(Below N is a link to NCBI taxonomic web page and E link to ESTHER at designed phylum.) > cellular organisms: NE > Eukaryota: NE > Opisthokonta: NE > Metazoa: NE > Eumetazoa: NE > Bilateria: NE > Protostomia: NE > Ecdysozoa: NE > Panarthropoda: NE > Arthropoda: NE > Mandibulata: NE > Pancrustacea: NE > Hexapoda: NE > Insecta: NE > Dicondylia: NE > Pterygota: NE > Neoptera: NE > Holometabola: NE > Amphiesmenoptera: NE > Lepidoptera: NE > Glossata: NE > Neolepidoptera: NE > Heteroneura: NE > Ditrysia: NE > Obtectomera: NE > Bombycoidea: NE > Saturniidae: NE > Saturniinae: NE > Saturniini: NE > Antheraea: NE > Antheraea polyphemus: NE
LegendThis sequence has been compared to family alignement (MSA) red => minority aminoacid blue => majority aminoacid color intensity => conservation rate title => sequence position(MSA position)aminoacid rate Catalytic site Catalytic site in the MSA MFYKLLFCLCIVAAHAGEQDTSKTADCKTHKDEVPIATSQSGVFRGSWMT TRRGRRFQAYRGIRYAEPPVGELRFQPPKPILYYKDVVDASKEGPACPLP VPDDYYVDEDCLAINVYTPNNKVKKPLPVIMYIHPGAFYAFTGRSDVAGP GYLLDRDIVFVAFNYRLATLGFMSTGDKLAPGNNGMKDQVMAMRWVQRNI AAFGGDPNSVTLAGYSAGSISVMLHMISPMSKGLFHRGISMSASPINKEP LPNNFQSLAVKQAQIVNCSTASNQAIVDCLKTISWKVLGDSLPQFFVGGD PIGLWGPVVENDFGQERFLDIQPLDAIRQGRFHSVPHIISQTKYEFFYQV FELFKNDTLITRMNDDWETAARVSFLLPEKNIRAAANKLKEVYLEGKPVA KDNRTIQGVGGLYRDSITSLGVHRMANLMCRHSKHPVYYYEFSYFGDNSH YEDPVTGKPFGAVHHDDLIYLLTMSYRFPVIETTSPHSYVIDEMTALWYN FARYDDPNPRGDTPELNSLVWPVMKPDDRKYLRIGNKLTVHKNMFEDRYK VWDELYPIQY
References
Title: Cloning of putative odorant-degrading enzyme and integumental esterase cDNAs from the wild silkmoth, Antheraea polyphemus Ishida Y, Leal WS Ref: Insect Biochemistry & Molecular Biology, 32:1775, 2002 : PubMed
Odorant-degrading enzymes have been postulated to participate in the fast deactivation of insect pheromones. These proteins are expressed specifically in the sensillar lymph of insect antennae in such low amounts that, hitherto, isolation and protein-based cDNA cloning has not been possible. Using degenerate primers based on conserved amino acid sequences of insect carboxylesterases and juvenile hormone esterases, we were able to amplify partial cDNA fragments, which were then used for the design of gene-specific primers for RACE. This bioinformatics approach led us to the cloning of cDNAs, encoding a putative odorant-degrading enzyme (Apol-ODE) and a putative integumental esterase (Apol-IE) from the wild silkmoth, Antheraea polyphemus. Apol-ODE had a predicted molecular mass of 59,994 Da, pI of 6.63, three potential N-glycosylation sites, and a putative catalytic site Ser characterized by the sequence Gly(195)-Glu-Ser-Ala-Gly-Ala. Apol-IE gave calculated molecular mass of 61,694 Da, pI of 7.49, two potential N-glycosylation sites, and a putative active site with the sequence Gly(214)-Tyr-Ser-Ala-Gly. The transcript of Apol-ODE was detected by RT-PCR in male antennae and branches (sensillar tissues), but not in female antennae and other control tissues. Apol-IE was detected in male and female antennae as well as legs.
Title: Pheromone binding and inactivation by moth antennae Vogt RG, Riddiford LM Ref: Nature, 293:161, 1981 : PubMed
The antennae of male silk moths are extremely sensitive to the female sex pheromone such that a male moth can find a female up to 4.5 km away. This remarkable sensitivity is due to both the morphological and biochemical design of these antennae. Along the branches of the plumose antennae are the sensilla trichodea, each consisting of a hollow cuticular hair containing two unbranched dendrites bathed in a fluid, the receptor lymph ,3. The dendrites and receptor lymph are isolated from the haemolymph by a barrier of epidermal cells which secreted the cuticular hair. Pheromone molecules are thought to diffuse down 100 A-wide pore tubules through the cuticular wall and across the receptor lymph space to receptors located in the dendritic membrane. To prevent the accumulation of residual stimulant and hence sensory adaptation, the pheromone molecules are subsequently inactivated in an apparent two-step process of rapid 'early inactivation' followed by much slower enzymatic degradation. The biochemistry involved in this sequence of events is largely unknown. We report here the identification of three proteins which interact with the pheromone of the wild silk moth Antheraea polyphemus: a pheromone-binding protein and a pheromone-degrading esterase, both uniquely located in the pheromone-sensitive sensilla; and a second esterase common to all cuticular tissues except the sensilla.
