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AbstractA cytosolic polyamine N-acetyltransferase that preferentially catalyzes the acetylation of spermidine in the N8-position was identified in the free-living pathogenic amoeba Acanthamoeba culbertsoni. In addition to spermidine, the enzyme also catalyzed the acetylation of spermine and putrescine with Michaelis constants (Km values) of 97, 12, and 10M, respectively. The Km value for acetylcoenzyme...
AbstractThe characteristics and kinetic properties of an arylalkylamine N-acetyltransferase were studied in partially purified preparations of the human filarial parasite Onchocerca volvulus. The enzyme, which had a relative molecular mass (Mr) of 3738 kDa, catalyzed the acetylation of arylalkylamines but did not accept arylamines or polyamines as substrates. The optimal pH for enzyme activity was...