Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary for 7.6.2.2 extracted from

  • Orelle, C.; Gubellini, F.; Durand, A.; Marco, S.; Levy, D.; Gros, P.; Di Pietro, A.; Jault, J.M.
    Conformational change induced by ATP binding in the multidrug ATP-binding cassette transporter BmrA (2008), Biochemistry, 47, 2404-2412.
    View publication on PubMed
Search for more literature for 7.6.2.2

Protein Variants

Protein Variants Comment Organism
E504A site-directed mutagenesis, ATPase inactive mutant Bacillus subtilis
E504Q site-directed mutagenesis, ATPase inactive mutant Bacillus subtilis
K380A site-directed mutagenesis, ATPase inactive mutant Bacillus subtilis
K380R site-directed mutagenesis, the ATPase activity of the mutant is highly reduced Bacillus subtilis

Inhibitors

Inhibitors Comment Organism Structure
8-azido-ATP
-
 Bacillus subtilis
vanadate
-
 Bacillus subtilis

Localization

Localization Comment Organism GeneOntology No. Textmining
membrane
-
 Bacillus subtilis 16020
-

Metals/Ions

Metals/Ions Comment Organism Structure
Mg2+
-
 Bacillus subtilis

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
ATP + H2O + xenobiotic/in Bacillus subtilis
-
 ADP + phosphate + xenobiotic/out
-
 ?

Organism

Organism UniProt Comment Textmining
Bacillus subtilis
-
-
-

Purification (Commentary)

Purification (Comment) Organism
recombinant wild-type and mutant enzymes, reconstitution in proteoliposomes Bacillus subtilis

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
1.35 1.5 purified wild-type BmrA Bacillus subtilis

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
ATP + H2O + xenobiotic/in
-
 Bacillus subtilis ADP + phosphate + xenobiotic/out
-
 ?
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

Synonyms Comment Organism
BmrA
-
 Bacillus subtilis
multidrug ATP-binding cassette transporter
-
 Bacillus subtilis
multidrug resistance ABC transporter
-
 Bacillus subtilis

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
37
-
 assay at Bacillus subtilis

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
8
-
 assay at Bacillus subtilis

Cofactor

Cofactor Comment Organism Structure
ATP
-
 Bacillus subtilis