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Literature summary extracted from

  • Murata, T.; Yamato, I.; Kakinuma, Y.; Shirouzu, M.; Walker, J.E.; Yokoyama, S.; Iwata, S.
    Ion binding and selectivity of the rotor ring of the Na+-transporting V-ATPase (2008), Proc. Natl. Acad. Sci. USA, 105, 8607-8612.
    View publication on PubMedView publication on EuropePMC

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
7.2.2.1 0.005 ml of 2 mg/ml purified K-ring in 20 mM Tris-HCl, pH 7.5, 100 mM LiCl, 10% glycerol, and 0.32 mM n-dodecyl-beta-D-maltoside by sitting drop vapor diffusion method, mixing with 0.005 ml of reservoir solution consisting of 100 mM Tris-HCl, pH 7.5, 4% glycerol, 240 mM potassium citrate, 1.2 mM undecylmaltoside, and 34% PEG 400, at 20°C, in presence or absence of 10 mM NaCl, first appearance after 3 days, maximal size after 3 weeks, X-ray diffraction structure determination and analysis at 2.8 A resolution Enterococcus hirae

Inhibitors

EC Number Inhibitors Comment Organism Structure
7.2.2.1 H+ competitively inhibits binding of Na+ to the K-ring of the enzyme, binding structure, overview Enterococcus hirae
7.2.2.1 Li+ competitively inhibits binding of Na+ to the K-ring of the enzyme, binding structure, overview Enterococcus hirae

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
7.2.2.1 additional information
-
 additional information Na+ binding kinetics Enterococcus hirae

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
7.2.2.1 ATP + H2O + Na+/in Enterococcus hirae
-
 ADP + phosphate + Na+/out
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
7.2.2.1 Enterococcus hirae
-
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
7.2.2.1 purification of the V-ATPase and isolation of the K-ring by by anion exchange chromatography and gel filtration Enterococcus hirae

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
7.2.2.1 ATP + H2O + Na+/in
-
 Enterococcus hirae ADP + phosphate + Na+/out
-
 ?
7.2.2.1 ATP + H2O + Na+/in the purified rotor ring, i.e. K-ring, of the V-ATPase binds one Na+ ion per K-monomer with high affinity. Interaction with the stator subunit, i.e. I-subunit, is essential for Na binding to or release from the K-ring, respectively, ion translocation model, overview Enterococcus hirae ADP + phosphate + Na+/out
-
 ?
7.2.2.1 additional information K+, Tl+, Rb+, and Cs+ cannot substitute Na+ Enterococcus hirae ?
-
 ?

Synonyms

EC Number Synonyms Comment Organism
7.2.2.1 Na+-transporting V-ATPase
-
 Enterococcus hirae
7.2.2.1 vacuole-type ATPase
-
 Enterococcus hirae

Cofactor

EC Number Cofactor Comment Organism Structure
7.2.2.1 ATP
-
 Enterococcus hirae