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Comp Biochem Physiol B Biochem Mol Biol


Title:Cloning of two carboxylesterase cDNAs from the swimming crab Portunus trituberculatus: Molecular evidences for their putative roles in methyl farnesotae degradation
Author(s):Tao T; Xie X; Liu M; Jiang Q; Zhu D;
Address:"Key laboratory of Applied Marine Biotechnology of Ministry of Education, Ningbo University, 315211 Ningbo, China. Key laboratory of Applied Marine Biotechnology of Ministry of Education, Ningbo University, 315211 Ningbo, China. Electronic address: zhudongfa@nbu.edu.cn"
Journal Title:Comp Biochem Physiol B Biochem Mol Biol
Year:2017
Volume:20161005
Issue:
Page Number:100 - 107
DOI: 10.1016/j.cbpb.2016.10.001
ISSN/ISBN:1879-1107 (Electronic) 1096-4959 (Linking)
Abstract:"The sesquiterpenoid methyl farnesoate (MF) is the unepoxidized form of insect juvenile hormone (JH) III, and is considered an equivalent of JH in crustaceans. Degradation of MF is similar to that of JH which occurs through ester hydrolysis by specific carboxylesterases (CXEs). In this study, the full-length cDNAs of two JH esterase-like CXEs were cloned from the swimming crab, Portunus trituberculatus. The predicted amino acid sequences of the two PtCXEs contain the conserved motifs including catalytic triad and oxyanion hole, which are the hallmark of the CXE family proteins. The phylogenetic analysis showed that the two PtCXEs may belong to the hormone/semiochemical processing group of CXE family, indicating their possible roles on metabolism of hormones. Transcripts of both PtCXEs were most abundant in hepatopancreas and the PtCXE2 was also highly expressed in ovary. The mRNA levels of two PtCXEs in hepatopancreas were induced by in vivo MF treatment and eyestalk ablation, further indicating their potential in degrading MF. However, during the ovarian maturation, expression of the two PtCXEs increased significantly in the early-vitellogenic stage, prior to the remarkable rise in hemolymph MF titer reported by our previous studies. Taken together, our results suggest that the two PtCXEs can potentially serve as the MF esterases, but their catalytic activity may not be restricted to MF"
Keywords:"Ablation Techniques Amino Acid Sequence Animals Brachyura/drug effects/*enzymology/genetics/growth & development Carboxylesterase/chemistry/*genetics/*metabolism Cloning, Molecular DNA, Complementary/*genetics Fatty Acids, Unsaturated/*metabolism/pharmaco;"
Notes:"MedlineTao, Tian Xie, Xi Liu, Mingxin Jiang, Qinghua Zhu, Dongfa eng England 2016/10/30 Comp Biochem Physiol B Biochem Mol Biol. 2017 Jan; 203:100-107. doi: 10.1016/j.cbpb.2016.10.001. Epub 2016 Oct 5"

 
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