Zhang_2005_Insect.Biochem.Mol.Biol_35_153

Reference

Title : Molecular and biochemical characterization of juvenile hormone epoxide hydrolase from the silkworm, Bombyx mori - Zhang_2005_Insect.Biochem.Mol.Biol_35_153
Author(s) : Zhang QR , Xu WH , Chen FS , Li S
Ref : Insect Biochemistry & Molecular Biology , 35 :153 , 2005
Abstract :

One major route of insect juvenile hormone (JH) degradation is epoxide hydration by JH epoxide hydrolase (JHEH). A full-length cDNA (1536 bp) encoding a microsomal JHEH was isolated from the silkworm, Bombyx mori. Bommo-JHEH cDNA contains an open reading frame encoding a 461-amino acid protein (52 kDa), which reveals a high degree of similarity to the previously reported insect JHEHs. The residues Tyr298, Tyr373, and the HGWP motif corresponding to the oxyanion hole of JHEHs and the residues Asp227, His430, and Glu403 in the catalytic triad are well conserved in Bommo-JHEH. Bommo-JHEH was highly expressed in the fat body, where its mRNA expression pattern was in contrast to the pattern of hemolymph levels of JH during the larval development, suggesting that Bommo-JHEH plays an important role in JH degradation. Recombinant Bommo-JHEH (52 kDa) expressed in Sf9 insect cells was membrane-bound and had a high level of enzyme activity (300-fold over the control activity). This Bommo-JHEH study provides a better understanding of how JH levels are regulated in the domesticated silkworm.

PubMedSearch : Zhang_2005_Insect.Biochem.Mol.Biol_35_153
PubMedID: 15681225
Gene_locus related to this paper: bommo-q6u6j0

Related information

Gene_locus bommo-q6u6j0

Citations formats

Zhang QR, Xu WH, Chen FS, Li S (2005)
Molecular and biochemical characterization of juvenile hormone epoxide hydrolase from the silkworm, Bombyx mori
Insect Biochemistry & Molecular Biology 35 :153

Zhang QR, Xu WH, Chen FS, Li S (2005)
Insect Biochemistry & Molecular Biology 35 :153