title: Mevalonate-dependent enzymatic synthesis of amorphadiene driven by an ATP-regeneration system using polyphosphate kinase.
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.
authors.affiliation: Graduate School of Agriculture, Tokyo University of Agriculture and Technology, 3-5-8 Saiwaicho, Fuchu, Tokyo 183-8509, Japan.
authors.forename: Manami
authors.initials: M
authors.lastname: Shimane
authors.forename: Yoshinori
authors.initials: Y
authors.lastname: Sugai
authors.forename: Ryosuke
authors.initials: R
authors.lastname: Kainuma
authors.forename: Masahiro
authors.initials: M
authors.lastname: Natsume
authors.forename: Hiroshi
authors.initials: H
authors.lastname: Kawaide
mesh_terms: D000255:Adenosine Triphosphate / Q000737:chemistry*; D001426:Bacterial Proteins / Q000737:chemistry* / Q000235:genetics; D055162:Biocatalysis; D003001:Cloning, Molecular; D004926:Escherichia coli / Q000235:genetics; D009682:Magnetic Resonance Spectroscopy; D008798:Mevalonic Acid / Q000737:chemistry*; D017856:Phosphotransferases (Phosphate Group Acceptor) / Q000737:chemistry* / Q000235:genetics; D000081223:Polycyclic Sesquiterpenes; D011122:Polyphosphates / Q000737:chemistry; D011994:Recombinant Proteins / Q000737:chemistry / Q000235:genetics; D012717:Sesquiterpenes / Q000138:chemical synthesis*; D012996:Solutions
chemical_list: D001426:Bacterial Proteins; D000081223:Polycyclic Sesquiterpenes; D011122:Polyphosphates; D011994:Recombinant Proteins; D012717:Sesquiterpenes; D012996:Solutions; C515348:amorpha-4,11-diene; D000255:Adenosine Triphosphate; D017856:Phosphotransferases (Phosphate Group Acceptor); C022424:polyphosphate kinase; D008798:Mevalonic Acid