PT  - JOURNAL ARTICLE
AU  - Osamu Ueda
AU  - Shigeyuki Kitamura
AU  - Shigeru Ohta
TI  - Deacylation of <em>N</em>-Arylformamides and<em>N</em>-Arylacetamides by Formamidase in Rat Liver
AID  - 10.1124/dmd.30.12.1297
DP  - 2002 Dec 01
TA  - Drug Metabolism and Disposition
PG  - 1297--1299
VI  - 30
IP  - 12
4099  - http://dmd.aspetjournals.org/content/30/12/1297.short
4100  - http://dmd.aspetjournals.org/content/30/12/1297.full
SO  - Drug Metab Dispos2002 Dec 01; 30
AB  - The in vitro deacylation of N-arylformamides and N-arylacetamides to arylamines was examined in rat liver preparations. When 2-acetylaminofluorene or 2-formylaminofluorene was incubated with rat liver microsomes or cytosol, the deacylated metabolite, 2-aminofluorene, was formed. The deacylating activity of liver microsomes was inhibited by bis(4-nitrophenyl)phosphate and phenylmethanesulfonyl fluoride, inhibitors of carboxylesterase. In contrast, the activity of liver cytosol was inhibited by diisopropyl fluorophosphate, an inhibitor of formamidase. Deacylation of these compounds appear to be mainly catalyzed by carboxylesterase in liver microsomes and formamidase in liver cytosol. 2-Formylaminofluorene, 2-acetylaminofluorene, 1-formylaminopyrene, 4-formylaminobiphenyl, 2-formylaminonaphthalene, 1-formylaminonaphthalene, and 2-acetylaminofluorene were deacylated by formamidase purified from rat liver cytosol. Formamidase catalyzed both N-formylation of arylamines, and deacylation of N-arylformamides andN-arylacetamides. The American Society for Pharmacology and Experimental Therapeutics