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The control of NAD specific malic enzyme from cauliflower bud mitochondria by metabolites

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Summary

NAD malic enzyme (EC. 1.1.1.39) has been purified from cauliflower (Brassica oleracea. var. botrytis) bud mitochondria. The enzyme exhibits complex regulatory properties being activated by a variety of metabolites including glycolytic intermediates, CoA, sulphate and Krebs cycle acids—the tricarboxylic acids with the exception of citrate being more effective than dicarboxylic acids. Fructose diphosphate which is a positive effector of the enzyme increases the affinity of the enzyme for L-malate.

The enzyme is inhibited by glutamate, aspartate, phosphate and ATP, in the latter case the inhibition is largely due to chelation of Mg2+. The plot of rate versus malate concentration is sigmoid at pH 7.0 with Mg2+ but normal Michaelis-Menten kinetics are observed with Mn2+. The molecular weight of the enzyme as measured by gel filtration is ca. 400000. The physiological significance of the responses to metabolites is discussed.

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References

  • Andrews, P.: The gel-filtration behaviour of proteins related to their molecular weights over a wide range. Biochem. J. 96, 595–606 (1965)

    PubMed  Google Scholar 

  • Coleman, J. O. D., Palmer, J. M.: The oxidation of malate by isolated plant mitochondria. Europ. J. Biochem. 26, 499–509 (1972)

    PubMed  Google Scholar 

  • Davies, D. D.: Control of and by pH. Symp. Soc. exp. Biol. 27, 513–529 (1973)

    PubMed  Google Scholar 

  • Davies, D. D., Corbett, R. J.: Glyoxylate decarboxylase activity in higher plants. Phytochem. 8, 529–542 (1969)

    Article  Google Scholar 

  • Davies, D. D., Patil, K. D.: Regulation of ‘Malic’ enzyme of Solanum tuberosum by metabolites. Biochem. J. 137, 45–53 (1974)

    PubMed  Google Scholar 

  • Davies, D. D., Nascimento, K. H., Patil, K. D.: The distribution and properties of NADP ‘malic’ enzyme in flowering plants. Phytochem. 13, 2417–2425 (1974)

    Article  Google Scholar 

  • Frenkel, R.: Bovine heart ‘Malic’ enzyme. Isolation and partial purification of a cyotplasmic and a mitochondrial enzyme. J. biol. Chem. 246, 3069–3074 (1972)

    Google Scholar 

  • Hatch, M. D., Mau, S. L., Kagawa, T.: Properties of leaf NAD malic enzyme from plants with C4 pathway photosynthesis. Arch. Biochem. Biophys. 165, 188–200 (1974)

    PubMed  Google Scholar 

  • Lance, C., Hobson, G. E., Young, R. E., Biale, J. B.: The metabolic processes in cytoplasmic particles of the avocado fruit. IX The oxidation of pyruvate and malate during the climacteric cycle. Plant Physiol. 42, 471–478 (1967)

    PubMed  Google Scholar 

  • Macrae, A. R.: Isolation and properties of a ‘Malic’ enzyme from cauliflower bud mitochondria. Biochem. J. 122, 495–501 (1971a)

    PubMed  Google Scholar 

  • Macrae, A. R.: ‘Malic’ enzyme activity of plant mitochondria. Phytochem. 10, 2343–2347 (1971b)

    Article  Google Scholar 

  • Macrae, A. R., Moorhouse, R.: The oxidation of malate by mitochondria isolated from cauliflower buds. Europ. J. Biochem. 16, 96–102 (1970)

    PubMed  Google Scholar 

  • Nicholls, D. G., Shepherd, D., Garland, P. B.: A continuous recording technique for the measurement of carbondioxide and its application to mitochondrial oxidation and decarboxylation reactions. Biochem. J. 103, 677–691 (1967)

    PubMed  Google Scholar 

  • Rhodes, M. J. C., Wooltorton, L. S. C., Galliard, T., Hulme, A. C.: Metabolic changes in excised fruit tissue—I factors affecting the development of a malate decarboxylation system during the ageing of disks of pre-climacteric apples. Phytochem. 7, 1439–1451 (1968)

    Article  Google Scholar 

  • Sauer, L. A.: Mitochondrial NAD-dependent malic enzyme: a new regulatory enzyme. FEBS Lett. 33(2), 251–255 (1973)

    Article  PubMed  Google Scholar 

  • Shen, L. C., Atkinson, D. E.: Regulation of pyruvate dehydrogenase from Escherichia coli. J. biol. Chem. 245 5974–5978 (1970)

    PubMed  Google Scholar 

  • Ulrich, A. L.: Metabolism of non volatile organic acids in excised barley roots as related to cation-anion balance during salt accumulation. Amer. J. Bot. 28, 526–537 (1941)

    Google Scholar 

  • Warburg, O., Christian, W.: Isolation and crystallisation of enolase. Biochem. Z. 310, 384–421 (1942)

    Google Scholar 

  • Wiskich, J. T., Bonner, W. D.: Preparation and properties of sweet potato mitochondria. Plant Physiol. 38, 594–604 (1963)

    Google Scholar 

Download references

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Authors and Affiliations

  1. School of Biological Sciences, University of East Anglia, NR4 7TJ, Norwich, UK

    D. D. Davies & K. D. Patil

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  1. D. D. Davies
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  2. K. D. Patil
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Davies, D.D., Patil, K.D. The control of NAD specific malic enzyme from cauliflower bud mitochondria by metabolites. Planta 126, 197–211 (1975). https://doi.org/10.1007/BF00388963

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  • DOI: https://doi.org/10.1007/BF00388963

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