K. Aida et al., CLONING AND NUCLEOTIDE-SEQUENCE OF A NOVEL, MALE-PREDOMINANT CARBOXYLESTERASE IN MOUSE-LIVER, Biochimica et biophysica acta, 1174(1), 1993, pp. 72-74
As a family of serine-dependent enzymes, the carboxylesterases (EC 3.1
.1.1) demonstrate a broad substrate specificity. Mouse carboxylesteras
es comprise at least 20 genetically distinct loci. We cloned a full-le
ngth cDNA for a novel mouse carboxylesterase, Es-male which was expres
sed predominantly in,male livers. This carboxylesterase consisted of 5
54 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 mi
crosomal carboxylesterase.