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Literature summary for 7.1.2.1 extracted from

  • Sampedro, J.G.; Ruiz-Granados, Y.G.; Najera, H.; Tellez-Valencia, A.; Uribe, S.
    Fluorescence quenching by nucleotides of the plasma membrane H+-ATPase from Kluyveromyces lactis (2007), Biochemistry, 46, 5616-5622.
    View publication on PubMed

Inhibitors

Inhibitors Comment Organism Structure
adenosine 5'-(beta,gamma-imido)-triphosphate 5 mM, 60% inhibition Kluyveromyces lactis
ADP 5 mM, 60% inhibition, Kd value 0.8 mM Kluyveromyces lactis

Localization

Localization Comment Organism GeneOntology No. Textmining

Organism

Organism UniProt Comment Textmining
Kluyveromyces lactis
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-
-

Purification (Commentary)

Purification (Comment) Organism
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Kluyveromyces lactis

Reaction

Reaction Comment Organism Reaction ID
ATP + H2O + 4 H+[side 1] = ADP + phosphate + 4 H+[side 2] binding of the nucleotide to the N-domain is coupled to the movement of a loop beta structure and to the exposure of the W505 residue located in the loop Kluyveromyces lactis

Source Tissue

Source Tissue Comment Organism Textmining

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
ATP + H2O + H+/in reaction is slightly cooperative, Hill number 1.5, S0.5 value 0.8 mM ATP. Kd value of ATP 0.7 mM Kluyveromyces lactis ADP + phosphate + H+/out
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Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
3 6 ATP pH 6.8, 25°C Kluyveromyces lactis