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Published March 31, 2015 | Version v1
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Allosteric substrate inhibition of Arabidopsis NAD-dependent malic enzyme 1 is released by fumarate

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Tronconi, Marcos Ariel, Wheeler, Mariel Claudia Gerrard, Martinatto, Andrea, Zubimendi, Juan Pablo, Andreo, Carlos Santiago, Drincovich, María Fabiana (2015): Allosteric substrate inhibition of Arabidopsis NAD-dependent malic enzyme 1 is released by fumarate. Phytochemistry 111: 37-47, DOI: 10.1016/j.phytochem.2014.11.009, URL: http://dx.doi.org/10.1016/j.phytochem.2014.11.009

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urn:lsid:plazi.org:pub:D8457224FFB9FFB4D6563D460F2EFFDC

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Figure: 10.5281/zenodo.10487827 (DOI)
Figure: 10.5281/zenodo.10487830 (DOI)
Figure: 10.5281/zenodo.10487832 (DOI)
Figure: 10.5281/zenodo.10487834 (DOI)
Figure: 10.5281/zenodo.10487838 (DOI)
Figure: 10.5281/zenodo.10487840 (DOI)

References

  • Araujo, W.L, Nunes-Nesi, A., Fernie, A.R., 2011. Fumarate: multiple functions of a simple metabolite. Phytochemistry 72, 838-843.
  • Arias, C.L., Andreo, C.S., Drincovich, M.F., Gerrard Wheeler, M.C., 2013. Fumarate and cytosolic pH as modulators of the synthesis or consumption of C4 organic acids through NADP-malic enzyme in Arabidopsis thaliana. Plant Mol. Biol. 81, 297- 307.
  • Backhausen, J.E., Kitzmann, C., Scheibe, R., 1994. Competition between electron acceptors in photosynthesis: regulation of the malate valve during CO2 fixation and nitrite reduction. Photosynth. Res. 42, 75-86.
  • Carrari, F., Baxter, C., Usadel, B., Urbanczyk-Wochniak, E., Zanor, M.I., Nunes-Nesi, A., Nikiforova, V., Centero, D., Ratzka, A., Pauly, M., Sweetlove, L.J., Fernie, A.R., 2006. Integrated analysis of metabolite and transcript levels reveals the metabolic shifts that underlie tomato fruit development and highlight regulatory aspects of metabolic network behavior. Plant Physiol. 142, 1380- 1396.
  • Centeno, D.C., Osorio, S., Nunes-Nesi, A., Bertolo, A.L.F., Carneiro, R.T., Araujo, W.L., Steinhauser, M.C., Michalska, J., Rohrmann, J., Geigenberger, P., Oliver, S.N., Stitt, M., Carrari, F., Rose, J.K.C., Fernie, A.R., 2011. Malate plays a crucial role in starch metabolism, ripening, and soluble solid content of tomato fruit and affects postharvest softening. Plant Cell 23, 162-184.
  • Chia, D.W., Yoder, T.J., Reiter, W.D., Gibson, S.I., 2000. Fumaric acid: an overlooked form of fixed carbon in Arabidopsis and other plant species. Planta 211, 743- 751.
  • Daily, M. D, Gray, J. J, 2009. Allosteric communication occurs via networks of tertiary and quaternary motions in proteins. PLoS Comput Biol. 5, e1000293.
  • Daily, M.D., Gray, J.J., 2007. Local motions in a benchmark of allosteric proteins. Proteins 67, 385-399.
  • Fernie, A.R., Martinoia, E., 2009. Malate. Jack of all trades or master of a few? Phytochemistry 70, 828-832.
  • Gerrard Wheeler, M.C., Arias, C.L., Tronconi, M.A., Maurino, V.G., Andreo, C.S., Drincovich, M.F., 2008. Arabidopsis thaliana NADP-malic enzyme isoforms: high degree of identity but clearly distinct properties. Plant Mol. Biol. 67, 231-242.
  • Gibon, Y., Blaesing, O.E., Hannemann, J., Carillo, P., Hohne, M., Hendriks, J.H.M., Palacios, N., Cross, J., Selbig, J., Stitt, M., 2004. A robot-based platform to measure multiple enzyme activities in Arabidopsis using a set of cycling assays: comparison of changes of enzyme activities and transcript levels during diurnal cycles and in prolonged darkness. Plant Cell 16, 3304-3325.
  • Hanning, I., Heldt, H.W., 1993. On the function of mitochondrial metabolism during photosynthesis in spinach (Spinacia oleracea L.) leaves. Partitioning between respiration and export of redox equivalents and precursors for nitrate assimilation products.. Plant Physiol. 103, 1147-1154.
