Polyphosphate:AMP phosphotransferase and polyphosphate:ADP phosphotransferase activities of Pseudomonas aeruginosa.
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.
Biochemicals Division, YAMASA Corporation, Choshi, Chiba, 288-0056, Japan.
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Ishige
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Noguchi
D001483:Base Sequence; D015153:Blotting, Western; D017931:DNA Primers; D017856:Phosphotransferases (Phosphate Group Acceptor) / Q000378:metabolism*; D011550:Pseudomonas aeruginosa / Q000201:enzymology*
D017931:DNA Primers; D017856:Phosphotransferases (Phosphate Group Acceptor); C423573:polyphosphate ADP phosphotransferase; C059169:polyphosphate AMP phosphotransferase