EVIDENCE FOR ARYLAMINE N-ACETYLTRANSFERASE ACTIVITY IN THE FUNGI CANDIDA-ALBICANS

N-acetyltransferase activities were determined in Candida albicans, wh ich is a member of the normal flora of the mucous membranes in the res piratory, gastrointestinal and female genital tract. The N-acetylation of 2-aminofluorene and p-aminobenzoic acid by the N-acetyltransferase from Candida albicans was determined using high pressure liquid chrom atography. The activities (mean +/- S.D.) of N-acetyltransferase from Candida albicans cytosols were 1.06 +/- 0.01 nmol/min per mg protein f or the acetylation of 2-aminofluorene substrate, and not detectable le vels of acetyl-p-aminobenzoic acid for the acetylation of p-aminobenzo ic acid. The apparent kinetic constants K-m and V-max values were 0.17 +/- 0.06 mM and 1.43 +/- 0.42 nmol/min per mg protein, respectively, for 2-aminofluorene substrate. The optimum pH value for the enzyme act ivity was 8.0. The optimal temperature for the enzyme activity is 40 d egrees C for 2-aminofluorene substrate. Among a series of divalent cat ions and salts, Fe2+, SCN-, I-, and NH4+ were demonstrated to be the m ost potent inhibitors. The N-acetyltransferase activity was inhibited by iodoacetamide: at 0.25 mM iodoacetamide, activity was reduced 50% a nd 1.0 mM iodoacetamide inhibited activity more than 90%. This is the first demonstration of acetyl CoA arylamine N-acetyltransferase activi ty in the yeast-like fungus Candida albicans. (C) 1997 Elsevier Scienc e Ireland Ltd.