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Literature summary for 2.1.1.79 extracted from

  • Courtois, F.; Ploux, O.
    Escherichia coli cyclopropane fatty acid synthase: is a bound bicarbonate ion the active-site base? (2005), Biochemistry, 44, 13583-13590.
    View publication on PubMed

Protein Variants

Protein Variants Comment Organism
C139S mutant retains 31% of the activity of the wild-type enzyme. While addition of free bicarbonate has almost no effect on the wild-type enzyme activity, the mutants enzyme is rescued by the addition of free bicarbonate. Catalytic efficiencies of the rescued mutant is 85% of wild-type activity Escherichia coli
E239A catalytic efficiency is 0.2% of wild-type value Escherichia coli
E239Q catalytic efficiency is less than 0.02% of wild-type value Escherichia coli
H266A catalytic efficiency is 5.3% of wild-type value. While addition of free bicarbonate has almost no effect on the wild-type enzyme activity, the mutants enzyme is rescued by the addition of free bicarbonate. Catalytic efficiencies of the rescued mutant is 16% of wild-type activity Escherichia coli
Y317F catalytic efficiency is 0.7% of wild-type value. While addition of free bicarbonate has almost no effect on the wild-type enzyme activity, the mutants enzyme is rescued by the addition of free bicarbonate. Catalytic efficiencies of the rescued mutant is 14% of wild-type activity Escherichia coli

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.07
-
S-adenosyl-L-methionine 37°C, pH 8.0, wild-type enzyme Escherichia coli
0.075
-
S-adenosyl-L-methionine 37°C, pH 8.0, mutant enzyme C139S Escherichia coli
0.078
-
S-adenosyl-L-methionine 37°C, pH 8.0, mutant enzyme H266A Escherichia coli

Organism

Organism UniProt Comment Textmining
Escherichia coli
-
-
-

Purification (Commentary)

Purification (Comment) Organism
wild-type and six-histidine-tagged mutant enzymes H266A, Y317F, E239A, and E239Q Escherichia coli

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
S-adenosyl-L-methionine + phospholipid olefinic fatty acid
-
Escherichia coli S-adenosyl-L-homocysteine + phospholipid cyclopropane fatty acid
-
?

Synonyms

Synonyms Comment Organism
cyclopropane fatty acid synthase
-
Escherichia coli

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
0.0025
-
S-adenosyl-L-methionine 37°C, pH 8.0, mutant enzyme H266A Escherichia coli
0.0142
-
S-adenosyl-L-methionine 37°C, pH 8.0, mutant enzyme C139S Escherichia coli
0.042
-
S-adenosyl-L-methionine 37°C, pH 8.0, wild-type enzyme Escherichia coli