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Literature summary extracted from
- A soluble inorganic pyrophosphatase from the cattle tick Rhipicephalus microplus capable of hydrolysing polyphosphates (2018), Insect Mol. Biol., 27, 260-267 .
Cloned(Commentary)
| EC Number | Cloned (Comment) | Organism |
|---|---|---|
| 3.6.1.1 | gene ppa, recombinant expression of the His-tagged enzyme in Escherichia coli strain Rosetta-Gami B (DE3)pLysS | Rhipicephalus microplus |
| 3.6.1.11 | gene ppa, recombinant expression of the His-tagged enzyme in Escherichia coli strain Rosetta-Gami B (DE3)pLysS | Rhipicephalus microplus |
KM Value [mM]
| EC Number | KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|---|
| 3.6.1.1 | additional information | - |
additional information | Michaelis-Menten kinetics, overview | Rhipicephalus microplus | |
| 3.6.1.1 | 0.1224 | - |
diphosphate | recombinant enzyme, pH 7.5, 30°C | Rhipicephalus microplus |  |
| 3.6.1.1 | 0.3315 | - |
polyphosphate glass type 15 | recombinant enzyme, pH 7.5, 30°C | Rhipicephalus microplus | |
| 3.6.1.1 | 0.7244 | - |
Triphosphate | recombinant enzyme, pH 7.5, 30°C | Rhipicephalus microplus | |
| 3.6.1.11 | additional information | - |
additional information | Michaelis-Menten kinetics, overview | Rhipicephalus microplus | |
| 3.6.1.11 | 0.3315 | - |
polyphosphate glass type 15 | recombinant enzyme, pH 7.5, 30°C | Rhipicephalus microplus | |
| 3.6.1.11 | 0.7244 | - |
polyphosphate3 | recombinant enzyme, pH 7.5, 30°C | Rhipicephalus microplus |
Localization
| EC Number | Localization | Comment | Organism | GeneOntology No. | Textmining |
|---|---|---|---|---|---|
| 3.6.1.1 | soluble | - |
Rhipicephalus microplus | - |
- |
Metals/Ions
| EC Number | Metals/Ions | Comment | Organism | Structure |
|---|---|---|---|---|
| 3.6.1.1 | Mg2+ | required, family I diphosphatases are Mg2+-dependent, activates | Rhipicephalus microplus | |
| 3.6.1.1 | additional information | no effect on activity by Mn2+ and Zn2+ | Rhipicephalus microplus | |
| 3.6.1.11 | Mg2+ | required, family I diphosphatases are Mg2+-dependent, activates | Rhipicephalus microplus | |
| 3.6.1.11 | additional information | no effect on activity by Mn2+ and Zn2+ | Rhipicephalus microplus |
Natural Substrates/ Products (Substrates)
| EC Number | Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
|---|---|---|---|---|---|---|---|
| 3.6.1.1 | diphosphate + H2O | Rhipicephalus microplus | - |
2 phosphate | - |
? | |
| 3.6.1.1 | additional information | Rhipicephalus microplus | the soluble enzyme from cattle tick Rhipicephalus microplus is capable of hydrolysing polyphosphates, molecular docking assays of RmPPase with polyphosphates, and molecular modelling, overview | ? | - |
- |
|
| 3.6.1.1 | polyphosphate glass type 15 + H2O | Rhipicephalus microplus | - |
? | - |
? | |
| 3.6.1.1 | triphosphate + H2O | Rhipicephalus microplus | - |
3 phosphate | - |
? | |
| 3.6.1.11 | additional information | Rhipicephalus microplus | the soluble enzyme from cattle tick Rhipicephalus microplus is capable of hydrolysing polyphosphates, molecular docking assays of RmPPase with polyphosphates, and molecular modelling, overview | ? | - |
- |
|
Organism
| EC Number | Organism | UniProt | Comment | Textmining |
|---|---|---|---|---|
| 3.6.1.1 | Rhipicephalus microplus | H6BG92 | - |
- |
| 3.6.1.11 | Rhipicephalus microplus | - |
- |
- |
Purification (Commentary)
| EC Number | Purification (Comment) | Organism |
|---|---|---|
| 3.6.1.1 | recombinant His-tagged enzyme from Escherichia coli strain Rosetta-Gami B (DE3)pLysS by nickel affinity chromatography | Rhipicephalus microplus |
| 3.6.1.11 | recombinant His-tagged enzyme from Escherichia coli strain Rosetta-Gami B (DE3)pLysS by nickel affinity chromatography | Rhipicephalus microplus |
Substrates and Products (Substrate)
| EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|---|
| 3.6.1.1 | diphosphate + H2O | - |
