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Literature summary for 7.6.2.1 extracted from

  • Auland, M.E.; Morris, M.B.; Roufogalis, B.D.
    Separation and characterization of two Mg2+-ATpase activities from human erythrocyte membrane (1994), Arch. Biochem. Biophys., 312, 272-277.
    View publication on PubMed
Search for more literature for 7.6.2.1

Inhibitors

Inhibitors Comment Organism Structure
Ca2+
-
 Homo sapiens
F- inhibition increases in the presence of 0.01 mM AlCl3 Homo sapiens
La3+
-
 Homo sapiens
vanadate
-
 Homo sapiens

Localization

Localization Comment Organism GeneOntology No. Textmining
plasma membrane
-
 Homo sapiens 5886
-

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
ATP + H2O Homo sapiens role of the enzyme in the control of erythrocyte shape, possibly through association with the ATP-dependent translocation of phosphatidylserine and phosphatidylethanolamine from the outer to the inner leaflet of the bilayer ADP + phosphate
-
 ?

Organism

Organism UniProt Comment Textmining
Homo sapiens
-
-
-

Source Tissue

Source Tissue Comment Organism Textmining
erythrocyte
-
 Homo sapiens
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
ATP + H2O activity is stimulated twofold by addition of 2 mM ATP Homo sapiens ADP + phosphate
-
 ?
ATP + H2O role of the enzyme in the control of erythrocyte shape, possibly through association with the ATP-dependent translocation of phosphatidylserine and phosphatidylethanolamine from the outer to the inner leaflet of the bilayer Homo sapiens ADP + phosphate
-
 ?
dATP + H2O at 2 mM nearly as active as ATP Homo sapiens dADP + H2O
-
 ?
GTP + H2O at 2 mM, 40% of the activity with 2 mM ATP Homo sapiens GDP + phosphate
-
 ?