Bedoukian   RussellIPM   RussellIPM   Piezoelectric Micro-Sprayer


Home
Animal Taxa
Plant Taxa
Semiochemicals
Floral Compounds
Semiochemical Detail
Semiochemicals & Taxa
Synthesis
Control
Invasive spp.
References

Abstract

Guide

Alphascents
Pherobio
InsectScience
E-Econex
Counterpart-Semiochemicals
Print
Email to a Friend
Kindly Donate for The Pherobase

« Previous AbstractHighly Sensitive Gas-Sensing Films for Volatile Organic Acids from Imidazolium-Based Poly(ionic liquid)s    Next AbstractInterleukin-17-induced neutrophil extracellular traps mediate resistance to checkpoint blockade in pancreatic cancer »

J Insect Sci


Title:Identification and Characterization of Aldehyde Oxidase 5 in the Pheromone Gland of the Silkworm (Lepidoptera: Bombycidae)
Author(s):Zhang Y; Yang Y; Shen G; Mao X; Jiao M; Lin Y;
Address:"State Key Laboratory of Silkworm Genome Biology, Southwest University, Chongqing, China. Biological Science Research Center, Southwest University, Chongqing, China. Chongqing Key Laboratory of Sericulture Science, Chongqing, China. Chongqing Engineering and Technology Research Center for Novel Silk Materials, Chongqing, China"
Journal Title:J Insect Sci
Year:2020
Volume:20
Issue:6
Page Number: -
DOI: 10.1093/jisesa/ieaa132
ISSN/ISBN:1536-2442 (Electronic) 1536-2442 (Linking)
Abstract:"Aldehyde oxidases (AOXs) are a subfamily of cytosolic molybdo-flavoenzymes that play critical roles in the detoxification and degradation of chemicals. Active AOXs, such as AOX1 and AOX2, have been identified and functionally analyzed in insect antennae but are rarely reported in other tissues. This is the first study to isolate and characterize the cDNA that encodes aldehyde oxidase 5 (BmAOX5) in the pheromone gland (PG) of the silkworm, Bombyx mori. The size of BmAOX5 cDNA is 3,741 nucleotides and includes an open reading frame, which encodes a protein of 1,246 amino acid residues. The theoretical molecular weight and isoelectric point of BmAOX5 are approximately 138 kDa and 5.58, respectively. BmAOX5 shares a similar primary structure with BmAOX1 and BmAOX2, containing two [2Fe-2S] redox centers, a FAD-binding domain, and a molybdenum cofactor (MoCo)-binding domain. RT-PCR revealed BmAOX5 to be particularly highly expressed in the PG (including ovipositor) of the female silkworm moth, and the expression was further confirmed by in situ hybridization, AOX activity staining, and anti-BmAOX5 western blotting. Further, BmAOX5 was shown to metabolize aromatic aldehydes, such as benzaldehyde, salicylaldehyde, and vanillic aldehyde, and fatty aldehydes, such as heptaldehyde and propionaldehyde. The maximum reaction rate (Vmax) of benzaldehyde as substrate was 21 mU and Km was 1.745 mmol/liter. These results suggested that BmAOX5 in the PG could metabolize aldehydes in the cytoplasm for detoxification or participate in the degradation of aldehyde pheromone substances and odorant compounds to identify mating partners and locate suitable spawning sites"
Keywords:"*Aldehyde Oxidase/chemistry/genetics/isolation & purification/metabolism Animals Arthropod Antennae/metabolism *Bombyx/genetics/metabolism Genes, Insect Moths/genetics/metabolism Pheromones/*metabolism Scent Glands/*metabolism Bombyx mori activity stainin;"
Notes:"MedlineZhang, Yandi Yang, Yu Shen, Guanwang Mao, Xueqin Jiao, Mengyao Lin, Ying eng 2020/12/10 J Insect Sci. 2020 Nov 1; 20(6):31. doi: 10.1093/jisesa/ieaa132"

 
Back to top
 
Citation: El-Sayed AM 2024. The Pherobase: Database of Pheromones and Semiochemicals. <http://www.pherobase.com>.
© 2003-2024 The Pherobase - Extensive Database of Pheromones and Semiochemicals. Ashraf M. El-Sayed.
Page created on 22-11-2024