Polyphosphate:AMP phosphotransferase and polyphosphate:ADP phosphotransferase activities of Pseudomonas aeruginosa

Biochem Biophys Res Commun. 2001 Mar 2;281(3):821-6. doi: 10.1006/bbrc.2001.4415.

Abstract

In Pseudomonas aeruginosa PAO1, we have found massive polyphosphate:AMP phosphotransferase activity and polyphosphate:ADP phosphotransferase activity known as the reverse catalytic activity of polyphosphate kinase which participates in polyphosphate synthesis in the bacterium. Biochemical analysis using the partially purified polyphosphate:ADP phosphotransferase has revealed that it is independent of polyphosphate kinase and can function as polyphosphate-dependent nucleoside diphosphate kinase which most prefers GDP to the other three nucleoside diphosphates as a phospho-acceptor. It has been also demonstrated that polyphosphate:AMP phosphotransferase activity marked in the bacterium mainly originates from the combined action of the polyphosphate:ADP phosphotransferase described above and adenylate kinase. Both of the polyphosphate-utilizing activities require short polyP as a phospho-donor whose chain length is <75.

MeSH terms

  • Base Sequence
  • Blotting, Western
  • DNA Primers
  • Phosphotransferases (Phosphate Group Acceptor) / metabolism*
  • Pseudomonas aeruginosa / enzymology*

Substances

  • DNA Primers
  • Phosphotransferases (Phosphate Group Acceptor)
  • polyphosphate ADP phosphotransferase
  • polyphosphate AMP phosphotransferase