Subcellular localization and some properties of the N-deacetylase of the Cestode Moniezia expansa.
1. Acetanilide, acetamidophenol, acetanisidide, acetamidobenzoic acid and acetamidobenzaldehyde were hydrolysed by enzyme preparations from Moniezia expansa. Deacetylation occurred in the distal cytoplasm of the proglottids. 2. N-Deacetylase activity was found in the 75 000g supernatant of the tapeworm homogenates. The molecular weight of the enzyme was about 95 000. 3. The optimal pH of deacetylation for all substrates was 7-4. Dithiothreitol enhanced the reaction, but glutathione and cysteine were without effect. 4. Deacetylase activity was inhibited by p-chloromercuribenzoate, N-ethylmaleimide, Zn++, Cu++ and anthelmintic organophosphates.
D000083:Acetanilides / Q000378:metabolism; D000115:Acetylesterase / Q000037:antagonists & inhibitors; D000581:Amidohydrolases / Q000378:metabolism*; D000813:Anilides; D000818:Animals; D002589:Cestoda / Q000201:enzymology*; D008970:Molecular Weight; D009943:Organophosphorus Compounds / Q000494:pharmacology; D012756:Sheep; D013438:Sulfhydryl Compounds / Q000494:pharmacology; D013439:Sulfhydryl Reagents / Q000494:pharmacology
D000083:Acetanilides; D000813:Anilides; D009943:Organophosphorus Compounds; D013438:Sulfhydryl Compounds; D013439:Sulfhydryl Reagents; D000115:Acetylesterase; D000581:Amidohydrolases