Hydrolysis of ester- and amide-type drugs by the purified isoenzymes of nonspecific carboxylesterase from rat liver.
Five purified carboxylesterases from rat liver microsomes show a differing capacity for the hydrolysis of ester- and amide-type drugs. The two closely related enzymes that are responsible for the microsomal hydrolysis of palmitoyl-CoA and long chain monoacylglycerides exhibit the highest propanidid-and aspirin-cleaving rates. The predominant nonspecific esterase of microsomes is responsible for the hydrolysis of procaine, clofibrate, isoarecaidine esters, butanilicaine, octanoylamide, and possibly butyryl thiocholine. Finally, the palmitoyl carnitine-cleaving esterase splits phenacetin and acetanilide. The purified nonspecific esterase with the lowest isoelectric point is not involved in the metabolism of the drugs mentioned.
D000577:Amides / Q000378:metabolism*; D000818:Animals; D001115:Arecoline / Q000031:analogs & derivatives / Q000378:metabolism; D001241:Aspirin / Q000378:metabolism; D043182:Carboxylesterase; D002264:Carboxylic Acids / Q000378:metabolism*; D002265:Carboxylic Ester Hydrolases / Q000302:isolation & purification / Q000378:metabolism*; D002794:Choline / Q000031:analogs & derivatives / Q000378:metabolism; D002994:Clofibrate / Q000378:metabolism; D004952:Esters / Q000378:metabolism*; D006868:Hydrolysis; D066298:In Vitro Techniques; D007527:Isoenzymes / Q000302:isolation & purification / Q000378:metabolism; D007700:Kinetics; D008862:Microsomes, Liver / Q000201:enzymology*; D011343:Procaine / Q000378:metabolism; D011410:Propanidid / Q000378:metabolism; D051381:Rats
D000577:Amides; D002264:Carboxylic Acids; D004952:Esters; D007527:Isoenzymes; C015000:arecaidine esters; D001115:Arecoline; D011343:Procaine; D011410:Propanidid; D002265:Carboxylic Ester Hydrolases; D043182:Carboxylesterase; D002994:Clofibrate; D002794:Choline; D001241:Aspirin