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Literature summary extracted from

  • Kawano-Kawada, M.; Takahashi, H.; Igarashi, K.; Murata, T.; Yamato, I.; Homma, M.; Kakinuma, Y.
    Significance of the glutamate-139 residue of the V-type Na+-ATPase NtpK subunit in catalytic turnover linked with salt tolerance of Enterococcus hirae (2011), J. Bacteriol., 193, 3657-3661.
    View publication on PubMedView publication on EuropePMC

Protein Variants

EC Number Protein Variants Comment Organism
7.2.2.3 E139D the E139D mutant of the NtpK subunit loses tolerance to sodium but not to lithium at pH 10. The mutant enzyme retains relatively high specific activity and affinity for the lithium ion compared to the sodium ion. Vmax values of the mutant enzyme are reduced to approximately 34% of that of the wild type enzyme Enterococcus hirae

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
7.2.2.3 0.02
-
Na+/in wild type enzyme, pH and temperature not specified in the publication Enterococcus hirae
7.2.2.3 0.029
-
ATP wild type enzyme, in the presence of Na+, pH and temperature not specified in the publication Enterococcus hirae
7.2.2.3 0.04
-
ATP wild type enzyme, in the presence of Li+, pH and temperature not specified in the publication Enterococcus hirae
7.2.2.3 0.06
-
Li+/in wild type enzyme, pH and temperature not specified in the publication Enterococcus hirae
7.2.2.3 0.067
-
ATP mutant enzyme E139D, in the presence of Li+, pH and temperature not specified in the publication Enterococcus hirae
7.2.2.3 0.1
-
ATP mutant enzyme E139D, in the presence of Na+, pH and temperature not specified in the publication Enterococcus hirae

Organism

EC Number Organism UniProt Comment Textmining
7.2.2.3 Enterococcus hirae
-
-
-
7.2.2.3 Enterococcus hirae ATCC 9790
-
-
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
7.2.2.3 ATP + H2O + Li+/in wild-type enzyme thus recognizes Na+ slightly better than Li+ Enterococcus hirae ADP + phosphate + Li+/out
-
?
7.2.2.3 ATP + H2O + Li+/in wild-type enzyme thus recognizes Na+ slightly better than Li+ Enterococcus hirae ATCC 9790 ADP + phosphate + Li+/out
-
?
7.2.2.3 ATP + H2O + Na+/in wild-type enzyme thus recognizes Na+ slightly better than Li+ Enterococcus hirae ADP + phosphate + Na+/out
-
?
7.2.2.3 ATP + H2O + Na+/in wild-type enzyme thus recognizes Na+ slightly better than Li+ Enterococcus hirae ATCC 9790 ADP + phosphate + Na+/out
-
?

Synonyms

EC Number Synonyms Comment Organism
7.2.2.3 Na+-ATPase
-
Enterococcus hirae
7.2.2.3 NtpK V-type Na+-ATPase subunit, the NtpK subunit forms the rotor ring of the Vo moiety, which is responsible for ion translocation Enterococcus hirae
7.2.2.3 vacuolar-type ATPase
-
Enterococcus hirae