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Literature summary extracted from

  • Heitkamp, T.; Kalinowski, R.; Boettcher, B.; Boersch, M.; Altendorf, K.; Greie, J.
    K+-translocating KdpFABC P-type ATPase from Escherichia coli acts as a functional and structural dimer (2008), Biochemistry, 47, 3564-3575.
    View publication on PubMed

Cloned(Commentary)

EC Number Cloned (Comment) Organism
7.2.2.6 expression of wild-type and mutant enzymes in strain TKW3205 Escherichia coli

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
7.2.2.6 additional information
-
 additional information kinetics Escherichia coli

Localization

EC Number Localization Comment Organism GeneOntology No. Textmining
7.2.2.6 membrane intramembrane enzyme Escherichia coli 16020
-

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
7.2.2.6 72000
-
 2 * 72000, SDS-PAGE, functional and structural dimeric enzyme with a close vicinity of two KdpB subunits within the functional KdpFABC complex, a dissociation constant for a monomer/dimer equilibrium between 30 and 50 nM, structure, overview Escherichia coli
7.2.2.6 350000
-
 gel filtration, KdpFABC complex, a cross-linked preparation Escherichia coli

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
7.2.2.6 ATP + H2O + K+/out Escherichia coli
-
 ADP + phosphate + K+/in
-
 ?

Organism

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

Reaction

EC Number Reaction Comment Organism Reaction ID
7.2.2.6 ATP + H2O + K+[side 1] = ADP + phosphate + K+[side 2] catalytic mechanism Escherichia coli
a

Renatured (Commentary)

EC Number Renatured (Comment) Organism
7.2.2.6 reconstitution of functional dimeric KdpFABC complexes, overview 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
-
 ?

Subunits

EC Number Subunits Comment Organism
7.2.2.6 dimer 2 * 72000, SDS-PAGE, functional and structural dimeric enzyme with a close vicinity of two KdpB subunits within the functional KdpFABC complex, a dissociation constant for a monomer/dimer equilibrium between 30 and 50 nM, structure, overview Escherichia coli

Synonyms

EC Number Synonyms Comment Organism
7.2.2.6 K+-translocating KdpFABC P-type ATPase
-
 Escherichia coli
7.2.2.6 More the enzyme belongs to the superfamily of P-type ATPases Escherichia coli

Cofactor

EC Number Cofactor Comment Organism Structure
7.2.2.6 ATP two cooperative ATP-binding sides within the functional enzyme Escherichia coli