N-Acetyltransferase activities with p-aminobenzoic acid and 2-aminoflu
orene as substrates were determined in isolates of the bacterium Esche
richia coli. The N-acetyltransferase activity was determined by an ace
tyl CoA recycling assay and high pressure liquid chromatography. The N
-acetyltransferase activities from a number of E. coli isolates were f
ound to be 0.67 +/- 0.04 nmole/min/mg protein for 2-aminofluorene, and
0.46 +/- 0.02 nmole/min/mg protein for p-aminobenzoic acid. The appar
ent K-m and V-max values obtained were 2.85 +/- 0.65 mM and 7.51 +/- 0
.86 nmol/min/mg protein, respectively, for 2-aminofluorene, and 2.35 /- 0.39 mM and 9.43 +/- 0.78 nmol/min/mg protein, respectively, for p-
aminobenzoic acid. The optimal pH value for the enzyme activity was 7.
0 for both substrates tested. The optimal temperature for enzyme activ
ity was 37 degrees C for both substrates. The N-acetyltransferase acti
vity was inhibited by iodoacetamide: at 0.25 mM iodoacetamide, activit
y was reduced 50%, and at 1.0 mM, more than 90%. Among a series of div
alent cations and salts, CU2+ and Zn2+ were demonstrated to be the mos
t potent inhibitors. This report is the first demonstration of acetyl
CoA:arylamine N-acetyltransferase activity in E. coli.