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Literature summary extracted from

  • Siebers, A.; Kollmann, R.; Dierkes, G.; Altendorf, K.
    Rapid, high yield purification and characterization of the K+-translocating Kdp-ATPase from Escherichia coli (1992), J. Biol. Chem., 257, 12717-12721.
No PubMed abstract available

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
7.2.2.6 0.01
-
 K+
-
 Escherichia coli
7.2.2.6 0.08
-
 ATP
-
 Escherichia coli

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
7.2.2.6 Mg2+
-
 Escherichia coli

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
7.2.2.6 20267
-
 1 * 58189 + 1 * 72112 + 1 * 20267, DNA-sequence analysis Escherichia coli
7.2.2.6 58189
-
 1 * 58189 + 1 * 72112 + 1 * 20267, DNA-sequence analysis Escherichia coli
7.2.2.6 72112
-
 1 * 58189 + 1 * 72112 + 1 * 20267, DNA-sequence analysis Escherichia coli
7.2.2.6 150600
-
 DNA-sequence analysis Escherichia coli

Organism

EC Number Organism UniProt Comment Textmining
7.2.2.6 Escherichia coli
-
-
-
7.2.2.6 Escherichia coli TKA 1000
-
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
7.2.2.6
-
 Escherichia coli

Specific Activity [micromol/min/mg]

EC Number Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
7.2.2.6 0.964
-
-
 Escherichia coli

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
7.2.2.6 ATP + H2O + K+/out
-
 Escherichia coli ADP + phosphate + K+/in
-
 ?
7.2.2.6 ATP + H2O + K+/out
-
 Escherichia coli TKA 1000 ADP + phosphate + K+/in
-
 ?
7.2.2.6 ATP + H2O + K+[side 1] ATP in form of MgATP2- Escherichia coli ADP + phosphate + K+[side 2]
-
 ?
7.2.2.6 ATP + H2O + K+[side 1] ATP in form of MgATP2- Escherichia coli TKA 1000 ADP + phosphate + K+[side 2]
-
 ?

Subunits

EC Number Subunits Comment Organism
7.2.2.6 trimer 1 * 58189 + 1 * 72112 + 1 * 20267, DNA-sequence analysis Escherichia coli