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Literature summary for 2.1.1.79 extracted from

  • Iwig, D.F.; Uchida, A.; Stromberg, J.A.; Booker, S.J.
    The activity of Escherichia coli cyclopropane fatty acid synthase depends on the presence of bicarbonate (2005), J. Am. Chem. Soc., 127, 11612-11613.
    View publication on PubMed
Search for more literature for 2.1.1.79

Activating Compound

Activating Compound Comment Organism Structure
bicarbonate required. CFA synthase isolated and assayed in potassium bicarbonate buffer displayes more than 3-fold higher activity than in HEPES buffer Escherichia coli

Protein Variants

Protein Variants Comment Organism
E239A mutant shows 0.57% of wild-type activity Escherichia coli
E239D mutant shows 0.96% of wild-type activity Escherichia coli
H266A mutant shows 2.1% of wild-type activity Escherichia coli
Y317F mutant shows 0.45% of wild-type activity Escherichia coli

Inhibitors

Inhibitors Comment Organism Structure
Borate competitive Escherichia coli

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.0705
-
 S-adenosyl-L-methionine purification buffer/assay buffer: KHCO3/HEPES Escherichia coli
0.0716
-
 S-adenosyl-L-methionine purification buffer/assay buffer: HEPES/KHCO3 Escherichia coli
0.0887
-
 S-adenosyl-L-methionine purification buffer/assay buffer: HEPES/HEPES Escherichia coli
0.0997
-
 S-adenosyl-L-methionine purification buffer/assay buffer: KHCO3/KHCO3 Escherichia coli

Organism

Organism UniProt Comment Textmining
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
CFA synthase
-
 Escherichia coli

Ki Value [mM]

Ki Value [mM] Ki Value maximum [mM] Inhibitor Comment Organism Structure
2.02
-
 Borate
-
 Escherichia coli