Rhipicephalus microplus | 2 phosphate | - |
? | |
| 3.6.1.1 | additional information | the soluble enzyme from cattle tick Rhipicephalus microplus is capable of hydrolysing polyphosphates, molecular docking assays of RmPPase with polyphosphates, and molecular modelling, overview | Rhipicephalus microplus | ? | - |
- |
|
| 3.6.1.1 | additional information | the recombinant enzyme rRmPPase has a greater affinity, higher catalytic efficiency and increased cooperativity for sodium phosphate glass type 15 (polyP15) than for sodium tripolyphosphate (polyP3). Molecular docking study. PolyP3 binds close to the Mg2+ atoms in the catalytic region of the protein, participating in their coordination network, whereas polyP15 interactions involve negatively charged phosphate groups and basic amino acid residues, such as Lys56, Arg58, and Lys193. PolyP15 has a more favourable theoretical binding affinity than polyP3, thus supporting the kinetic data | Rhipicephalus microplus | ? | - |
- |
|
| 3.6.1.1 | polyphosphate glass type 15 + H2O | - |
Rhipicephalus microplus | ? | - |
? | |
| 3.6.1.1 | triphosphate + H2O | - |
Rhipicephalus microplus | 3 phosphate | - |
? | |
| 3.6.1.11 | additional information | the soluble enzyme from cattle tick Rhipicephalus microplus is capable of hydrolysing polyphosphates, molecular docking assays of RmPPase with polyphosphates, and molecular modelling, overview | Rhipicephalus microplus | ? | - |
- |
|
| 3.6.1.11 | additional information | the recombinant enzyme rRmPPase, a inorganic diphosphatase (EC 3.6.1.1) from Rhipicephalus microplus, also shows exopolyphosphatase activity. It has a greater affinity, higher catalytic efficiency and increased cooperativity for sodium phosphate glass type 15 (polyP15) than for sodium tripolyphosphate (polyP3). Molecular docking study. PolyP3 binds close to the Mg2+ atoms in the catalytic region of the protein, participating in their coordination network, whereas polyP15 interactions involve negatively charged phosphate groups and basic amino acid residues, such as Lys56, Arg58, and Lys193. PolyP15 has a more favourable theoretical binding affinity than polyP3, thus supporting the kinetic data | Rhipicephalus microplus | ? | - |
- |
|
| 3.6.1.11 | polyphosphate glass type 15 + H2O | - |
Rhipicephalus microplus | ? | - |
? | |
| 3.6.1.11 | polyphosphate3 + H2O | - |
Rhipicephalus microplus | diphosphate + phosphate | - |
? | |
Synonyms
| EC Number | Synonyms | Comment | Organism |
|---|---|---|---|
| 3.6.1.1 | family I pyrophosphatase | - |
Rhipicephalus microplus |
| 3.6.1.1 | inorganic pyrophosphatase | - |
Rhipicephalus microplus |
| 3.6.1.1 | More | cf. EC 3.6.1.11 | Rhipicephalus microplus |
| 3.6.1.1 | PPase | - |
Rhipicephalus microplus |
| 3.6.1.1 | pyrophosphatase | - |
Rhipicephalus microplus |
| 3.6.1.1 | RmPPase | - |
Rhipicephalus microplus |
| 3.6.1.11 | More | cf. EC 3.6.1.1 | Rhipicephalus microplus |
Temperature Optimum [°C]
| EC Number | Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
|---|---|---|---|---|
| 3.6.1.1 | 30 | - |
assay at | Rhipicephalus microplus |
| 3.6.1.11 | 30 | - |
recombinant enzyme | Rhipicephalus microplus |
pH Optimum
| EC Number | pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|---|
| 3.6.1.1 | 7.5 | - |
recombinant enzyme | Rhipicephalus microplus |
| 3.6.1.11 | 7.5 | - |
recombinant enzyme | Rhipicephalus microplus |
General Information
| EC Number | General Information | Comment | Organism |
|---|---|---|---|
| 3.6.1.1 | metabolism | the inorganic diphosphatase from Rhipicephalus microplus seems to be involved in polyphosphate metabolism | Rhipicephalus microplus |
| 3.6.1.1 | physiological function | inorganic pyrophosphatases (PPases) are ubiquitous, essential metal-dependent enzymes capable of supplying thermodynamic energy to many important biosynthetic reactions by hydrolysis of diphosphate to phosphate | Rhipicephalus microplus |
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