Literature summary for 2.1.1.79 extracted from

Guangqi, E.; Lesage, D.; Ploux, O.
Insight into the reaction mechanism of the Escherichia coli cyclopropane fatty acid synthase: isotope exchange and kinetic isotope effects (2010), Biochimie, 92, 1454-1457.

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Cloned(Commentary)

Cloned (Comment)	Organism
His-tagged recombinant protein	Escherichia coli

Organism

Organism	UniProt	Comment	Textmining
Escherichia coli	-	-	-

Reaction

Reaction	Comment	Organism	Reaction ID
S-adenosyl-L-methionine + phospholipid olefinic fatty acid = S-adenosyl-L-homocysteine + phospholipid cyclopropane fatty acid	both chemical steps of the enzymatic cyclopropanation, the methyl addition onto the double bond and the deprotonation step, are rate determining	Escherichia coli	a

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	-	?
S-adenosyl-L-methionine + phospholipid olefinic fatty acid	-	Escherichia coli	S-adenosyl-L-homocysteine + phospholipid cyclopropane fatty acid	no exchange of the cylopropane methylene protons with the solvent during catalysis. There is a significant intermolecular primary tritium kinetic isotope effect consistent with a partially rate determining deprotonation step	?

Synonyms

Synonyms	Comment	Organism
CFAS	-	Escherichia coli
cyclopropane fatty acid synthase	-	Escherichia coli

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Release 2023.1 (January 2023)