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Literature summary extracted from

  • Nassi, P.; Marchetti, E.; Nediani, C.; Liguri, G.; Ramponi, G.
    Acylphosphatase induced modifications in the functional properties of erythrocyte membrane sodium pump (1993), Biochim. Biophys. Acta, 1147, 19-26.
    View publication on PubMed

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
3.6.1.7 0.000147
-
 Na+/K+-ATPase phosphoenzyme intermediate high affinity for this substrate Homo sapiens

Localization

EC Number Localization Comment Organism GeneOntology No. Textmining
3.6.1.7 cytoplasm
-
 Homo sapiens 5737
-

Organism

EC Number Organism UniProt Comment Textmining
3.6.1.7 Homo sapiens
-
 human
-
3.6.1.7 Homo sapiens
-
 two isoenzymatic forms: one prevalent in skeletal and cardiac muscle, the other in red blood cells
-

Purification (Commentary)

EC Number Purification (Comment) Organism
3.6.1.7 erythrocyte isoenzyme Homo sapiens

Source Tissue

EC Number Source Tissue Comment Organism Textmining
3.6.1.7 erythrocyte
-
 Homo sapiens
-

Specific Activity [micromol/min/mg]

EC Number Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
3.6.1.7 7500
-
 erythrocyte isoenzyme, substrate benzoyl phosphate, 25°C Homo sapiens

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3.6.1.7 (Ca2+-Mg2+)-ATPase phosphorylated intermediate + H2O erythrocyte type enzyme, acylphosphorylated intermediates from human erythrocyte membrane Homo sapiens ?
-
 ?
3.6.1.7 1,3-diphosphoglycerate + H2O
-
 Homo sapiens 3-phosphoglycerate + phosphate
-
 ?
3.6.1.7 acylphosphate + H2O specifically catalyzes the hydrolysis of the carboxyl-phosphate bond of various acylphosphates Homo sapiens carboxylate + phosphate
-
 ?
3.6.1.7 benzoyl phosphate + H2O
-
 Homo sapiens benzoate + phosphate
-
 ?
3.6.1.7 carbamoyl phosphate + H2O
-
 Homo sapiens carbamate + phosphate
-
 ?
3.6.1.7 Na+/K+-ATPase phosphoenzyme intermediate + H2O mechanism Homo sapiens ?
-
 ?
3.6.1.7 Na+/K+-ATPase phosphoenzyme intermediate + H2O acylphosphatase can actively hydrolyze Na+/K+-ATPase phosphoenzyme Homo sapiens ?
-
 ?
3.6.1.7 Na+/K+-ATPase phosphoenzyme intermediate + H2O acylphosphatase produces a modification in the stoichiometry of the ATP driven cation transport by the Na+,K+ pump Homo sapiens ?
-
 ?
3.6.1.7 Na+/K+-ATPase phosphoenzyme intermediate + H2O from erythrocyte membrane Homo sapiens ?
-
 ?
3.6.1.7 Na+/K+-ATPase phosphoenzyme intermediate + H2O acylphosphatase significantly enhances the rate of strophantidine-sensitive ATP hydrolysis, it uncouples erythrocyte membrane N+,K+ pump Homo sapiens ?
-
 ?
3.6.1.7 Na+/K+-ATPase phosphoenzyme intermediate + H2O acylphosphatase markedly affects the functional properties of Na+,K+ pump, notably the rate of ATP hydrolysis and of cation, Na+,Rb+, transport Homo sapiens ?
-
 ?
3.6.1.7 Na+/K+-ATPase phosphoenzyme intermediate + H2O acylphosphorylated phosphoenzyme intermediate, enzyme has a high affinity for this substrate Homo sapiens ?
-
 ?
3.6.1.7 succinoyl phosphate + H2O
-
 Homo sapiens succinate + phosphate
-
 ?

Synonyms

EC Number Synonyms Comment Organism
3.6.1.7 More two isoenzymatic forms: one prevalent in skeletal and cardiac muscle named muscle type, the other in red blood cells named erythrocyte or common type, even if both isoforms are expressed in all tissues Homo sapiens

Temperature Stability [°C]

EC Number Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
3.6.1.7 100
-
 2 h: heat inactivation Homo sapiens