Inhibition of L-Glycerol 3-Phosphate Acyltransferase from Escherichia coil by cis-9, l0-Methylenehexadecanoic Acid

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Abstract
Acyl-CoA: L-glycerol 3-phosphate acyltransferase [EC 2.3.1.15] from E. coli is a particulate enzyme, which was found to be inhibited by cis-9, 10-methylenehexadecanoate. The inhibition was noncompetitive with respect to L-glycerol 3-phosphate. Palmitate, elaidate, and trans-vaccenate showed no inhibition of the acyltransferase, whereas palmitoleate, oleate, and cis-vaccenate inhibited. cis-9, l0-Methylenehexadecanoate was approximately twice as inhibitory as mono-olefinic acids. The free fatty acids in the cells were also found to vary with different growth phases. There was a ten-fold increase in the amount of free cis-9, l0-methylenehexadecanoic acid in the cells from the early exponential to the stationary phase.

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