Gene_locus Report for: bommo-q6u6j0

Bombyx mori (Silk moth) juvenile hormone epoxide hydrolase

the sequence is from the structure: some differences with Q6U6J0

(Below N is a link to NCBI taxonomic web page and E link to ESTHER at designed phylum.)
> cellular organisms: N E > Eukaryota: N E > Opisthokonta: N E > Metazoa: N E > Eumetazoa: N E > Bilateria: N E > Protostomia: N E > Ecdysozoa: N E > Panarthropoda: N E > Arthropoda: N E > Mandibulata: N E > Pancrustacea: N E > Hexapoda: N E > Insecta: N E > Dicondylia: N E > Pterygota: N E > Neoptera: N E > Holometabola: N E > Amphiesmenoptera: N E > Lepidoptera: N E > Glossata: N E > Neolepidoptera: N E > Heteroneura: N E > Ditrysia: N E > Obtectomera: N E > Bombycoidea: N E > Bombycidae: N E > Bombycinae: N E > Bombyx: N E > Bombyx mori: N E

Title: Crystal structure of juvenile hormone epoxide hydrolase from the silkworm Bombyx mori
Zhou K, Jia N, Hu C, Jiang YL, Yang JP, Chen Y, Li S, Li WF, Zhou CZ
Ref: Proteins, 82:3224, 2014 : PubMed
Abstract


ESTHER: Zhou_2014_Proteins_82_3224
PubMedSearch: Zhou 2014 Proteins 82 3224
PubMedID: 25143157
Gene_locus related to this paper: bommo-q6u6j0

Abstract

The juvenile hormone (JH) epoxide hydrolase (JHEH) catalyzes the degradation of JH, which regulates the metamorphosis development of insects. Here we report the 2.30 A crystal structure of JHEH from the silkworm Bombyx mori (BmJHEH). The overall structure of BmJHEH is composed of an N-terminal segment followed by a core hydrolase domain, which is interrupted by an all-alpha lid domain. Structural analyses together with molecular simulation reveal insights into the conservation and specificity of the active-site pocket. These findings increase our understanding of the substrate recognition and catalysis of microsomal epoxide hydrolase family and might help the design of JH-derived pesticides. (c) Proteins 2014;. (c) 2014 Wiley Periodicals, Inc.



        

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


ESTHER: Zhang_2005_Insect.Biochem.Mol.Biol_35_153
PubMedSearch: Zhang 2005 Insect.Biochem.Mol.Biol 35 153
PubMedID: 15681225
Gene_locus related to this paper: bommo-q6u6j0

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.