A corpora allata farnesyl diphosphate synthase in mosquitoes displaying a metal ion dependent substrate specificity |
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| Institution: | 1. Laboratório de Biologia Molecular de Artrópodes-LBMA-IB-RC-UNESP (Univ Estadual Paulista), Av. 24-A, n° 1515, CEP 13506-900, Bela Vista, Rio Claro, SP, Brazil;2. Centro de Biociências, Universidade Federal do Rio Grande do Norte, Av. Sen. Salgado Filho, 3000, CEP 59072-970, Candelária, Natal, RN, Brazil;3. Laboratório de Imunologia e Alergia Experimental-LIAE, Departamento de Clínica Médica, Faculdade de Ciências Médicas, FCM, Universidade Estadual de Campinas-UNICAMP, Rua Tessália Vieira de Camargo n° 126, Cidade Universitária “Zeferino Vaz”, CEP 13083-887 Campinas, SP, Brazil;4. Centro de Estudos de Venenos e Animais Peçonhentos-CEVAP (Univ Estadual Paulista), Rua José Barbosa de Barros, 1780, Fazenda Experimental Lageado, CEP 18610-307 Botucatu, SP, Brazil;1. Institute of Mathematical Sciences, Faculty of Science, University of Malaya, 50603 Kuala Lumpur, Malaysia;2. Department of Physics, Chemistry and Mathematics, Alabama A&M University, Normal, AL 35762-4900, USA;3. Department of Mathematics, King Abdulaziz University, Jeddah 21589, Saudi Arabia;4. Department of Applied Mathematics, National Research Nuclear University, 31 Kashirskoe Hwy, Moscow 115409, Russian Federation;5. School of Mathematics, University of the Witwatersrand, Private Bag 3, Wits 2050, Johannesburg, South Africa;6. Mathematics Department, Faculty of Science, Zagazig University, Zagazig 44519, Egypt;7. Department of Mathematics, Faculty of Science and Arts, Yozgat Bozok University, 66100 Yozgat, Turkey;8. Science Program, Texas A&M University at Qatar, PO Box 23874, Doha, Qatar |
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| Abstract: | Farnesyl diphosphate synthase (FPPS) is a key enzyme in isoprenoid biosynthesis, it catalyzes the head-to-tail condensation of dimethylallyl diphosphate (DMAPP) with two molecules of isopentenyl diphosphate (IPP) to generate farnesyl diphosphate (FPP), a precursor of juvenile hormone (JH). In this study, we functionally characterized an Aedes aegypti FPPS (AaFPPS) expressed in the corpora allata. AaFPPS is the only FPPS gene present in the genome of the yellow fever mosquito, it encodes a 49.6 kDa protein exhibiting all the characteristic conserved sequence domains on prenyltransferases. AaFPPS displays its activity in the presence of metal cofactors; and the product condensation is dependent of the divalent cation. Mg2+ ions lead to the production of FPP, while the presence of Co2+ ions lead to geranyl diphosphate (GPP) production. In the presence of Mg2+ the AaFPPS affinity for allylic substrates is GPP > DMAPP > IPP. These results suggest that AaFPPS displays “catalytic promiscuity”, changing the type and ratio of products released (GPP or FPP) depending on allylic substrate concentrations and the presence of different metal cofactors. This metal ion-dependent regulatory mechanism allows a single enzyme to selectively control the metabolites it produces, thus potentially altering the flow of carbon into separate metabolic pathways. |
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| Keywords: | Farnesyl diphosphate synthase Mosquito Juvenile hormone Prenyltranferases Metal dependence Substrate specificity |
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