Abstract
Lemna aldolase has been purified by ion-exchange and affinity chromatography. The enzyme is inhibited by pyridoxal phosphate in a manner which suggests that pyridoxal phosphate forms a non-covalent complex with the enzymes which is in equilibrium with the Schiff base covalently modified enzyme. The kinetics of the reversal of inhibition have been used to test the proposition that the fall in aldolase activity observed during periods of nitrogen starvation is due to inhibition by pyridoxal phosphate. It is concluded that the in vivo loss of aldolase activity is not due to pyridoxal phosphate and that the in vitro inhibition of glycolytic enzymes by pyridoxal phosphate is due to the reaction with lysine residues at the active sites which are necessary to bind the strongly acidic sugar phosphates.
This is a preview of subscription content, log in via an institution to check access.
Similar content being viewed by others
References
Anderson, L.E., Pacold, I.: Chloroplast and cytoplasmic enzymes IV. Pea leaf fructose 1,6-diphosphate aldolases. Plant Physiol. 49, 393–397 (1972)
Anderson, L.E., Heinrikron, R.L., Noyes, L.: Chloroplast and cytoplasmic enzymes. Subunit structure of pea leaf aldolases. Arch. Bioch. Biophys. 169, 262–268 (1975)
Beechey, R.B., Happold, F.C.: Pyridoxamine phosphate transaminases. Biochem. J. 66, 520–527 (1957)
Brooks, K., Criddle, R.S.: Enzymes of the carbon cycle of photosynthesis I. Isolation and properties of spinach leaf aldolase. Arch. Bioch. Biophys. 117, 650–659 (1966)
Cheng, S.S., Engel, P.C.: The equilibrium position of the reaction of bovine liver glutamate dehydrogenase with pyridoxal 5′-phosphate. Biochem. J. 147, 351–358 (1975)
Davies, D.D.: Metabolic control in higher plants. In: Biosynthesis and its control in plants, Miborrow, B. V. ed. Phytochem. Soc. Symp. No. 9, pl-20 1973
Domeschke, W., Domagk, G.F.: Protein structure and enzyme activity III. Inhibition of glucose-6-phosphate dehydrogenase and other enzymes involved in sugar metabolism by pyridoxal 5′-phosphate. Hoppe-Seylers Z. Physiol. Chem. 350, 1111–1116 (1969)
Glazer, R.L., Weber, G.: Pyridoxal 5′-phosphate inhibition of lactate production in rat liver supernatant fluid. Biochim. Biophys. Acta 237, 11–13 (1871)
Humphrey, T.J., Sarawek, S., Davies, D.D.: The effect of nitrogen deficiency on the growth and metabolism of Lemna minor L. Planta 137, 259–264 (1977)
Lebherg, H.G.: Synthesis and degradation of fructose diphosphate aldolase isoenzymes in avian brain. J. Biol. Chem. 250, 5967–5975 (1975)
Penhoet, E.E., Kochman, M., Rutter, W.J.: Isolation of fructose diphosphate aldolases A, B and C. Biochemistry 8, 4391–4396 (1969)
Piszkiewicz, D., Smith, E.L.: Bovine liver glutamate dehydrogenase. Equilibria and kinetics of imine formation by lysine-97 with pyridoxal 5′-phosphate. Biochemistry 10, 4544–4552 (1971)
Reshef, L., Heller, M.: Inactivation and protection of fructose diphosphate aldolase in rat adipose tissue extracts. J. Biol. Chem. 244, 766–770 (1969)
Shapiro, S., Enser, M., Pugh, E., Horecker, B.L.: The effect of pyridoxal phosphate on muscle aldolase. Arch. Biochem. Biophys. 128, 554–562 (1968)
Teixeira, A.R.N., Davies, D.D.: The control of plant glutamate dehydrogenase by pyridoxal 5′-phosphate. Phytochemistry 13, 2071–2080 (1974)
Trewavas, A.: The turnover of nucleic acids in Lemna minor. Plant Physiol. 45, 742–751 (1970)
Warburg, O., Christian, W.: Isolierung und Kristallisation des Gärungsferments Enolase. Biochem. Z. 310, 384–393 (1942)
Author information
Authors and Affiliations
Rights and permissions
About this article
Cite this article
Sarawek, S., Davies, D.D. The effect of pyridoxal phosphate on the activity of aldolase from Lemna minor L.. Planta 137, 265–270 (1977). https://doi.org/10.1007/BF00388161
Received:
Accepted:
Issue Date:
DOI: https://doi.org/10.1007/BF00388161