Skip to main content
PMC home page
Plant Physiology logoLink to Plant Physiology
. 1978 Mar;61(3):469–471. doi: 10.1104/pp.61.3.469

Light Modulation of the Activity of Carbon Metabolism Enzymes in the Crassulacean Acid Metabolism Plant Kalanchoë 1

Vimal K Gupta 1,2, Louise E Anderson 1,3
PMCID: PMC1091891  PMID: 16660316

Abstract

When intact Kalanchoë plants are illuminated NADP-linked malic dehydrogenase and three enzymes of the reductive pentose phosphate pathway, ribulose-5-phosphate kinase, NADP-linked glyceraldehyde-3-phosphate dehydrogenase, and sedoheptulose-1,7-diphosphate phosphatase, are activated. In crude extracts these enzymes are activated by dithiothreitol treatment. Light or dithiothreitol treatment does not inactivate the oxidative pentose phosphate pathway enzyme glucose-6-phosphate dehydrogenase. Likewise, neither light, in vivo, nor dithiothreitol, in vitro, affects fructose-1,6-diphosphate phosphatase. Apparently the potential for modulation of enzyme activity by the reductively activated light effect mediator system exists in Crassulacean acid metabolism plants, but some enzymes which are light-dark-modulated in the pea plant are not in Kalanchoë.

Full text

PDF
469

Selected References

These references are in PubMed. This may not be the complete list of references from this article.

  1. Anderson L. E. Activation of pea leaf chloroplast sedoheptulose 1,7-diphosphate phosphatase by light and dithiothreitol. Biochem Biophys Res Commun. 1974 Aug 5;59(3):907–913. doi: 10.1016/s0006-291x(74)80065-3. [DOI] [PubMed] [Google Scholar]
  2. Anderson L. E., Advani V. R. Chloroplast and cytoplasmic enzymes: three distinct isoenzymes associated with the reductive pentose phosphate cycle. Plant Physiol. 1970 May;45(5):583–585. doi: 10.1104/pp.45.5.583. [DOI] [PMC free article] [PubMed] [Google Scholar]
  3. Anderson L. E., Avron M. Light Modulation of Enzyme Activity in Chloroplasts: Generation of Membrane-bound Vicinal-Dithiol Groups by Photosynthetic Electron Transport. Plant Physiol. 1976 Feb;57(2):209–213. doi: 10.1104/pp.57.2.209. [DOI] [PMC free article] [PubMed] [Google Scholar]
  4. Anderson L. E., Duggan J. X. Light modulation of glucose-6-phosphate dehydrogenase: partial characterization of the light inactivation system and its effects on the properties of the chloroplastic and cytoplasmic forms of the enzyme. Plant Physiol. 1976 Aug;58(2):135–139. doi: 10.1104/pp.58.2.135. [DOI] [PMC free article] [PubMed] [Google Scholar]
  5. Buchanan B. B., Schürmann P., Kalberer P. P. Ferredoxin-activated fructose diphosphatase of spinach chloroplasts. Resolution of the system, properties of the alkaline fructose diphosphatase component, and physiological significance of the ferredoxin-linked activation. J Biol Chem. 1971 Oct 10;246(19):5952–5959. [PubMed] [Google Scholar]
  6. Johnson H. S. NADP-malate dehydrogenase: photoactivation in leaves of plants with Calvin cycle photosynthesis. Biochem Biophys Res Commun. 1971 May 21;43(4):703–709. doi: 10.1016/0006-291x(71)90672-3. [DOI] [PubMed] [Google Scholar]
  7. Kelly G. J., Zimmermann G., Latzko E. Light induced activation of fructose-1, 6-bisphosphatase in isolated intact chloroplasts. Biochem Biophys Res Commun. 1976 May 3;70(1):193–199. doi: 10.1016/0006-291x(76)91127-x. [DOI] [PubMed] [Google Scholar]
  8. Levi C., Gibbs M. Carbon dioxide fixation in isolated kalanchoe chloroplasts. Plant Physiol. 1975 Jul;56(1):164–166. doi: 10.1104/pp.56.1.164. [DOI] [PMC free article] [PubMed] [Google Scholar]
  9. Viswanathan P. N., Srivastava L. M., Krishnan P. S. Diurnal Variations in Some Enzymes of Carbohydrate Metabolism in Tapioca Leaves. Plant Physiol. 1962 May;37(3):283–287. doi: 10.1104/pp.37.3.283. [DOI] [PMC free article] [PubMed] [Google Scholar]

Articles from Plant Physiology are provided here courtesy of Oxford University Press

RESOURCES