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Gene Review

Men  -  Malic enzyme

Drosophila melanogaster

Synonyms: CG10120, Dmel\CG10120, MDH, ME, MEN, ...
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High impact information on Men


Biological context of Men

  • By using mutation in the Men gene and deficiencies uncovering this locus, we could show that the ME activity recovered in cytosolic fractions originates exclusively from the Men gene located at map position 87D-1 on the right arm of the 3rd chromosome [6].
  • A number of null alleles have been recovered; heterozygotes for these nulls and a Men deficiency are both viable and fertile [7].
  • The genetic and cytogenetic locations of the structural gene (Men) for malic enzyme have been determined [7].
  • The occurrence of crossing over in Drosophila imeretensis males, as well as the tetrameric structure of malic enzyme, was confirmed [8].
  • During the early through middle period of the last larval instar, when ecdysone levels are low, MDH responded to JH rapidly by increasing activity, while little or no response was measured in mature larvae (postfeeding stage) and fresh pupae when the endogenous pulse of ecdysone is high [9].

Anatomical context of Men


Associations of Men with chemical compounds

  • The Drosophila malate dehydrogenase, or malic enzyme (ME) encoded by the Men gene, is a non-mitochondrial enzyme recovered in the cytosolic fraction [6].
  • In addition, high/low sucrose diet fed to wild types or mutants affected the activity of larval MDH, but the enzyme remained sensitive to administration of JH [9].
  • The activity of Drosophila cytosolic malate dehydrogenase (MDH; EC, a key enzyme in the biosynthesis of lipids, was found to be regulated by both the sesquiterpenoid juvenile hormone (JH), and the steroid hormone ecdysone [9].
  • 2. The allozyme forms (MDH A, MDH B, MDH C) were indistinguishable in terms of NAD and L-malate optima, while they are distinguishable in terms of NADH and OAA saturation conditions [11].

Other interactions of Men


  1. Correlations between development rates, enzyme activities, ribosomal DNA spacer-length phenotypes, and adaptation in Drosophila melanogaster. Cluster, P.D., Marinković, D., Allard, R.W., Ayala, F.J. Proc. Natl. Acad. Sci. U.S.A. (1987) [Pubmed]
  2. Biochemical analyses of natural and induced null variants of Drosophila enzymes. Lee, C.Y., Charles, D., Bronson, D. J. Biol. Chem. (1979) [Pubmed]
  3. Drosophila alcohol dehydrogenase polymorphism and carbon-13 fluxes: opportunities for epistasis and natural selection. Freriksen, A., de Ruiter, B.L., Scharloo, W., Heinstra, P.W. Genetics (1994) [Pubmed]
  4. Dosage compensation in Drosophila: NADP-enzyme activities and cross-reacting material. Williamson, J.H., Bentley, M.M. Genetics (1983) [Pubmed]
  5. The involvement of catalase in alcohol metabolism in Drosophila melanogaster larvae. van der Zel, A., Dadoo, R., Geer, B.W., Heinstra, P.W. Arch. Biochem. Biophys. (1991) [Pubmed]
  6. Regulation of cytosolic malate dehydrogenase by juvenile hormone in Drosophila melanogaster. Farkas, R., Danis, P., Medved'ová, L., Mechler, B.M., Knopp, J. Cell Biochem. Biophys. (2002) [Pubmed]
  7. Genetic and cytogenetic studies of malic enzyme in Drosophila melanogaster. Voelker, R.A., Ohnishi, S., Langley, C.H., Gausz, J., Gyurkovics, H. Biochem. Genet. (1981) [Pubmed]
  8. Localization of genes coding for biochemical traits on the second chromosome of Drosophila imeretensis Sokolov (D. littoralis Meigen). Gontcharenko, G.G., Mitrofanov, V.G., Korochkin, L.I. Biochem. Genet. (1985) [Pubmed]
  9. Genetic and hormonal control of cytosolic malate dehydrogenase activity in Drosophila melanogaster. Farkas, R., Knopp, J. Gen. Physiol. Biophys. (1998) [Pubmed]
  10. Ontogeny, cell distribution, and the physiological role of NADP-malic enxyme in Drosophila melanogaster. Geer, B.W., Krochko, D., Williamson, J.H. Biochem. Genet. (1979) [Pubmed]
  11. Biochemical studies of supernatant malate dehydrogenase allozymes in Drosophila melanogaster. Alahiotis, S. Comp. Biochem. Physiol., B (1979) [Pubmed]
  12. The isolation and characterization of mutant alleles at a new X-linked locus, mex, affecting NADP(+)-dependent enzymes in Drosophila melanogaster. Gromnicki, A.R., Bentley, M.M. Biochem. Genet. (1991) [Pubmed]
  13. Characterization of a low-activity allele of NADP+-dependent isocitrate dehydrogenase from Drosophila melanogaster. Bentley, M.M., Meidinger, R.G., Williamson, J.H. Biochem. Genet. (1983) [Pubmed]
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