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Literature summary for 7.6.2.1 extracted from

  • Hrafnsdottir, S.; Menon, A.K.
    Reconstitution and partial characterization of phospholipid flippase activity from detergent extracts of the Bacillus subtilis cell membrane (2000), J. Bacteriol., 182, 4198-4206.
    View publication on PubMedView publication on EuropePMC
Search for more literature for 7.6.2.1

Localization

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

Metals/Ions

Metals/Ions Comment Organism Structure
additional information Mg2+ or Ca2+ are not required Bacillus subtilis

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
ATP + phospholipid/out Bacillus subtilis
-
 ADP + phosphate + phospholipid/in
-
 ?
ATP + phospholipid/out Bacillus subtilis 1E51
-
 ADP + phosphate + phospholipid/in
-
 ?
additional information Bacillus subtilis phospholipids are synthesized on the inner leaflet of the cytoplasmic membrane in bacteria and must translocate to the outer leaflet to propagate a bilayer, transbilayer movement of phospholipids has been shown to be fast and independent of metabolic energy, and it is facilitated by membrane flippases, transport across protein-free membranes is negligible ?
-
 ?
additional information Bacillus subtilis 1E51 phospholipids are synthesized on the inner leaflet of the cytoplasmic membrane in bacteria and must translocate to the outer leaflet to propagate a bilayer, transbilayer movement of phospholipids has been shown to be fast and independent of metabolic energy, and it is facilitated by membrane flippases, transport across protein-free membranes is negligible ?
-
 ?

Organism

Organism UniProt Comment Textmining
Bacillus subtilis
-
-
-
Bacillus subtilis 1E51
-
-
-

Purification (Commentary)

Purification (Comment) Organism
membrane vesicle preparation from strain 1E51, purification by Triton X-100 extraction, glycerol fradient fractionation, and ion exchange chromatography, and reconstitution of the active enzyme in proteoliposomes, overview Bacillus subtilis

Renatured (Commentary)

Renatured (Comment) Organism
purification and reconstitution of the active enzyme in proteoliposomes, overview Bacillus subtilis

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
additional information
-
 enzyme activity in artificial membrane vesicles Bacillus subtilis

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
ATP + phospholipid/out
-
 Bacillus subtilis ADP + phosphate + phospholipid/in
-
 ?
ATP + phospholipid/out
-
 Bacillus subtilis 1E51 ADP + phosphate + phospholipid/in
-
 ?
di-C4-phosphatidylcholine/out labeled model substrate Bacillus subtilis di-C4-phosphatidylcholine/in
-
 ?
di-C4-phosphatidylcholine/out labeled model substrate Bacillus subtilis 1E51 di-C4-phosphatidylcholine/in
-
 ?
long-chain phospholipid/out
-
 Bacillus subtilis long-chain phospholipid/in
-
 ?
long-chain phospholipid/out
-
 Bacillus subtilis 1E51 long-chain phospholipid/in
-
 ?
additional information phospholipids are synthesized on the inner leaflet of the cytoplasmic membrane in bacteria and must translocate to the outer leaflet to propagate a bilayer, transbilayer movement of phospholipids has been shown to be fast and independent of metabolic energy, and it is facilitated by membrane flippases, transport across protein-free membranes is negligible Bacillus subtilis ?
-
 ?
additional information the enzyme does not require energy supply for activity Bacillus subtilis ?
-
 ?
additional information phospholipids are synthesized on the inner leaflet of the cytoplasmic membrane in bacteria and must translocate to the outer leaflet to propagate a bilayer, transbilayer movement of phospholipids has been shown to be fast and independent of metabolic energy, and it is facilitated by membrane flippases, transport across protein-free membranes is negligible Bacillus subtilis 1E51 ?
-
 ?
additional information the enzyme does not require energy supply for activity Bacillus subtilis 1E51 ?
-
 ?

Synonyms

Synonyms Comment Organism
ATP-independent flippase
-
 Bacillus subtilis

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
35
-
 assay at Bacillus subtilis

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7.5
-
 assay at Bacillus subtilis