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Literature summary for 3.6.1.1 extracted from

  • Cruz, C.S.; Costa, E.P.; Machado, J.A.; Silva, J.N.; Romeiro, N.C.; Moraes, J.; Silva, J.R.; Fonseca, R.N.; Vaz, I.S.; Logullo, C.; Campos, E.
    A soluble inorganic pyrophosphatase from the cattle tick Rhipicephalus microplus capable of hydrolysing polyphosphates (2018), Insect Mol. Biol., 27, 260-267 .
    View publication on PubMed

Cloned(Commentary)

Cloned (Comment) Organism
gene ppa, recombinant expression of the His-tagged enzyme in Escherichia coli strain Rosetta-Gami B (DE3)pLysS Rhipicephalus microplus

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
additional information
-
additional information Michaelis-Menten kinetics, overview Rhipicephalus microplus
0.1224
-
diphosphate recombinant enzyme, pH 7.5, 30°C Rhipicephalus microplus
0.3315
-
polyphosphate glass type 15 recombinant enzyme, pH 7.5, 30°C Rhipicephalus microplus
0.7244
-
Triphosphate recombinant enzyme, pH 7.5, 30°C Rhipicephalus microplus

Localization

Localization Comment Organism GeneOntology No. Textmining
soluble
-
Rhipicephalus microplus
-
-

Metals/Ions

Metals/Ions Comment Organism Structure
Mg2+ required, family I diphosphatases are Mg2+-dependent, activates Rhipicephalus microplus
additional information no effect on activity by Mn2+ and Zn2+ Rhipicephalus microplus

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
diphosphate + H2O Rhipicephalus microplus
-
2 phosphate
-
?
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 ?
-
-
polyphosphate glass type 15 + H2O Rhipicephalus microplus
-
?
-
?
triphosphate + H2O Rhipicephalus microplus
-
3 phosphate
-
?

Organism

Organism UniProt Comment Textmining
Rhipicephalus microplus H6BG92
-
-

Purification (Commentary)

Purification (Comment) Organism
recombinant His-tagged enzyme from Escherichia coli strain Rosetta-Gami B (DE3)pLysS by nickel affinity chromatography Rhipicephalus microplus

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
diphosphate + H2O
-
Rhipicephalus microplus 2 phosphate
-
?
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 ?
-
-
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 ?
-
-
polyphosphate glass type 15 + H2O
-
Rhipicephalus microplus ?
-
?
triphosphate + H2O
-
Rhipicephalus microplus 3 phosphate
-
?

Synonyms

Synonyms Comment Organism
family I pyrophosphatase
-
Rhipicephalus microplus
inorganic pyrophosphatase
-
Rhipicephalus microplus
More cf. EC 3.6.1.11 Rhipicephalus microplus
PPase
-
Rhipicephalus microplus
pyrophosphatase
-
Rhipicephalus microplus
RmPPase
-
Rhipicephalus microplus

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
30
-
assay at Rhipicephalus microplus

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7.5
-
recombinant enzyme Rhipicephalus microplus

General Information

General Information Comment Organism
metabolism the inorganic diphosphatase from Rhipicephalus microplus seems to be involved in polyphosphate metabolism Rhipicephalus microplus
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