Any feedback?
Literature summary extracted from
- Conformational change induced by ATP binding in the multidrug ATP-binding cassette transporter BmrA (2008), Biochemistry, 47, 2404-2412.
Protein Variants
| EC Number | Protein Variants | Comment | Organism |
|---|---|---|---|
| 7.6.2.2 | E504A | site-directed mutagenesis, ATPase inactive mutant | Bacillus subtilis |
| 7.6.2.2 | E504Q | site-directed mutagenesis, ATPase inactive mutant | Bacillus subtilis |
| 7.6.2.2 | K380A | site-directed mutagenesis, ATPase inactive mutant | Bacillus subtilis |
| 7.6.2.2 | K380R | site-directed mutagenesis, the ATPase activity of the mutant is highly reduced | Bacillus subtilis |
Inhibitors
| EC Number | Inhibitors | Comment | Organism | Structure |
|---|---|---|---|---|
| 7.6.2.2 | 8-azido-ATP | - |
Bacillus subtilis |  |
| 7.6.2.2 | vanadate | - |
Bacillus subtilis | |
Localization
| EC Number | Localization | Comment | Organism | GeneOntology No. | Textmining |
|---|---|---|---|---|---|
| 7.6.2.2 | membrane | - |
Bacillus subtilis | 16020 | - |
Metals/Ions
| EC Number | Metals/Ions | Comment | Organism | Structure |
|---|---|---|---|---|
| 7.6.2.2 | Mg2+ | - |
Bacillus subtilis | |
Natural Substrates/ Products (Substrates)
| EC Number | Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
|---|---|---|---|---|---|---|---|
| 7.6.2.2 | ATP + H2O + xenobiotic/in | Bacillus subtilis | - |
ADP + phosphate + xenobiotic/out | - |
? | |
Organism
| EC Number | Organism | UniProt | Comment | Textmining |
|---|---|---|---|---|
| 7.6.2.2 | Bacillus subtilis | - |
- |
- |
Purification (Commentary)
| EC Number | Purification (Comment) | Organism |
|---|---|---|
| 7.6.2.2 | recombinant wild-type and mutant enzymes, reconstitution in proteoliposomes | Bacillus subtilis |
Specific Activity [micromol/min/mg]
| EC Number | Specific Activity Minimum [µmol/min/mg] | Specific Activity Maximum [µmol/min/mg] | Comment | Organism |
|---|---|---|---|---|
| 7.6.2.2 | 1.35 | 1.5 | purified wild-type BmrA | Bacillus subtilis |
Substrates and Products (Substrate)
| EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|---|
| 7.6.2.2 | ATP + H2O + xenobiotic/in | - |
Bacillus subtilis | ADP + phosphate + xenobiotic/out | - |
? | |
| 7.6.2.2 | ATP + H2O + xenobiotic/in | the enzyme forms stable, highly ordered ring-shaped structures, that are destroyed or whose formation is prevented upon addition of ATP in the presence of Mg2+ and the subsequent catalytic step responsible for such an effect, overview | Bacillus subtilis | ADP + phosphate + xenobiotic/out | - |
? | |
Synonyms
| EC Number | Synonyms | Comment | Organism |
|---|---|---|---|
| 7.6.2.2 | BmrA | - |
Bacillus subtilis |
| 7.6.2.2 | multidrug ATP-binding cassette transporter | - |
Bacillus subtilis |
| 7.6.2.2 | multidrug resistance ABC transporter | - |
Bacillus subtilis |
Temperature Optimum [°C]
| EC Number | Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
|---|---|---|---|---|
| 7.6.2.2 | 37 | - |
assay at | Bacillus subtilis |
pH Optimum
| EC Number | pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|---|
| 7.6.2.2 | 8 | - |
assay at | Bacillus subtilis |
Cofactor
| EC Number | Cofactor | Comment | Organism | Structure |
|---|---|---|---|---|
| 7.6.2.2 | ATP | - |
Bacillus subtilis | |
Use of this online version of BRENDA is free under the CC BY 4.0 license. See terms of use for full details.
Release 2023.1 (January 2023)
Legal
Curated at
Member of
