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Literature summary for 7.6.2.1 extracted from

  • Doerrler, W.T.; Raetz, C.R.
    ATPase activity of the MsbA lipid flippase of Escherichia coli (2002), J. Biol. Chem., 277, 36697-36705.
    View publication on PubMed
Search for more literature for 7.6.2.1

Activating Compound

Activating Compound Comment Organism Structure
Kdo2-lipid A
-
 Escherichia coli
Phospholipids The activity of purified MsbA is dependent upon the presence of phospholipids. Escherichia coli

Cloned(Commentary)

Cloned (Comment) Organism
the gene MsbA is cloned into pET28b behind the T7 promoter in-frame with an N-terminal His6tag Escherichia coli

Protein Variants

Protein Variants Comment Organism
A270T mutant and wild-type enzymes have similar activities at 30°C, but the mutant activity is decreased significant at 42°C Escherichia coli

Inhibitors

Inhibitors Comment Organism Structure
vanadate maximal half-inhibition at 0.035 mM Escherichia coli

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.878
-
 ATP pH 7.5, 37°C, KM value of purified, detergent-solubilized MsbA, whereas the KM value calculated in the presence of 0.05 mM KdO2-lipid A is decreased by more than half Escherichia coli

Organism

Organism UniProt Comment Textmining
Escherichia coli
-
-
-

Purification (Commentary)

Purification (Comment) Organism
recombinant wild-type and mutant enzymes Escherichia coli

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
0.002 0.004 activity of purified, detergent-solubilized MsbA Escherichia coli

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
ATP + H2O
-
 Escherichia coli ADP + phosphate
-
 ?

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7 8.5
-
 Escherichia coli