PMID:11106368

Citation	Ishige, K and Noguchi, T (2000) Inorganic polyphosphate kinase and adenylate kinase participate in the polyphosphate:AMP phosphotransferase activity of Escherichia coli. Proc. Natl. Acad. Sci. U.S.A. 97:14168-71
Abstract	Polyphosphate kinase (PPK), responsible for the processive synthesis of inorganic polyphosphate (polyP) from ATP in Escherichia coli, can transfer in reverse the terminal phosphate residue of polyP to ADP to yield ATP. PolyP also serves as a donor in a polyP:AMP phosphotransferase (PAP) activity observed in extracts of Acinetobacter johnsonii and Myxococcus xanthus. We have found that overexpression of the gene encoding PPK results in a large enhancement of PAP activity in E. coli. The PAP activity requires both PPK and adenylate kinase in equimolar amounts. PPK and adenylate kinase form a complex in the presence of polyphosphate. We discuss a phosphotransfer mechanism that involves both enzymes and enables polyP to be a phospho-donor to AMP.
Links	PubMed PMC18889 Online version:10.1073/pnas.011518098
Keywords	Adenylate Kinase/metabolism; Catalysis; Escherichia coli/enzymology; Phosphates/metabolism; Phosphotransferases (Phosphate Group Acceptor)/biosynthesis; Phosphotransferases (Phosphate Group Acceptor)/metabolism
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