Structural highlights
Function
EST1_PIG Involved in the detoxification of xenobiotics and in the activation of ester and amide prodrugs. Active towards triacylglycerides containing short-chain fatty acids from C2 to C6, and 1(3)-monoacylglycerols containing fatty acids from C2 to C12. Inactive on long-chain triacylglycerols and diacylglycerol. Hydrolyzes aromatic and alkyl esters and vitamin A acetate. The hydrolysis rate depends upon the amino acid promoiety and the esterification site of the prodrug. Aromatic promoieties are favored, highest rates are observed with phenylalanyl progdrugs, hydrolysis of valyl and isoleucyl prodrugs is less efficient. With floxuridine prodrugs, activity is higher on 5' monoesters than on 3' monoesters. With gemcitabine prodrugs, activity is higher on 3' monoesters than on 5' monoesters.[1] [2] [3]
References
- ↑ Landowski CP, Lorenzi PL, Song X, Amidon GL. Nucleoside ester prodrug substrate specificity of liver carboxylesterase. J Pharmacol Exp Ther. 2006 Feb;316(2):572-80. PMID:16223870 doi:10.1124/jpet.105.092726
- ↑ Schindler R, Mentlein R, Feldheim W. Purification and characterization of retinyl ester hydrolase as a member of the non-specific carboxylesterase supergene family. Eur J Biochem. 1998 Feb 1;251(3):863-73. PMID:9490062 doi:10.1046/j.1432-1327.1998.2510863.x
- ↑ David L, Guo XJ, Villard C, Moulin A, Puigserver A. Purification and molecular cloning of porcine intestinal glycerol-ester hydrolase--evidence for its identity with carboxylesterase. Eur J Biochem. 1998 Oct 1;257(1):142-8. PMID:9799112 doi:10.1046/j.1432-1327.1998.2570142.x