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Literature summary 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

Activating Compound

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

Cloned(Commentary)

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

Protein Variants

EC Number Protein Variants Comment Organism
7.6.2.1 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

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

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
7.6.2.1 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

EC Number Organism UniProt Comment Textmining
7.6.2.1 Escherichia coli
-
-
-

Purification (Commentary)

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

Specific Activity [micromol/min/mg]

EC Number Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
7.6.2.1 0.002 0.004 activity of purified, detergent-solubilized MsbA Escherichia coli

Substrates and Products (Substrate)

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

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
7.6.2.1 7 8.5
-
Escherichia coli