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Literature summary extracted from

  • Weiss, P.H.; Batista, F.; Wagner, G.; Magalhaes, M.d.e. .L.; Miletti, L.C.
    Kinetic and biochemical characterization of Trypanosoma evansi nucleoside triphosphate diphosphohydrolase (2015), Exp. Parasitol., 153, 98-104 .
    View publication on PubMed

Activating Compound

EC Number Activating Compound Comment Organism Structure
3.6.1.15 D-glucose increases Vmax, especially in presence of cations Trypanosoma evansi
3.6.1.15 sucrose increases Vmax, especially in presence of cations Trypanosoma evansi

Cloned(Commentary)

EC Number Cloned (Comment) Organism
3.6.1.15 DNA and amino acid sequence determination and analysis, recombinant expression of the soluble His-tagged enzyme in Escherichia coli strain Rosetta Gammi (DE3) Trypanosoma evansi

Inhibitors

EC Number Inhibitors Comment Organism Structure
3.6.1.15 Na+
-
Trypanosoma evansi

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
3.6.1.15 additional information
-
additional information steady-state kinetics, Vmax values, overview Trypanosoma evansi
3.6.1.15 0.55
-
UTP pH 7.5, 25°C, recombinant enzyme, in presence of 10 mM KCl, 0.5 mM CaCl2, 10 mM MgCl2, 10 mM glucose, and 100 mM sucrose Trypanosoma evansi
3.6.1.15 1.04
-
ADP pH 7.5, 25°C, recombinant enzyme, in presence of 10 mM KCl, 0.5 mM CaCl2, 10 mM MgCl2, 10 mM glucose, and 100 mM sucrose Trypanosoma evansi
3.6.1.15 1.08
-
ITP pH 7.5, 25°C, recombinant enzyme, in presence of 10 mM KCl, 0.5 mM CaCl2, 10 mM MgCl2, 10 mM glucose, and 100 mM sucrose Trypanosoma evansi
3.6.1.15 1.2
-
GTP pH 7.5, 25°C, recombinant enzyme, in presence of 10 mM KCl, 0.5 mM CaCl2, 10 mM MgCl2, 10 mM glucose, and 100 mM sucrose Trypanosoma evansi
3.6.1.15 1.26
-
ATP pH 7.5, 25°C, recombinant enzyme, in absence of cations Trypanosoma evansi
3.6.1.15 1.5
-
ATP pH 7.5, 25°C, recombinant enzyme, in presence of Ca2+ Trypanosoma evansi
3.6.1.15 1.53
-
ATP pH 7.5, 25°C, recombinant enzyme, in presence of 10 mM KCl, 0.5 mM CaCl2, 10 mM MgCl2, 10 mM glucose, and 100 mM sucrose Trypanosoma evansi
3.6.1.15 1.53
-
ATP pH 7.5, 25°C, recombinant enzyme, in presence of Na+ Trypanosoma evansi
3.6.1.15 1.54
-
ATP pH 7.5, 25°C, recombinant enzyme, in presence of K+ Trypanosoma evansi
3.6.1.15 1.59
-
ATP pH 7.5, 25°C, recombinant enzyme, in presence of Mg2+ Trypanosoma evansi

Localization

EC Number Localization Comment Organism GeneOntology No. Textmining
3.6.1.15 cell surface
-
Trypanosoma evansi 9986
-
3.6.1.15 membrane the enzyme is a membrane bound protein facing the extracellular side of the cell Trypanosoma evansi 16020
-

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
3.6.1.15 Ca2+ activates Trypanosoma evansi
3.6.1.15 K+ activates Trypanosoma evansi
3.6.1.15 Mg2+ activates Trypanosoma evansi
3.6.1.15 additional information cations are required for catalytic activity, highest activity with a combination of K+, Mg2+, and Ca2+, with sucrose and glucose Trypanosoma evansi

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
3.6.1.15 ATP + H2O Trypanosoma evansi
-
ADP + phosphate
-
?

Organism

EC Number Organism UniProt Comment Textmining
3.6.1.15 Trypanosoma evansi A0A0E3JDD8
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
3.6.1.15 recombinant soluble His-tagged enzyme from Escherichia coli strain Rosetta Gammi (DE3) to homogeneity by nickel affinity chromatography and dialysis Trypanosoma evansi

Source Tissue

EC Number Source Tissue Comment Organism Textmining
3.6.1.15 trypomastigote
-
Trypanosoma evansi
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3.6.1.15 ADP + H2O
-
Trypanosoma evansi AMP + phosphate
-
?
3.6.1.15 ATP + H2O
-
Trypanosoma evansi ADP + phosphate
-
?
3.6.1.15 GTP + H2O
-
Trypanosoma evansi GDP + phosphate
-
?
3.6.1.15 ITP + H2O
-
Trypanosoma evansi IDP + phosphate
-
?
3.6.1.15 additional information nucleoside phosphorylase activity was monitored spectrophotometrically by following orthophosphate release using the malachite green method Trypanosoma evansi ?
-
-
3.6.1.15 UTP + H2O
-
Trypanosoma evansi UDP + phosphate
-
?

Subunits

EC Number Subunits Comment Organism
3.6.1.15 ? x * 65000, recombinant His-tagged enzyme, SDS-PAGE, x * 65599, sequence calculation Trypanosoma evansi

Synonyms

EC Number Synonyms Comment Organism
3.6.1.15 NTPDase
-
Trypanosoma evansi
3.6.1.15 nucleoside triphosphate diphospho-hydrolase
-
Trypanosoma evansi
3.6.1.15 nucleoside triphosphate diphosphohydrolase
-
Trypanosoma evansi

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
3.6.1.15 25
-
assay at Trypanosoma evansi

Temperature Range [°C]

EC Number Temperature Minimum [°C] Temperature Maximum [°C] Comment Organism
3.6.1.15 10 45 at 10°C the enzyme shows little activity, which increases exponentially showing an optimum of 32°C, followed by rapidly decreasing rates and almost null activities at temperatures greater than 45°C Trypanosoma evansi

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
3.6.1.15 7.5
-
assay at Trypanosoma evansi

pI Value

EC Number Organism Comment pI Value Maximum pI Value
3.6.1.15 Trypanosoma evansi sequence calculation
-
6.91

General Information

EC Number General Information Comment Organism
3.6.1.15 evolution Sequence similarity analysis and distance tree show high level (98%) of identity between Trypanosoma evansi and Trypanosoma brucei brucei (UniProt ID D6XLB5) NTPDase. Trypanosoma evansi NTPDase encloses the GDA1/CD39 nucleoside phosphatase family domain as well as exopolyphosphatase (Ppx-GppA) domain following five apyrase conserved regions (ACR) Trypanosoma evansi
3.6.1.15 physiological function nucleoside triphosphate diphospho-hydrolases (NTPDases) catalyze the hydrolysis of several nucleosides tri and diphosphate playing major roles in eukaryotes including purinergic signaling, inflammation, hemostasis, purine salvage and host-pathogen interactions Trypanosoma evansi