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Literature summary extracted from

  • Ishige, K.; Noguchi, T.
    Polyphosphate:AMP phosphotransferase and polyphosphate:ADP phosphotransferase activities of Pseudomonas aeruginosa (2001), Biochem. Biophys. Res. Commun., 281, 821-826.
    View publication on PubMed

Localization

EC Number Localization Comment Organism GeneOntology No. Textmining
2.7.4.33 soluble
-
 Pseudomonas aeruginosa
-
-

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
2.7.4.33 Mg2+ required Pseudomonas aeruginosa

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
2.7.4.33 AMP + [phosphate]n Pseudomonas aeruginosa best substrate ADP + [phosphate]n-1
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
2.7.4.33 Pseudomonas aeruginosa
-
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
2.7.4.33 by gel filtration, separation from polyphosphate kinase activity Pseudomonas aeruginosa

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2.7.4.33 AMP + (phosphate)n the activity originates from combined action of the polyphosphate:ADP phosphotransferase and adenylate kinase Pseudomonas aeruginosa ADP + (phosphate)n-1
-
 ?
2.7.4.33 AMP + [phosphate]n best substrate Pseudomonas aeruginosa ADP + [phosphate]n-1
-
 ?
2.7.4.33 AMP + [phosphate]n best substrate is [phosphate]15 Pseudomonas aeruginosa ADP + [phosphate]n-1
-
 ?
2.7.4.33 additional information the partially purified polyphosphate:ADP phosphotransferase is independent of polyphosphate kinase, PPK, and can function as polyphosphate-dependent nucleoside diphosphate kinase, PADP, which most prefers GDP to the other three nucleoside diphosphates as a phospho-acceptor. Both of the polyphosphate-utilizing activities require short polyphosphate as a phospho-donor whose chain length is below 75. The PAP activity mainly originates from the combined action of adenylate kinase, ADK, and the PADP independent of PPK. Each partially purified enzyme alone cannot mediate phosphorylation of AMP with polyphosphate, but coincubation of the both enzymes results in a marked expression of PAP activity, confirming that PADP and ADK constitute the PAP Pseudomonas aeruginosa ?
-
 ?

Synonyms

EC Number Synonyms Comment Organism
2.7.4.33 PADP
-
 Pseudomonas aeruginosa
2.7.4.33 PAP
-
 Pseudomonas aeruginosa
2.7.4.33 polyphosphate:ADP phosphotransferase
-
 Pseudomonas aeruginosa
2.7.4.33 polyphosphate:AMP phosphotransferase
-
 Pseudomonas aeruginosa

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
2.7.4.33 30
-
 assay at Pseudomonas aeruginosa

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
2.7.4.33 7.4
-
 assay at Pseudomonas aeruginosa

General Information

EC Number General Information Comment Organism
2.7.4.33 additional information overexpression in strain PAO1 leads to a massive production of polyphosphate kinase, PPK, and a marked enhancement of polyphosphate-synthesizing activity, while the PAP activity is not affected by overproduction of PPK Pseudomonas aeruginosa