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Literature summary for 7.2.2.13 extracted from

  • Lifshitz, Y.; Lindzen, M.; Garty, H.; Karlish, S.J.
    Functional interactions of phospholemman (PLM) (FXYD1) with Na+,K+-ATPase. Purification of alpha1/beta1/PLM complexes expressed in Pichia pastoris (2006), J. Biol. Chem., 281, 15790-15799.
    View publication on PubMed
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Cloned(Commentary)

Cloned (Comment) Organism
expression in Pichia pastoris, with human transmembrane protein phospholemman Sus scrofa
expression of alpha subunit in HeLa cell, with rat transmembrane protein phospholemman Rattus norvegicus

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
additional information
-
 additional information presence of phospholemman lowers the K0.5 value for Na+ ions by about 30%, but does not affect the turnover rate or Km value of ATP. Different functional effects depend on the degree of phosphorylation of phospholemman at residue S68 Sus scrofa
additional information
-
 additional information presence of phospholemman raises the K0.5 value for Na+ ions. Different functional effects depend on the degree of phosphorylation of phospholemman at residue S68 Rattus norvegicus

Organism

Organism UniProt Comment Textmining
Rattus norvegicus
-
-
-
Sus scrofa P05024
-
-

Purification (Commentary)

Purification (Comment) Organism
recombinant alpha/beta subunits in complex with phospholemman Sus scrofa

Subunits

Subunits Comment Organism
More presence of transmembrane protein phospholemman in a complex with Na+K+-ATPase alpha/beta subunits markedly stabilizes Sus scrofa