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Literature summary for 7.2.2.1 extracted from

  • Kawano, M.; Igarashi, K.; Yamato, I.; Kakinuma, Y.
    Arginine residue at position 573 in Enterococcus hirae vacuolar-type ATPase NtpI subunit plays a crucial role in Na+ translocation (2002), J. Biol. Chem., 277, 24405-24410.
    View publication on PubMed
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Protein Variants

Protein Variants Comment Organism
R573E inactive mutant Enterococcus hirae
R573K mutant can grow in alcaline medium Enterococcus hirae
R573L inactive mutant Enterococcus hirae
R573Q inactive mutant Enterococcus hirae

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.002
-
 Na+/in biphasic affinity Enterococcus hirae
5
-
 Na+/in biphasic affinity Enterococcus hirae

Localization

Localization Comment Organism GeneOntology No. Textmining

Organism

Organism UniProt Comment Textmining
Enterococcus hirae
-
 ATCC 9790
-

Purification (Commentary)

Purification (Comment) Organism
purification of a His-tagged enzyme by affinity column chromatography Enterococcus hirae

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
0.00024
-
 ATPase activity, R573K mutant, pH 8.8, 20 mM NaCl Enterococcus hirae
0.00114
-
 ATPase activity, wild type enzyme, pH 8.8, 20 mM NaCl Enterococcus hirae

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
ATP + H2O + Na+/in
-
 Enterococcus hirae ADP + phosphate + Na+/out
-
 r