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Literature summary for 3.6.1.11 extracted from
- Putative binding mode of Escherichia coli exopolyphosphatase and polyphosphates based on a hybrid in silico/biochemical approach (2016), Arch. Biochem. Biophys., 606, 64-72 .
Cloned(Commentary)
| Cloned (Comment) | Organism |
|---|---|
| gene ppx, recombinant expression of N-terminally His6-tagged enzyme in Escherichia coli strains XL10-Gold and BL21-CodonPlus | Escherichia coli |
Metals/Ions
| Metals/Ions | Comment | Organism | Structure |
|---|---|---|---|
| K+ | activates | Escherichia coli |  |
| Mg2+ | required | Escherichia coli | |
Natural Substrates/ Products (Substrates)
| Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| additional information | Escherichia coli | exopolyphosphatase Ppx releases inorganic phosphate (Pi) from polyphosphate. Inorganic polyphosphate (polyP) is a linear anionic polymer of phosphate molecules which was found in all living organisms and may form aggregates. The phosphate molecules within polyphosphate are held together by high-energy phosphoanhydride bonds. The length of this polymer may vary between ten to hundreds of units, depending on the organism and its physiological stage | ? | - |
- |
|
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Escherichia coli | P0AFL6 | - |
- |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| additional information | exopolyphosphatase Ppx releases inorganic phosphate (Pi) from polyphosphate. Inorganic polyphosphate (polyP) is a linear anionic polymer of phosphate molecules which was found in all living organisms and may form aggregates. The phosphate molecules within polyphosphate are held together by high-energy phosphoanhydride bonds. The length of this polymer may vary between ten to hundreds of units, depending on the organism and its physiological stage | Escherichia coli | ? | - |
- |
|
| additional information | substrates are commercial sodium phosphate glass with 25-PP25-, 65-PP65-, or PPK-synthesized polyphosphate with 700-PP700-average number of residues. Released phosphate is detected by the malachite green method at 630 nm | Escherichia coli | ? | - |
- |
|
| polyphosphate25 + H2O | - |
Escherichia coli | polyphosphate24 + phosphate | - |
? | |
| polyphosphate65 + H2O | - |
Escherichia coli | polyphosphate64 + phosphate | - |
? | |
| polyphosphate700 + H2O | - |
Escherichia coli | polyphosphate699 + phosphate | - |
? | |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| ecPpx | - |
Escherichia coli |
| PPX | - |
Escherichia coli |
Temperature Optimum [°C]
| Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
|---|---|---|---|
| 37 | - |
assay at | Escherichia coli |
pH Optimum
| pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|
| 8 | - |
assay at | Escherichia coli |
General Information
| General Information | Comment | Organism |
|---|---|---|
| evolution | the exopolyphosphatase belongs to the ASKHA protein superfamily | Escherichia coli |
| malfunction | analysis of single ppx- or ppk- mutants and of the double mutant, demonstrate a relationship between these genes and the survival capacity | Escherichia coli |
| additional information | substrate binding structure analysis, different computational approaches, site-direct mutagenesis and kinetic data are applied to understand the relationship between structure and function of exopolyphosphatase. Enzyme residue H378 is proposed as a fundamental gatekeeper for the recognition of long chain polyphosphate. Implication of H378 protonation state, overview. Electrostatic and energy calculations and molecular docking study, molecular dynamics simulations, overview. The frontal surface of the protein has a clear predominance of electropositive potential and the minimum binding energies are also obtained in that surface. This is favored by interaction with R166,K197, H382, G380, and K414. Other favorable region is formed by residues K353, K428, K429, K430 and Q431 in the joint of domains I and IV. On the contrary, the binding energies of the back side of the protein surface are unfavorable to bind polyphosphate, consistent with a predominance of electronegative potential. Indeed, ecPpx is characterized by a clear division between electropositive (frontal) and electronegative (back) potential | Escherichia coli |
| physiological function | the exopolyphosphatase of Escherichia coli processively and completely hydrolyses long polyphosphate chains to ortho-phosphate. Polyphosphate plays a remarkable role in pathogenesis, survival and stress tolerance | Escherichia coli |
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