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Literature summary for 7.1.2.2 extracted from
- Cloning, purification, and nucleotide-binding traits of the catalytic subunit A of the V1VO ATPase from Aedes albopictus (2007), Protein Expr. Purif., 53, 378-383.
Cloned(Commentary)
| Cloned (Comment) | Organism |
|---|---|
| expression of the soluble His3-tagged V1VO ATPase subunit A of in Escherichia coli | Aedes albopictus |
Metals/Ions
| Metals/Ions | Comment | Organism | Structure |
|---|---|---|---|
| Mg2+ | activates | Aedes albopictus |  |
Molecular Weight [Da]
| Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
|---|---|---|---|
| 62800 | - |
x * 62800, recombinant His3-tagged subunit A of V1VO ATPase, SDS-PAGE | Aedes albopictus |
Natural Substrates/ Products (Substrates)
| Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| ATP + H2O + H+/in | Aedes albopictus | - |
ADP + phosphate + H+/out | - |
? | |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Aedes albopictus | - |
Asian tiger mosquito | - |
Purification (Commentary)
| Purification (Comment) | Organism |
|---|---|
| recombinant soluble His3-tagged V1VO ATPase subunit A from Escherichia coli by immobilized metal affinity and ion exchange chromatography to homogeneity | Aedes albopictus |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| ATP + H2O + H+/in | - |
Aedes albopictus | ADP + phosphate + H+/out | - |
? | |
| ATP + H2O + H+/in | ADP-analogue ADP-ATTO-647N bind slightly weaker to subunit A than the ATP-analogue ATP-ATTO-647N, binding of different nucleotides cause different secondary structural alterations in this subunit | Aedes albopictus | ADP + phosphate + H+/out | - |
? | |
Subunits
| Subunits | Comment | Organism |
|---|---|---|
| ? | x * 62800, recombinant His3-tagged subunit A of V1VO ATPase, SDS-PAGE | Aedes albopictus |
| More | secondary structure analysis by circular dichroism spectroscopy shows that subunit A of V1VO ATPase comprises 43% alpha-helix, 25% beta-sheet and 40% random coil content | Aedes albopictus |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| V1VO ATPase | - |
Aedes albopictus |
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