Summary
Gel-filtration of glyceraldehyde-3-phosphate dehydrogenase from Anabaena variabilis indicates a mol. wt. of 200,000–300,000, which is significantly greater than previously reported for this enzyme from other sources. Reaction rates in the presence NAD of and NADP suggest that one enzyme only is operative, being active with either coenzyme at any one time. Centrifugation and electrophoretic studies support this conclusion. The possible consequences of these results in the control of intermediary metabolism are discussed.
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Carr, N. G., and G. Exell: Ubiquinone concentrations in Athiorhodaceae grown under various environmental conditions. Biochem. J. 96, 688–692 (1965).
— and M. H. Hallaway: Reduction of phenolindo-2,6-dichlorophenol in dark and light by the blue-green alga Anabaena variabilis. J. gen. Microbiol. 39, 335–344 (1965).
Fuller, R. C., and M. Gibbs: Intracellular and phyllogenetic distribution of ribulose-1,5-diphosphate carboxylase and D-glyceraldehyde-3-phosphate dehydrogenases. Plant Physiol. 34, 324–329 (1959).
—, and G. A. Hudock: Triosephosphate dehydrogenase in plant and microbial photosynthesis. In: Biochemistry of chloroplasts, ed. T. W. Goodwin, vol. 2, p. 181–190. New York: Academic Press 1967.
Gibbs, M.: TPN triosephosphate dehydrogenase from plant tissue. In: Methods in enzymology, ed. S. P. Colowick, and N. O. Kaplan, vol. I, p. 411–415. New York: Academic Press 1955.
Heber, U., N. G. Pon, and M. Heber: Localization of carboxydismutase and triosephosphate dehydrogenases in the chloroplast. Plant Physiol. 38, 355–360 (1963).
Hood, W., and N. G. Carr: A single glyceraldehyde-3-phosphate dehydrogenase active with NAD and NADP in Anabaena variabilis. Biochem. biophys. Acta (Amst.) 146, 309–311 (1967).
Krebs, E. G.: Glyceraldehyde-3-phosphate dehydrogenase from yeast. In: Methods in enzymology, ed. S. P. Colowick, and N. O. Kaplan, vol. 1, p. 407–411. New York: Academic Press 1955.
Layne, E.: Spectrophotometric and turbidimetric methods for measuring proteins. In: Methods in enzymology, ed. S. P. Colowick, and N. O. Kaplan, vol. 3, p. 447–454. New York: Academic Press 1957.
Lebherz, H. G., and W. J. Rutter: Glyceraldehyde-3-phosphate dehydrogenase variants in phyletically diverse organisms. Science 157, 1198–1200 (1967).
Melandri, B. A., A. Baccarini, and P. Pupillo: Glyceraldehyde-3-phosphate dehydrogenase in photosynthetic tissues: Kinetic evidence for competitivity between NAD and NADP. Biochem. biophys. Res. Commun. 33, 160–164 (1968).
Müller, B., I. Ziegler u. H. Ziegler: Die lichtinduzierte, reversible Aktivitätssteigerung der NADP+-abhängigen Glycerinaldehyd-3-phosphat-dehydrogenase in Chloroplasten. X. Zum Mechanismus der Reaktion. Europ. J. Biochem. (in press).
Pearce, J., and N. G. Carr: The metabolism of acetate by the blue-green algae Anabaena variabilis and Anacystis nidulans. J. gen. Microbiol. 49, 301–313 (1967).
Scott, E., and D. S. Burns: Protein-protein interaction. The phycocyanin system. Biochemistry 4, 2597–2606 (1965).
Smillie, R. M., and R. C. Fuller: Further observations on glyceraldehyde-3-phosphate dehydrogenases in plants and photosynthetic bacteria. Biochem. biophys. Res. Commun. 3, 368–372 (1960).
Taylor, J. F.: Specific volumes and molecular weights of D-glyceraldehyde-3-phosphate dehydrogenase and aldolase. Fed. Proc. 9, 237 (1950).
Vernon, L. P., and M. D. Kamen: Studies on the metabolism of photosynthetic bacteria. XV. Photoacetoxidation of ferrocytochrome c in extracts of Rhodospirillum rubrum. Arch. Biochem. 44, 298–311 (1953).
Williams, R. A. D., and E. Bowden: The starch-gel electrophoresis of glucose-6-phosphate dehydrogenase and glyceraldehyde-3-phosphate dehydrogenase of Streptococcus faecalis, S. faecuim and S. durans. J. gen Microbiol. 50, 329–336 (1968).
Ziegler, H., I. Ziegler u. H. J. Schmidt-Clausen: Die lichtinduzierte Aktivitätssteigerung der NADP+-abhängigen Glycerinaldehyd-3-Phosphatdehydrogenase. VIII. Die Abhängigkeit der Enzymaktivität von Bestrahlungsstärke und-dauer bei Lemna. Planta (Berl.) 81, 181–192 (1968).
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Hood, W., Carr, N.G. Association of NAD and NADP linked glyceraldehyde-3-phosphate dehydrogenase in the blue-green alga, Anabaena variabilis . Planta 86, 250–258 (1969). https://doi.org/10.1007/BF00386457
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DOI: https://doi.org/10.1007/BF00386457