Mevalonate-Dependent Enzymatic Synthesis of Amorphadiene Driven by an ATP-Regeneration System Using Polyphosphate Kinase
Author(s) -
Manami Shimane,
Yoshinori Sugai,
Ryosuke Kainuma,
Masahiro Natsume,
Hiroshi Kawaide
Publication year - 2012
Publication title -
bioscience biotechnology and biochemistry
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.509
H-Index - 116
eISSN - 1347-6947
pISSN - 0916-8451
DOI - 10.1271/bbb.120177
Subject(s) - polyphosphate , biochemistry , enzyme , yield (engineering) , escherichia coli , chemistry , atp synthase , kinase , phosphate , gene , materials science , metallurgy
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.
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