Literature summary for 3.6.1.11 extracted from

Bolesch, D.G.; Keasling, J.D.
The effect of monovalent ions on polyphosphate binding to Escherichia coli exopolyphosphatase (2000), Biochem. Biophys. Res. Commun., 274, 236-241.

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Inhibitors

Inhibitors	Comment	Organism	Structure
AlF4-	10 mM, 25% loss of activity	Escherichia coli
VO43-	1 mM, less than 5% reduced activity	Escherichia coli

Metals/Ions

Metals/Ions	Comment	Organism	Structure
Mg2+	divalent cation required, Mg2+ is most effective	Escherichia coli

Organism

Organism	UniProt	Comment	Textmining
Escherichia coli	-	-	-

Reaction

Reaction	Comment	Organism	Reaction ID
(polyphosphate)n + H2O = (polyphosphate)n-1 + phosphate	the interaction of the enzyme with polyphosphate is independent on cation concentration, binding is not driven by entropy from release of polyelectrolyte condensed cations	Escherichia coli	a

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
(polyphosphate)n + H2O	-	Escherichia coli	(polyphosphate)n-1 + phosphate	-	?

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Release 2023.1 (January 2023)