Substrate Specificity of Carboxylesterase Isozymes and Their Contribution to Hydrolase Activity in Human Liver and Small Intestine

• Published in: Drug metabolism and disposition Vol. 34; no. 10; pp. 1734 - 1741
• Main Authors: Imai, Teruko, Taketani, Megumi, Shii, Mayumi, Hosokawa, Masakiyo, Chiba, Kan
• Format: Journal Article
• Language: English
• Published: Bethesda, MD Elsevier Inc 01.10.2006; American Society for Pharmacology and Experimental Therapeutics
• Subjects: Animals; Benzoates - chemistry; Benzoates - metabolism; Biological and medical sciences; Carboxylesterase - genetics; Carboxylesterase - metabolism; Carboxylic Ester Hydrolases - genetics; Carboxylic Ester Hydrolases - metabolism; Cell Line; Flurbiprofen - chemistry; Flurbiprofen - metabolism; Humans; Hydrolases - metabolism; Hydrolysis; Intestine, Small - enzymology; Intestine, Small - metabolism; Isoenzymes - genetics; Isoenzymes - metabolism; Liver - enzymology; Liver - metabolism; Medical sciences; Microsomes - enzymology; Microsomes - metabolism; Microsomes, Liver - enzymology; Microsomes, Liver - metabolism; Molecular Structure; Pharmacology. Drug treatments; Propranolol - chemistry; Propranolol - metabolism; Substrate Specificity; Human; Digestive system; Enzyme; Isozyme; Liver; Substrate specificity; Hydrolases; Esterases; Carboxylesterase; Small intestine; Biological activity; Carboxylic ester hydrolases

Hydrolase activity from human liver and small intestine microsomes was compared with that of recombinant human carboxylesterases, hCE-1 and hCE-2. Although both hCE-1 and hCE-2 are present in human liver, the dominant component was found to be hCE-1, whereas the hydrolase activity of the human small...