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Literature summary extracted from

  • Mimura, K.; Tahara, Y.; Shinji, N.; Tokuda, E.; Takenaka, H.; Hayashi, Y.
    Isolation of stable (alphabeta)4-tetraprotomer from Na+/K+-ATPase solubilized in the presence of short-chain fatty acids (2008), Biochemistry, 47, 6039-6051.
    View publication on PubMed

Organism

EC Number Organism UniProt Comment Textmining
7.2.2.13 Canis lupus
-
-
-
7.2.2.13 Sus scrofa
-
-
-

Source Tissue

EC Number Source Tissue Comment Organism Textmining
7.2.2.13 kidney
-
 Sus scrofa
-
7.2.2.13 kidney
-
 Canis lupus
-

Specific Activity [micromol/min/mg]

EC Number Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
7.2.2.13 32
-
 tetraprotomer, pH 7.3, 37°C Sus scrofa
7.2.2.13 32
-
 tetraprotomer, pH 7.3, 37°C Canis lupus
7.2.2.13 65
-
 diprotomer and protomer, 37°C, pH 7.3 Sus scrofa
7.2.2.13 65
-
 diprotomer and protomer, 37°C, pH 7.3 Canis lupus

Subunits

EC Number Subunits Comment Organism
7.2.2.13 More in presence of acetate anion, and, in decreasing order, NH4+ propionate, Rb+ propionate, K+ propionate, and Tl+ propionate, enzyme forms a tetraprotomer (alphabeta)4, consuming (alphabeta)2 diprotomer and (alphabeta) protomer. By exposure to 25°C, the tetraprotomer shows 34% dissociation to diprotomer Sus scrofa
7.2.2.13 More in presence of acetate anion, and, in decreasing order, NH4+ propionate, Rb+ propionate, K+ propionate, and Tl+ propionate, enzyme forms a tetraprotomer (alphabeta)4, consuming (alphabeta)2 diprotomer and (alphabeta) protomer. By exposure to 25°C, the tetraprotomer shows 34% dissociation to diprotomer Canis lupus