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Literature summary extracted from

  • Ishige, K.; Noguchi, T.
    Inorganic polyphosphate kinase and adenylate kinase participate in the polyphosphate:AMP phosphotransferase activity of Escherichia coli (2000), Proc. Natl. Acad. Sci. USA, 97, 14168-14171.
    View publication on PubMedView publication on EuropePMC

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 Escherichia coli
-
ADP + [phosphate]n-1
-
?
2.7.4.33 AMP + [phosphate]n Escherichia coli JM109
-
ADP + [phosphate]n-1
-
?
2.7.4.33 additional information Escherichia coli Escherichia coli strain JM109 possesses a very low level of intrinsic PAP activity that catalyzes the synthesis of ADP from AMP and polyphosphate. PPK and ADK together constitute the PAP activity, where it phosphorylates AMP with polyphosphate ?
-
?
2.7.4.33 additional information Escherichia coli JM109 Escherichia coli strain JM109 possesses a very low level of intrinsic PAP activity that catalyzes the synthesis of ADP from AMP and polyphosphate. PPK and ADK together constitute the PAP activity, where it phosphorylates AMP with polyphosphate ?
-
?

Organism

EC Number Organism UniProt Comment Textmining
2.7.4.33 Escherichia coli
-
-
-
2.7.4.33 Escherichia coli JM109
-
-
-

Source Tissue

EC Number Source Tissue Comment Organism Textmining

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2.7.4.33 AMP + (phosphate)n polyphosphate kinase and adenylate kinase together constitute the polyP:AMP phosphotransferase activity. Polyphosphate kinase and adenylate kinase form a complex in the presence of polyphosphate Escherichia coli ADP + (phosphate)n-1
-
?
2.7.4.33 AMP + (phosphate)n polyphosphate kinase and adenylate kinase together constitute the polyP:AMP phosphotransferase activity. Polyphosphate kinase and adenylate kinase form a complex in the presence of polyphosphate Escherichia coli JM109 ADP + (phosphate)n-1
-
?
2.7.4.33 AMP + [phosphate]n
-
Escherichia coli ADP + [phosphate]n-1
-
?
2.7.4.33 AMP + [phosphate]n
-
Escherichia coli JM109 ADP + [phosphate]n-1
-
?
2.7.4.33 additional information Escherichia coli strain JM109 possesses a very low level of intrinsic PAP activity that catalyzes the synthesis of ADP from AMP and polyphosphate. PPK and ADK together constitute the PAP activity, where it phosphorylates AMP with polyphosphate Escherichia coli ?
-
?
2.7.4.33 additional information Escherichia coli strain JM109 possesses a very low level of intrinsic PAP activity that catalyzes the synthesis of ADP from AMP and polyphosphate. PPK and ADK together constitute the PAP activity, where it phosphorylates AMP with polyphosphate Escherichia coli JM109 ?
-
?

Synonyms

EC Number Synonyms Comment Organism
2.7.4.33 PAP
-
Escherichia coli
2.7.4.33 polyP:AMP phosphotransferase
-
Escherichia coli

General Information

EC Number General Information Comment Organism
2.7.4.33 additional information polyphosphate kinase, PPK, responsible for the processive synthesis of inorganic polyphosphate from ATP in Escherichia coli, can transfer in reverse the terminal phosphate residue of polyphosphate to ADP to yield ATP. When coexpressed with adenylate kinase, ADK, in Escherichia coli, PPK and ADK together highly enhance the PAP activity in Escherichia coli Escherichia coli