Cloning and nucleotide sequence of a novel, male-predominant carboxylesterase in mouse liver

Abstract

As a family of serine-dependent enzymes, the carboxylesterases (EC 3.1.1.1) demonstrate a broad substrate specificity. Mouse carboxylesterases comprise at least 20 genetically distinct loci. We cloned a full-length cDNA for a novel mouse carboxylesterase, Es-male which was expressed predominantly in male livers. This carboxylesterase consisted of 554 amino acid residues, and exhibited 43% and 42% similarities to the known mouse esterases Es-22 and pEs-N, respectively. Es-male contained a C-terminal ER-retention signal PEEL, indicating that it may be a microsomal carboxylesterase.