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Literature summary for 3.6.1.5 extracted from

  • Kalita, B.; Patra, A.; Jahan, S.; Mukherjee, A.K.
    First report of the characterization of a snake venom apyrase (Ruviapyrase) from Indian Russells viper (Daboia russelii) venom (2018), Int. J. Biol. Macromol., 111, 639-648 .
    View publication on PubMed

Inhibitors

Inhibitors Comment Organism Structure
DTT
-
Daboia russelii
EDTA
-
Daboia russelii
iodoacetamide
-
Daboia russelii
additional information the catalytic activity and platelet deaggregation property of Ruviapyrase is significantly inhibited by EDTA, DTT, and iodoacetamide, and neutralized by commercial monovalent and polyvalent antivenom. Poor inhibition by PMSF Daboia russelii
Zn2+ 63% (ADPase) and 71% (ATPase) inhibition at 2 mM Daboia russelii

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.00254
-
ATP pH 7.4, 37°C Daboia russelii
0.00577
-
ADP pH 7.4, 37°C Daboia russelii

Localization

Localization Comment Organism GeneOntology No. Textmining
extracellular
-
Daboia russelii
-
-

Metals/Ions

Metals/Ions Comment Organism Structure
Ca2+ activates Daboia russelii
Mg2+ activates, less effective than Ca2+ Daboia russelii

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
83041
-
MALDI-TOF-mass spectrometry analysis and gel filtration Daboia russelii

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
ADP + H2O Daboia russelii
-
AMP + phosphate
-
?
ATP + H2O Daboia russelii
-
ADP + phosphate
-
?
additional information Daboia russelii Ruviapyrase does not show cytotoxicity against breast cancer (MCF-7) cells and haemolytic activity, it exhibits marginal anticoagulant and strong antiplatelet activity, and dose-dependently reverses the ADP-induced platelet aggregation. The catalytic activity and platelet deaggregation property of Ruviapyrase is significantly inhibited by EDTA, DTT and IAA, and neutralized by commercial monovalent and polyvalent antivenom ?
-
-

Organism

Organism UniProt Comment Textmining
Daboia russelii
-
-
-

Posttranslational Modification

Posttranslational Modification Comment Organism
glycoprotein the enzyme is a monomeric glycoprotein that contains 2.4% neutral sugars and 58.4% N-linked oligosaccharides and strongly binds to concanavalin A Daboia russelii

Purification (Commentary)

Purification (Comment) Organism
native enzyme 1.6fold (ATPase) and 2.3fold (ADPase) from venom by gel filtration and anion exchange chromatography Daboia russelii

Source Tissue

Source Tissue Comment Organism Textmining
venom
-
Daboia russelii
-

Storage Stability

Storage Stability Organism
the catalytic activity (both ATPase as well as ADPase) of Ruviapyrase declines rapidly at physiological conditions (37°C, pH 7.4). It loses 80% of its enzyme activity within 2 h of incubation albeit ATPase and ADPase activities of crude Russel viper venom are found to be more stable compared to Ruviapyrase Daboia russelii

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
ADP + H2O
-
Daboia russelii AMP + phosphate
-
?
ATP + H2O
-
Daboia russelii ADP + phosphate
-
?
additional information Ruviapyrase does not show cytotoxicity against breast cancer (MCF-7) cells and haemolytic activity, it exhibits marginal anticoagulant and strong antiplatelet activity, and dose-dependently reverses the ADP-induced platelet aggregation. The catalytic activity and platelet deaggregation property of Ruviapyrase is significantly inhibited by EDTA, DTT and IAA, and neutralized by commercial monovalent and polyvalent antivenom Daboia russelii ?
-
-
additional information Ruviapyrase hydrolysed adenosine triphosphate (ATP) to a significantly greater extent as compared to adenosine diphosphate (ADP). The enzyme is devoid of 5'-nucleotidase and phosphodiesterase activities. The specificity constant or kinetic efficiency of Ruviapyrase in hydrolysing ATP is 3.7folds higher compared to hydrolysis of ADP under identical experimental conditions Daboia russelii ?
-
-

Subunits

Subunits Comment Organism
monomer x * 79400, glycosylated enzyme, SDS-PAGE, x * 33000, deglycosylated enzyme, SDS-PAGE Daboia russelii

Synonyms

Synonyms Comment Organism
Ruviapyrase
-
Daboia russelii
snake venom apyrase
-
Daboia russelii

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
37
-
assay at Daboia russelii

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
248.6
-
ADP pH 7.4, 37°C Daboia russelii
410
-
ATP pH 7.4, 37°C Daboia russelii

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7.4
-
assay at Daboia russelii

kcat/KM [mM/s]

kcat/KM Value [1/mMs-1] kcat/KM Value Maximum [1/mMs-1] Substrate Comment Organism Structure
43085
-
ADP pH 7.4, 37°C Daboia russelii
161417
-
ATP pH 7.4, 37°C Daboia russelii