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Originally published as Genetics Published Articles Ahead of Print on March 23, 2009.
Genetics, Vol. 182, 565-574, June 2009, Copyright © 2009
doi:10.1534/genetics.109.100677
Quantifying Interactions Within the NADP(H) Enzyme Network in Drosophila melanogaster
Thomas J. S. Merritt1, Caitlin Kuczynski, Efe Sezgin2, Chen-Tseh Zhu, Seiji Kumagai3 and Walter F. Eanes
Department of Ecology and Evolution, Stony Brook University, Stony Brook, New York 11794
1 Corresponding author: Department of Chemistry and Biochemistry, Laurentian University, Sudbury, ON P3E 2C6, Canada.
E-mail: tmerritt{at}laurentian.ca
In this report, we use synthetic, activity-variant alleles in Drosophila melanogaster to quantify interactions across the enzyme network that reduces nicotinamide adenine dinucleotide phosphate (NADP) to NADPH. We examine the effects of large-scale variation in isocitrate dehydrogenase (IDH) or glucose-6-phosphate dehydrogenase (G6PD) activity in a single genetic background and of smaller-scale variation in IDH, G6PD, and malic enzyme across 10 different genetic backgrounds. We find significant interactions among all three enzymes in adults; changes in the activity of any one source of a reduced cofactor generally result in changes in the other two, although the magnitude and directionality of change differs depending on the gene and the genetic background. Observed interactions are presumably through cellular mechanisms that maintain a homeostatic balance of NADPH/NADP, and the magnitude of change in response to modification of one source of reduced cofactor likely reflects the relative contribution of that enzyme to the cofactor pool. Our results suggest that malic enzyme makes the largest single contribution to the NADPH pool, consistent with the results from earlier experiments in larval D. melanogaster using naturally occurring alleles. The interactions between all three enzymes indicate functional interdependence and underscore the importance of examining enzymes as components of a network.
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