The soluble citric acid cycle enzymes ofDrosophila melanogaster. II. Tissue and intracellular distribution of aconitase and NADP-dependent isocitrate dehydrogenase

Fox, David J.; Conscience-Egli, M; Abächerli, Erika

doi:10.1007/bf00486086

Cited by 18 publications

(5 citation statements)

References 19 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…Young female adults were on the average 1.6 times heavier than young males. Similar observations on IDH activity were noted for Drosophita melanogaster 4 .…”

Section: Discussionsupporting

confidence: 85%

Genetic polymorphism, mapping, and characterization of isocitrate dehydrogenase in Anopheles quadrimaculatus

Kim

Narang

Seawright

1987

Journal of Heredity

View full text Add to dashboard Cite

The isocitrate dehydrogenase-2 (Idh-2) locus of Anopheles quadrimaculatus was analyzed genetically and the enzyme was characterized physiochemically. Three-point testcrosses involving chromosome 3 markers showed that in female hybrids the gene sequence and the map distances are: nonstripe (st)--6.8--Idh-2--43.5--short antenna (Sa). Reduced recombination frequencies were observed in male hybrids (st--3.4--Idh-2--25.5--Sa). Idh-2 activity gradually increases during development and reaches a peak intensity in adults. Maximum enzyme activity of Idh-2 was obtained at pH 7.5. One-minute heat treatment at 50 degrees C caused about 50 percent reduction of IDH-2. Ethylene diamine tetraacetic acid (EDTA 5 mM) and p-chloromercuribenzoate (pCMB 10(-5)M) caused complete loss of activity of IDH-2, but pretreatment of the enzyme in situ with mercaptoethanol protected the activity of allozymes from inhibition by pCMB treatment.

show abstract

“…Young female adults were on the average 1.6 times heavier than young males. Similar observations on IDH activity were noted for Drosophita melanogaster 4 .…”

Section: Discussionsupporting

confidence: 85%

Genetic polymorphism, mapping, and characterization of isocitrate dehydrogenase in Anopheles quadrimaculatus

Kim

Narang

Seawright

1987

Journal of Heredity

View full text Add to dashboard Cite

show abstract

“…Examples include the CG3483 and CG7755 genes, both predicted to encode isocitrate dehydrogenase-like proteins. While at least one isocitrate dehydrogenase ( IDH ) is a component of the mitochondrial citric acid cycle, others have a cytoplasmic localization, producing αketoglutarate with a conversion of NADP+ to NADPH [35]. We also found that the mRNA encoding Glutathione Transferase E10 (GstE10), which utilizes the redox regulator glutathione in detoxification reactions, exhibits a translational rhythm (Table S4).…”

Section: Resultsmentioning

confidence: 82%

Translational Profiling of Clock Cells Reveals Circadianly Synchronized Protein Synthesis

et al. 2013

View full text Add to dashboard Cite

show abstract

“…Later, Sdh and aconitase (both TCA cycle enzymes) were shown to carry [4Fe-4S] clusters (Ruzicka and Beinert, 1978 ; Cammack, 1982 ). The Drosophila enzymes are no exception to the rule (Duke, 1968 ; Fox et al, 1972 ; Au and Scheffler, 1994 ; Vincent et al, 2012 ; Esposito et al, 2013 ). Failure to build these Fe-S clusters will inevitably block the TCA cycle, and thereby development and growth (Au and Scheffler, 1994 ; Yan et al, 1997 ; Walker et al, 2006 ; Uhrigshardt et al, 2013 ; Na et al, 2014 ).…”

Section: Fe-s and Moco Enzymesmentioning

confidence: 99%

Iron Sulfur and Molybdenum Cofactor Enzymes Regulate the Drosophila Life Cycle by Controlling Cell Metabolism

2018

View full text Add to dashboard Cite

Iron sulfur (Fe-S) clusters and the molybdenum cofactor (Moco) are present at enzyme sites, where the active metal facilitates electron transfer. Such enzyme systems are soluble in the mitochondrial matrix, cytosol and nucleus, or embedded in the inner mitochondrial membrane, but virtually absent from the cell secretory pathway. They are of ancient evolutionary origin supporting respiration, DNA replication, transcription, translation, the biosynthesis of steroids, heme, catabolism of purines, hydroxylation of xenobiotics, and cellular sulfur metabolism. Here, Fe-S cluster and Moco biosynthesis in Drosophila melanogaster is reviewed and the multiple biochemical and physiological functions of known Fe-S and Moco enzymes are described. We show that RNA interference of Mocs3 disrupts Moco biosynthesis and the circadian clock. Fe-S-dependent mitochondrial respiration is discussed in the context of germ line and somatic development, stem cell differentiation and aging. The subcellular compartmentalization of the Fe-S and Moco assembly machinery components and their connections to iron sensing mechanisms and intermediary metabolism are emphasized. A biochemically active Fe-S core complex of heterologously expressed fly Nfs1, Isd11, IscU, and human frataxin is presented. Based on the recent demonstration that copper displaces the Fe-S cluster of yeast and human ferredoxin, an explanation for why high dietary copper leads to cytoplasmic iron deficiency in flies is proposed. Another proposal that exosomes contribute to the transport of xanthine dehydrogenase from peripheral tissues to the eye pigment cells is put forward, where the Vps16a subunit of the HOPS complex may have a specialized role in concentrating this enzyme within pigment granules. Finally, we formulate a hypothesis that (i) mitochondrial superoxide mobilizes iron from the Fe-S clusters in aconitase and succinate dehydrogenase; (ii) increased iron transiently displaces manganese on superoxide dismutase, which may function as a mitochondrial iron sensor since it is inactivated by iron; (iii) with the Krebs cycle thus disrupted, citrate is exported to the cytosol for fatty acid synthesis, while succinyl-CoA and the iron are used for heme biosynthesis; (iv) as iron is used for heme biosynthesis its concentration in the matrix drops allowing for manganese to reactivate superoxide dismutase and Fe-S cluster biosynthesis to reestablish the Krebs cycle.

show abstract

The soluble citric acid cycle enzymes ofDrosophila melanogaster. II. Tissue and intracellular distribution of aconitase and NADP-dependent isocitrate dehydrogenase

Cited by 18 publications

References 19 publications

Genetic polymorphism, mapping, and characterization of isocitrate dehydrogenase in Anopheles quadrimaculatus

Genetic polymorphism, mapping, and characterization of isocitrate dehydrogenase in Anopheles quadrimaculatus

Translational Profiling of Clock Cells Reveals Circadianly Synchronized Protein Synthesis

Iron Sulfur and Molybdenum Cofactor Enzymes Regulate the Drosophila Life Cycle by Controlling Cell Metabolism

Contact Info

Product

Resources

About