Cloning and nucleotide sequence of a novel, male-predominant carboxylesterase in mouse liver.
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.
Aida
K
K
Pharmacogenetics Section, National Institute of Environmental Health Sciences, National Institutes of Health, Research Triangle Park, NC 27709.
Moore
R
R
Negishi
M
M
D000595:Amino Acid Sequence; D000818:Animals; D001483:Base Sequence; D002265:Carboxylic Ester Hydrolases / Q000096:biosynthesis / Q000235:genetics*; D003001:Cloning, Molecular; D008099:Liver / Q000201:enzymology*; D008297:Male; D051379:Mice; D008807:Mice, Inbred BALB C; D008811:Mice, Inbred DBA; D008969:Molecular Sequence Data; D012737:Sex Factors
D002265:Carboxylic Ester Hydrolases