Phosphatidic Acid Synthesis in Escherichia coli

AUTOR(ES)

Kito, Makoto

RESUMO

The kinetic properties of acyl-coenzyme A (CoA): l-α-glycerol-phosphate trans-acylase (EC 2.3.1.15) from Escherichia coli were studied. At 10 C, a temperature at which the reaction was proportional to time and enzyme concentration, the enzyme had an apparent Km of 60 μm for l-α-glycerol-phosphate. The curve describing the velocity of the reaction as a function of palmitoyl-CoA concentration was sigmoid but the plot of v−1 versus [S]−3 gave a straight line. A Km of about 11 μm was calculated for palmitoyl-CoA. Adenosine triphosphate specifically inhibited the reaction, being a noncompetitive inhibitor in respect to l-α-glycerol phosphate. Inhibition only occurred with high concentrations of palmitoyl-CoA, and maximal inhibition was 60%.

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