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Literature summary for 7.4.2.5 extracted from

  • Benabdelhak, H.; Schmitt, L.; Horn, C.; Jumel, K.; Blight, M.A.; Holland, I.B.
    Positive co-operative activity and dimerization of the isolated ABC ATPase domain of HlyB from Escherichia coli (2005), Biochem. J., 386, 489-495.
    View publication on PubMedView publication on EuropePMC
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Protein Variants

Protein Variants Comment Organism
D630M ATPase activity is 0.6% of wild-type activity Escherichia coli
K508M ATPase activity is 1.3% of wild-type activity Escherichia coli
P624C insoluble mutant protein Escherichia coli
P624L insoluble mutant protein Escherichia coli
P624R insoluble mutant protein Escherichia coli
P624S insoluble mutant protein Escherichia coli
V548A insoluble mutant protein Escherichia coli

Inhibitors

Inhibitors Comment Organism Structure
KCl no ATPase activity above 300 mM Escherichia coli
NaCl no ATPase activity above 300 mM Escherichia coli
orthovanadate IC50: 0.016 mM, competitive Escherichia coli

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.65
-
 ATP pH 8.0, 25°C, 10 mM NaCl Escherichia coli
1.09
-
 ATP pH 8.0, 25°C, 50 mM NaCl Escherichia coli
1.5
-
 ATP pH 8.0, 25°C, 100 mM NaCl Escherichia coli
2.33
-
 ATP pH 8.0, 25°C, 200 mM NaCl Escherichia coli

Metals/Ions

Metals/Ions Comment Organism Structure
Co2+ divalent cation required, Mg2+ shows 40% of the activity with Mn2+ Escherichia coli
Mg2+ divalent cation required, Mg2+ shows 80% of the activity with Mn2+ Escherichia coli
Mn2+ divalent cation required, Mn2+ is most effective Escherichia coli

Organism

Organism UniProt Comment Textmining
Escherichia coli
-
-
-

Storage Stability

Storage Stability Organism
-80°C, the ATPase domain is indefinitly stable in phosphate or Tris buffer, pH 8, in the absence of ATP concentrations of up to 25 mg/ml Escherichia coli
4°C, the ATPase domain is stable for at least 2 days in phosphate or Tris buffer, pH 8, in the absence of ATP concentrations of up to 25 mg/ml Escherichia coli

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
ATP + H2O + alpha-haemolysin/in
-
 Escherichia coli ADP + phosphate + alpha-haemolysin/out
-
 ?
ATP + H2O + alpha-haemolysin/in
-
 Escherichia coli DH5-alpha ADP + phosphate + alpha-haemolysin/out
-
 ?

Subunits

Subunits Comment Organism
monomer under most conditions, only the monomer form can be detected, indicating that dimers are very unstable. Monomers can interact at least transiently and are the important species during ATP hydrolysis Escherichia coli

Synonyms

Synonyms Comment Organism
HlyB
-
 Escherichia coli

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
0.11
-
 ATP pH 8.0, 25°C, 200 mM NaCl Escherichia coli
0.2
-
 ATP pH 8.0, 25°C, 100 mM NaCl Escherichia coli
0.31
-
 ATP pH 8.0, 25°C, 50 mM NaCl Escherichia coli
0.33
-
 ATP pH 8.0, 25°C, 10 mM NaCl Escherichia coli

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
8
-
-
 Escherichia coli

pH Range

pH Minimum pH Maximum Comment Organism
7 8.5 pH 7.0: about 75% of maximal activity, pH 8.5: about 85% of maximal activity Escherichia coli

IC50 Value

IC50 Value IC50 Value Maximum Comment Organism Inhibitor Structure
0.016
-
 IC50: 0.016 mM, competitive Escherichia coli orthovanadate