  • Hays, M.D., Ryan, D.K., Pennell S., 2004. A modified multisite Stern-Volmer equation for the determination of conditional stability constants and ligand concentrations of soil fulvic acid with metal ions. Anal. Chem. 76, 848-854.
  • Jiang, P., Du, W., Mancuso, A., Wellen, K.E., Yang, X., 2013. Reciprocal regulation of p53 and malic enzymes modulates metabolism and senescence. Nature 493, 689-693.
  • Karsten, W.E., Pais, J.E., Rao, G.S.J., Harris, B.G., Cook, P.F., 2003. Ascaris suum NADmalic enzyme is activated by malate and fumarate binding to separate allosteric sites. Biochemistry 42, 9712-9721.
  • Kummel, A., Panke, S., Heinemann, M., 2006. Systematic assignment of thermodynamic constraints in metabolic network models. BMC Bioinformatics 23, 512.
  • Laemmli, U.K., 1970. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227, 680-685.
  • Lehrer, S.S., Leavis, P.C., 1978. Solute quenching of protein fluorescence. Methods Enzymol. 49, 222-236.
  • Lee, C.P., Eubel, H., Millar, A.H., 2010. Diurnal changes in mitochondrial function reveal daily optimization of light and dark respiratory metabolism in Arabidopsis. Mol. Cell Proteomics 9, 2125-2139.
  • Mallick, S., Harris, B.G., Cook, P.F., 1991. Kinetic mechanism of NAD: malic enzyme from Ascaris suum in the direction of reductive carboxylation. J. Biol. Chem. 266, 2732-2738.
  • Mikaelian, I., Sergeant, A., 1992. A general and fast method to generate multiple site directed mutations. Nucleic Acids Res. 20, 376.
  • Moreadith, R.W., Lehninger, A.L., 1984. Purification, kinetic behavior, and regulation of NAD(P)1 malic enzyme of tumor mitochondria. J. Biol. Chem. 259, 6222- 6227.
  • Padmasree, K., Padmavathi, L, Raghavendra, A.S., 2002. Essentiality of mitochondrial oxidative metabolism for photosynthesis: optimization of carbon assimilation and protection against photoinhibition. Crit. Rev. Biochem. Mol. Biol. 37 (2), 71- 119.
  • Pracharoenwattana, I., Zhou, W.X., Keech, O., Francisco, P.B., Udomchalothorn, T., Tschoep, H., Stitt, M., Gibon, Y., Smith, S.M., 2010. Arabidopsis has a cytosolic fumarase required for the massive allocation of photosynthate into fumaric acid and for rapid plant growth on high nitrogen. Plant J. 62, 785-795.
  • Rao, G.S.J., Coleman, D.E., Karsten, W.E., Cook, P.F., Harris, B.G., 2003. Crystallographic studies on Ascaris suum NAD-malic enzyme bound to reduced cofactor and identification of an effector site. J. Biol. Chem. 278, 38051-38058.
  • Steinhauser, M.C., Steinhauser, D., Koehl, K., Carrari, F., Gibon, Y., Fernie, A.R., Stitt, M., 2010. Enzyme activity profiles during fruit development in tomato cultivars and Solanum pennellii. Plant Physiol. 153, 80-98.
  • Sweetlove, L.J., Beard, K.F.M., Nunes-Nesi, A., Fernie, A.R., Ratcliffe, R.G., 2010. Not just a circle: flux modes in the plant TCA cycle. Trends Plant Sci. 15, 462-470.
  • Tronconi, M.A., Gerrard Wheeler, M.C., Drincovich, M.F., Andreo, C.S., 2012. Differential fumarate binding to Arabidopsis NAD+ malic enzymes 1 and -2 produces an opposite activity modulation. Biochimie 94, 1421-1430.
  • Tronconi, M.A., Gerrard Wheeler, M.C., Maurino, V.G., Drincovich, M.F., Andreo, C.S., 2010a. NAD-malic enzymes of Arabidopsis thaliana display distinct kinetic mechanisms that support differences in physiological control. Biochem. J. 430, 295-303.
  • Tronconi, M.A., Maurino, V.G., Andreo, C.S., Drincovich, M.F., 2010b. Three different and tissue-specific NAD-malic enzyme generated by alternative subunit association in Arabidopsis thaliana. J. Biol. Chem. 285, 11870-11879.
  • Tronconi, M.A., Fahnenstich, H., Gerrard Wheeler, M.C., Andreo, C.S., Flugge, U.I., Drincovich, M.F., Maurino, V.G., 2008. Arabidopsis NAD-malic enzyme functions as a homodimer and heterodimer and has a major impact during nocturnal metabolism. Plant Physiol. 146, 1540-1552.
  • Willeford, K.O., Wedding, R.T., 1987. Evidence for a multiple subunit composition of plant NAD malic enzyme. J. Biol. Chem. 262, 8423-8429.
  • Yang, Z., Lanks, C.W., Tong, L., 2002. Molecular mechanism for the regulation of human mitochondrial NAD(P)+ dependent malic enzyme by ATP and fumarate. Structure 10, 951-960.