Literature summary for 2.1.1.79 extracted from

Chang, Y.Y.; Eichel, J.; Cronan, J.E., Jr.
Metabolic instability of Escherichia coli cyclopropane fatty acid synthase is due to RpoH-dependent proteolysis (2000), J. Bacteriol., 182, 4288-4294.

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General Stability

General Stability	Organism
the enzyme is a short-lived protein in vivo and its degradation is dependent on expression of the heat shock regulon	Escherichia coli

Natural Substrates/ Products (Substrates)

Natural Substrates	Organism	Comment (Nat. Sub.)	Natural Products	Comment (Nat. Pro.)	Rev.	Reac.
S-adenosyl-L-methionine + phospholipid olefinic fatty acid	Escherichia coli	increased level of cyclopropane fatty acid synthase activity as bacterial cultures enter stationary phase is transient, activity quickly declines to the basal level, the loss of activity is due to proteolytic degradation dependent on expression of the heat shock regulon	S-adenosyl-L-homocysteine + phospholipid cyclopropane fatty acid	-	?

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	-	?
S-adenosyl-L-methionine + phospholipid olefinic fatty acid	increased level of cyclopropane fatty acid synthase activity as bacterial cultures enter stationary phase is transient, activity quickly declines to the basal level, the loss of activity is due to proteolytic degradation dependent on expression of the heat shock regulon	Escherichia coli	S-adenosyl-L-homocysteine + phospholipid cyclopropane fatty acid	-	?

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Release 2023.1 (January 2023)