« Previous AbstractDisease and weather induce rapid shifts in a rangeland ecosystem mediated by a keystone species (Cynomys ludovicianus)    Next AbstractEvaluation of solid-phase micro-extraction coupled to gas chromatography-mass spectrometry for the headspace analysis of volatile compounds in cocoa products »

Insect Biochem Mol Biol

Title:		Characterisation of geranylgeranyl diphosphate synthase from the sandfly Lutzomyia longipalpis
Author(s):		Ducker C; French S; Pathak M; Taylor H; Sainter A; Askem W; Dreveny I; Santana AEG; Pickett JA; Oldham NJ;
Address:		"School of Chemistry, University of Nottingham, University Park, Nottingham, NG7 2RD, UK. School of Pharmacy, University of Nottingham, University Park, Nottingham, NG7 2RD, UK. Center of Engineering and Agrarian Science, Federal University of Alagoas, Maceio, Brazil. School of Chemistry, Cardiff University, Main Building, Park Pl, Cardiff, CF10 3AT, UK. School of Chemistry, University of Nottingham, University Park, Nottingham, NG7 2RD, UK. Electronic address: neil.oldham@nottingham.ac.uk"
Journal Title:		Insect Biochem Mol Biol
Year:		2023
Volume:		20230822
Issue:
Page Number:		104001 -
DOI:		10.1016/j.ibmb.2023.104001
ISSN/ISBN:		1879-0240 (Electronic) 0965-1748 (Linking)
Abstract:		"Leishmaniasis is a debilitating and often fatal neglected tropical disease. Males from sub-populations of the Leishmania-harbouring sandfly, Lutzomyia longipalpis, produce the diterpene sex and aggregation pheromone, sobralene, for which geranylgeranyl diphosphate (GGPP) is the likely isoprenoid precursor. We have identified a GGPP synthase (lzGGPPS) from L. longipalpis, which was recombinantly expressed in bacteria and purified for functional and kinetic analysis. In vitro enzymatic assays using LC-MS showed that lzGGPPS is an active enzyme, capable of converting substrates dimethylallyl diphosphate (DMAPP), (E)-geranyl diphosphate (GPP), (E,E)-farnesyl diphosphate (FPP) with co-substrate isopentenyl diphosphate (IPP) into (E,E,E)-GGPP, while (Z,E)-FPP was also accepted with low efficacy. Comparison of metal cofactors for lzGGPPS highlighted Mg(2+) as most efficient, giving increased GGPP output when compared against other divalent metal ions tested. In line with previously characterised GGPPS enzymes, GGPP acted as an inhibitor of lzGGPPS activity. The molecular weight in solution of lzGGPPS was determined to be approximately 221 kDa by analytical SEC, suggesting a hexameric assembly, as seen in the human enzyme, and representing the first assessment of GGPPS quaternary structure in insects"
Keywords:
Notes:		"PublisherDucker, Charles French, Stanley Pathak, Monika Taylor, Harry Sainter, Adam Askem, William Dreveny, Ingrid Santana, Antonio Euzebio Goulart Pickett, John A Oldham, Neil J eng England 2023/08/25 Insect Biochem Mol Biol. 2023 Aug 22; 161:104001. doi: 10.1016/j.ibmb.2023.104001"