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Literature summary for 7.2.2.3 extracted from
- Na+-stimulated ATPase of alkaliphilic halotolerant cyanobacterium Aphanothece halophytica translocates Na+ into proteoliposomes via Na+ uniport mechanism (2010), BMC Biochem., 11, 30.
Activating Compound
| Activating Compound | Comment | Organism | Structure |
|---|---|---|---|
| ATP | ATPase activity increases as ATP increased and the activity is saturated at about 6 mM ATP | Aphanothece halophytica |  |
| carbonyl cyanide m-chlorophenyl hydrazine | - |
Aphanothece halophytica | |
| nitrate | - |
Aphanothece halophytica | |
Inhibitors
| Inhibitors | Comment | Organism | Structure |
|---|---|---|---|
| additional information | not inhibited by 0.2 mM amiloride, 0.01 mM orthovanadate, 0.5 mM NEM, 50 mM KNO3, 20 mM KSCN, 1 mM CCP, and 1 mM ouabain | Aphanothece halophytica | |
| N,N-dicyclohexylcarbodiimide | 78% residual activity at 1 mM in the presence of 10 mM NaCl. Inhibition in the absence of NaCl occurs after 20 min yielding 80 and 70% inhibition at pH 7.6 and pH 9.0, respectively | Aphanothece halophytica | |
| Sodium azide | 64% residual activity at 5 mM | Aphanothece halophytica | |
KM Value [mM]
| KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|
| 1.2 | - |
ATP | apparent value, at pH 7.6, temperature not specified in the publication | Aphanothece halophytica | |
| 2 | - |
Na+/in | apparent value, at pH 7.6, temperature not specified in the publication | Aphanothece halophytica | |
Localization
| Localization | Comment | Organism | GeneOntology No. | Textmining |
|---|---|---|---|---|
| membrane | proteoliposome | Aphanothece halophytica | 16020 | - |
Metals/Ions
| Metals/Ions | Comment | Organism | Structure |
|---|---|---|---|
| Mg2+ | maximal ATPase activity is observed at 5 mM Mg2+ | Aphanothece halophytica | |
| additional information | K+, Li+, and Ca2+ have no stimulatory effect on enzyme activity | Aphanothece halophytica | |
| Na+ | the enzyme is stimulated about 9fold at pH 7.6 and about 11fold at both pH 9.0 and 11.0 with 10 mM NaCl | Aphanothece halophytica | |
Molecular Weight [Da]
| Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
|---|---|---|---|
| 6500 | - |
x * 56000 + x * 52000 + x * 35000 + x * 25000 + x * 22000 + x * 16500 + x * 6500, SDS-PAGE | Aphanothece halophytica |
| 16500 | - |
x * 56000 + x * 52000 + x * 35000 + x * 25000 + x * 22000 + x * 16500 + x * 6500, SDS-PAGE | Aphanothece halophytica |
| 22000 | - |
x * 56000 + x * 52000 + x * 35000 + x * 25000 + x * 22000 + x * 16500 + x * 6500, SDS-PAGE | Aphanothece halophytica |
| 25000 | - |
x * 56000 + x * 52000 + x * 35000 + x * 25000 + x * 22000 + x * 16500 + x * 6500, SDS-PAGE | Aphanothece halophytica |
| 35000 | - |
x * 56000 + x * 52000 + x * 35000 + x * 25000 + x * 22000 + x * 16500 + x * 6500, SDS-PAGE | Aphanothece halophytica |
| 52000 | - |
x * 56000 + x * 52000 + x * 35000 + x * 25000 + x * 22000 + x * 16500 + x * 6500, SDS-PAGE | Aphanothece halophytica |
| 56000 | - |
x * 56000 + x * 52000 + x * 35000 + x * 25000 + x * 22000 + x * 16500 + x * 6500, SDS-PAGE | Aphanothece halophytica |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Aphanothece halophytica | - |
- |
- |
Purification (Commentary)
| Purification (Comment) | Organism |
|---|---|
| PEG 6000 precipitation and Superose 6 gel filtration | Aphanothece halophytica |
Specific Activity [micromol/min/mg]
| Specific Activity Minimum [µmol/min/mg] | Specific Activity Maximum [µmol/min/mg] | Comment | Organism |
|---|---|---|---|
| 0.0266 | - |
crude enzyme from membrane vesicles, at pH 7.6, temperature not specified in the publication | Aphanothece halophytica |
| 0.4667 | - |
after 17.5fold purification, at pH 7.6, temperature not specified in the publication | Aphanothece halophytica |
Storage Stability
| Storage Stability | Organism |
|---|---|
| -20°C, purified enzyme, 1 month, the enzyme remains stable | Aphanothece halophytica |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| ATP + H2O + Na+/in | the purified enzyme catalyzes the hydrolysis of ATP in the presence of Na+ but not K+, Li+ and Ca2+ | Aphanothece halophytica | ADP + phosphate + Na+/out | - |
? | |
Subunits
| Subunits | Comment | Organism |
|---|---|---|
| ? | x * 56000 + x * 52000 + x * 35000 + x * 25000 + x * 22000 + x * 16500 + x * 6500, SDS-PAGE | Aphanothece halophytica |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| Na+-stimulated ATPase | - |
Aphanothece halophytica |
pH Stability
| pH Stability | pH Stability Maximum | Comment | Organism |
|---|---|---|---|
| 6 | 11 | when the pH is increased from pH 6.0 to pH 9.0, the enzyme activity is increased progressively. Increasing the pH further to pH 11.0 results in a slightly declined enzyme activity | Aphanothece halophytica |
Expression
| Organism | Comment | Expression |
|---|---|---|
| Aphanothece halophytica | cells grown at 2 M NaCl show higher enzyme activity than those grown at 0.5 M NaCl. ATPase activity in is slightly increased upon increasing the pH from 5.0 to 7.6 | up |
General Information
| General Information | Comment | Organism |
|---|---|---|
| physiological function | the enzyme functions as an electrogenic Na+ pump which transports only Na+ upon hydrolysis of ATP. Na+- and ATP-dependent H+ efflux from proteoliposomes, is driven by the electric potential generated by Na+-stimulated ATPase | Aphanothece halophytica |
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