558-60. DOI:10.1271/bbb.120177 · 1.06 Impact Factor