Title : Cloning and nucleotide sequence of a novel, male-predominant carboxylesterase in mouse liver - Aida_1993_Biochim.Biophys.Acta_1174_72 |
Author(s) : Aida K , Moore R , Negishi M |
Ref : Biochimica & Biophysica Acta , 1174 :72 , 1993 |
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. |
PubMedSearch : Aida_1993_Biochim.Biophys.Acta_1174_72 |
PubMedID: 7916639 |
Gene_locus related to this paper: mouse-Ces3a |
Gene_locus | mouse-Ces3a |
Aida K, Moore R, Negishi M (1993)
Cloning and nucleotide sequence of a novel, male-predominant carboxylesterase in mouse liver
Biochimica & Biophysica Acta
1174 :72
Aida K, Moore R, Negishi M (1993)
Biochimica & Biophysica Acta
1174 :72