title: Molecular aspects of carboxylesterase isoforms in comparison with other esterases.
abstract: The involvement of carboxylesterase, acetylcholinesterase, butyrylcholinesterase and cholesterol esterase in pharmacology and toxicology are well recognized. However, there are few papers concerning the comparative studies of these serine hydrolases in terms of molecular level. Recently, we have studied various aspects of carboxylesterases using cDNAs of carboxylesterase isozymes purified from 9 animal species and human liver microsomes, and found that there is high homology of the N-terminal amino acid sequences of the isozymes tested. On the other hand, we compared the amino acid sequences at the active site of the individual esterases and found that the sequences of all esterases tested are strictly conserved. These results strongly suggest that the esterases involved are classified into the serine hydrolase super family.
authors.affiliation: Laboratory of Biochemical Pharmacology and Toxicology, Faculty of Pharmaceutical Sciences, Chiba University, Japan.
authors.forename: T
authors.initials: T
authors.lastname: Satoh
authors.forename: M
authors.initials: M
authors.lastname: Hosokawa
mesh_terms: D000595:Amino Acid Sequence; D000818:Animals; D001483:Base Sequence; D002265:Carboxylic Ester Hydrolases / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism; D004950:Esterases / Q000737:chemistry*; D006801:Humans; D007527:Isoenzymes / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism; D008862:Microsomes, Liver / Q000201:enzymology; D008969:Molecular Sequence Data; D013045:Species Specificity; D013379:Substrate Specificity
chemical_list: D007527:Isoenzymes; D004950:Esterases; D002265:Carboxylic Ester Hydrolases