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Literature summary extracted from

  • Kiffer-Moreira, T.; Fernandes Sampaio, M.E.; Alviano, D.S.; Axelband, F.; Cesar, G.V.; Cosentino-Gomes, D.; Rodrigues, M.L.; Nimrichter, L.; Vieyra, A.; Alviano, C.S.; Meyer-Fernandes, J.R.
    Biochemical characterization of an ecto-ATP diphosphohydrolase activity in Candida parapsilosis and its possible role in adenosine acquisition and pathogenesis (2010), FEMS Yeast Res., 10, 735-746.
    View publication on PubMed

Inhibitors

EC Number Inhibitors Comment Organism Structure
3.6.1.5 4,4'-diisothiocyanatostilbene-2,2'-disulfonic acid 0.5 mM reduces enzyme activity in yeast living cells by 83.1% Candida parapsilosis
3.6.1.5 ARL 67156 i.e. 6-N,N'-diethyl-D-beta-gamma-dibromomethylene-ATP, inhibits the ecto-ATPase activity in a dose-dependent manner (about 60% residual activity at 0.5 mM in the presence of 50 mM ATP and about 40% residual activity at 0.5 mM in the presence of 0.5 mM ATP) Candida parapsilosis
3.6.1.5 additional information ecto-ATPase activity is insensitive to 10 mM inorganic phosphate. Ammonium molybdate, 5'-AMP, 4-nitrophenyl phosphate, beta-glycerphosphate, sodium fluoride, sodium tartrate, levamizole, ouabain, oligomycin, and sodium azide have no effect on the Mg2+-stimulated ecto-ATPase Candida parapsilosis
3.6.1.5 suramin 0.5 mM suramin reduces enzyme activity in yeast living cells by 81.8% Candida parapsilosis

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
3.6.1.5 0.6
-
 ATP at 30°C in 50 mM HEPES, pH 7.2 Candida parapsilosis

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
3.6.1.5 Co2+ stimulates ecto-ATPase activity Candida parapsilosis
3.6.1.5 Mg2+ ecto-ATPase activity is increased in the presence of 5 mM Mg2+ Candida parapsilosis
3.6.1.5 Mn2+ stimulates ecto-ATPase activity Candida parapsilosis

Organism

EC Number Organism UniProt Comment Textmining
3.6.1.5 Candida parapsilosis
-
-
-
3.6.1.5 Candida parapsilosis CCT3834
-
-
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3.6.1.5 ADP + 2 H2O 82.2% activity compared to ATP Candida parapsilosis adenosine + 2 phosphate
-
 ?
3.6.1.5 ADP + 2 H2O 82.2% activity compared to ATP Candida parapsilosis CCT3834 adenosine + 2 phosphate
-
 ?
3.6.1.5 ATP + 2 H2O 100% activity Candida parapsilosis AMP + 2 phosphate
-
 ?
3.6.1.5 ATP + 2 H2O 100% activity Candida parapsilosis CCT3834 AMP + 2 phosphate
-
 ?
3.6.1.5 CTP + 2 H2O 15.9% activity compared to ATP Candida parapsilosis CMP + 2 phosphate
-
 ?
3.6.1.5 GTP + 2 H2O 20.7% activity compared to ATP Candida parapsilosis GMP + 2 phosphate
-
 ?
3.6.1.5 GTP + 2 H2O 20.7% activity compared to ATP Candida parapsilosis CCT3834 GMP + 2 phosphate
-
 ?
3.6.1.5 ITP + 2 H2O 70.7% activity compared to ATP Candida parapsilosis IMP + 2 phosphate
-
 ?
3.6.1.5 ITP + 2 H2O 70.7% activity compared to ATP Candida parapsilosis CCT3834 IMP + 2 phosphate
-
 ?
3.6.1.5 UTP + 2 H2O 43.3% activity compared to ATP Candida parapsilosis UMP + 2 phosphate
-
 ?
3.6.1.5 UTP + 2 H2O 43.3% activity compared to ATP Candida parapsilosis CCT3834 UMP + 2 phosphate
-
 ?

Synonyms

EC Number Synonyms Comment Organism
3.6.1.5 ecto-ATP diphosphohydrolase
-
 Candida parapsilosis
3.6.1.5 ecto-ATPase
-
 Candida parapsilosis

pH Range

EC Number pH Minimum pH Maximum Comment Organism
3.6.1.5 3 9 the Mg2+-stimulated ATPase activity increases with the pH. At pH 9.0, the values of ATP hydrolysis are around 7fold higher than those obtained at pH 3.0 Candida parapsilosis