Abstract
The degradation of starch by a protein fraction of Kalanchoë daigremontiana Hamet et Perrier, obtained by ammoniumsulfate precipitation (30–70%), was found to be catalyzed by α-and β-amylase (EC 3.2.1.1 and EC 3.2.1.2, respectively) and by starch phosphorylase (EC 2.4.1.1). The activity of these enzymes was determined by chromatographic analysis of the reaction products; separation and identification of α-amylase was accomplished by heat-inactivation of β-amylase and α-glucosidase. When the interaction of amylolytic and phosphorolytic enzymes was comparatively studied, it was found that without inorganic phosphorus in the reaction mixture, 14C-starch was converted predominantly to maltose and glucose; supplementation with 1–10 mM orthophosphate (Pi) resulted in an increase in glucose-1-phosphate formation and a concomitant reduction of maltose production. Since the total volume of starch degradation remained approximately constant, Pi apparently inhibits β-amylase (Ki about 3 mM Pi). Thus, free Pi in the cell participates in the regulation of starch catabolism, serving as a substrate for starch phosphorylase while simultaneously reducing the production of maltose. With respect to glucan synthesis, adenosinediphosphoglucose-α-1,4-glucosyltransferase (EC 2.4.1.22), maltose phosphorylase and maltoseglucosyltransferase were also found to be active. The last-named enzyme catalyzes an exchange between dextrins and is considered to provide primer carbohydrates for the synthesis of polyglucans.
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Abbreviations
- ADPG:
-
adenosinediphosphoglucose
- G1P:
-
glucose-1-phosphate
- PEG:
-
polyethylenglycol
- PEP:
-
phosphoenolpyruvate
- Pi:
-
orthophosphate
References
Aspinall, G.O., Rashbrook, R.B., Kessler, G.: The man of Ivory Nut (Phytelephas macrocarpa). II. The partial acid hydrolysis of mannans A and B. J. Chem. Soc. 215–221 (1958)
Burr, B., Nelson, O.E.: Maize α-glucan phosphorylase. Eur. J. Biochem. 56, 539–546 (1975)
Chen-She, S.H., Lewis, D.H., Walker, D.A.: Stimulation of photosynthetic starch formation by sequestration of cytoplasmic orthophosphate. New Phytol. 74, 383–392 (1975)
Clutterbuck, V.J., Briggs, D.E.: Enzyme formation and release by isolated barley aleurone layers. Phytochemistry 12, 537–546 (1973)
Heldt, H.W., Chon, C.J.A., Maronde, D., Herold, A., Stankovic, Z.S., Walker, D.A., Kraminer, A., Kirk, M.R., Heber, U.: Role of orthophosphate and other factors in the regulation of starch formation in leaves and isolated chloroplasts. Plant Physiol. 59, 1146–1155 (1977)
Jones, G., Whelan, W.J.: The action pattern of D-enzyme, a transmaltodextrinylase from potato. Carbohydr. Res. 9, 483–490 (1969)
Kaiser, W.M., Bassham, J.A.: Light-dark regulation of starch metabolism in chloroplasts. Plant Physiol. 63, 109–113 (1979)
Kluge, M., Ting, I.: Crassulacean Acid Metabolism. Heidelberg, Berlin, New York: Springer 1978
Linden, J.C., Tanner, W., Kandler, O.: Properties of glucosyltransferase and glucantransferase from spinach. Plant Physiol. 54, 752–757 (1974)
Linden, J.C., Schilling, N., Brackenhofer, H., Kandler, O.: Asymmetric labelling of maltose during photosynthesis in 14CO2. Z. Pflanzenphysiol. 76, 176–181 (1975)
Peavey, D.G., Steup, M., Gibbs, M.: Characterization of starch breakdown in the intact spinach chloroplasts. Plant Physiol. 60, 305–308 (1977)
Pongratz, P., Beck, E.: Diurnal oscillation of amylolytic activity in spinach chloroplasts. Plant Physiol. 62, 687–689 (1978)
Preiss, J., Levi, C.: Regulation of α-1,4-glucan metabolism in photosynthetic systems. Proc. IV. Intern. Congr. on Photosynthesis (London 1977), pp. 457–468, Hall, D.O., Coombs, I., Goodwin, T.W., eds. London: Biochem. Soc. 1978
Recondo, E., Leloir, L.F.: Adenosine diphosphate glucose and starch synthesis. Biochem. Biophys. Res. Commun. 6, 85–88 (1961)
Rodaway, S.I., Kende, H.: No effect of 5-fluorouracil on the properties of purified α-amylase from barley half-seeds. Plant Physiol. 61, 1–6 (1978)
Schilling, N., Kandler, O.: α-Glucose-1-phosphate, a precursor in the biosynthesis of maltose in higher plants. Trans. Biochem. Soc. 3, 985–987 (1975)
Steup, M., Peavey, D.G., Gibbs, M.: The regulation of starch metabolism by inorganic phosphate. Biochem. Biophys. Res. Commun. 72, 1554–1561 (1976)
Steup, M., Latzko, E.: Intracellular localization of phosphorylases in spinach and pea leaves. Planta 145, 69–75 (1979)
Sutton, B.G.: Glycolysis in CAM plants. Aust. J. Plant Physiol. 2, 389–402 (1975a)
Sutton, B.G.: Kinetic properties of phosphorylase and phosphofructokinase of Kalanchoë daigremontiana and Atriplex spongiosa. Aust. J. Plant Physiol. 2, 403–411 (1975b)
Thoma, J.A., Spradlin, I.E., Dygert, S.: In: The Enzymes, 3rd edn., pp. 45–189, Boyer, P.D., ed. New York: Academic Press 1971
Ting, I.P., Osmond, C.B.: Activation of plant P-enolpyruvate carboxylases by glucose-6-phosphate: a particular role in Crassulacean acid metabolism. Plant Sci. Lett. 123–128 (1973)
Trevelyan, W.E., Procter, D.P., Harrison, J.S.: Detection of sugars on paper chromatograms. Nature (London) 166, 444–445 (1950)
Vieweg, G.M., de Fekete, M.A.R.: Diurnal fluctuation of amylase activity in Kalanchoë daigremontiana leaves. Z. Pflanzenphysiol. 81, 74–79 (1977)
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Schilling, N., Dittrich, P. Interaction of hydrolytic and phosphorolytic enzymes of starch metabolism in Kalanchoë daigremontiana . Planta 147, 210–215 (1979). https://doi.org/10.1007/BF00388740
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DOI: https://doi.org/10.1007/BF00388740