Skip to main content
PMC home page
Plant Physiology logoLink to Plant Physiology
. 1983 Jul;72(3):877–885. doi: 10.1104/pp.72.3.877

Enzyme Regulation in Crassulacean Acid Metabolism Photosynthesis 1

Studies on Thioredoxin-Linked Enzymes of KalanchoË daigremontiana

Steven W Hutcheson 1,2, Bob B Buchanan 1
PMCID: PMC1066337  PMID: 16663102

Abstract

Fructose-1,6-bisphosphatase (FBPase) and sedoheptulose-1,7-bisphosphatase (SBPase) were identified and purified from the Crassulacean acid metabolism (CAM) plant, Kalanchoë daigremontiana. FBPase and SBPase showed respective molecular weights of 180,000 and 76,000, and exhibited immunological cross-reactivity with their counterparts from chloroplasts of C3 (spinach) and C4 (corn) plants. Based on Western blot analysis, FBPase was composed of four identical 45,000-dalton subunits and SBPase of two identical 38,000-dalton subunits. Immunological evidence, together with physical properties, indicated that both enzymes were of chloroplast origin.

Kalanchoë FBPase and SBPase could be activated by thioredoxin f reduced chemically by dithiothreitol or photochemically by a reconstituted Kalanchoë ferredoxin/thioredoxin system. Both enzymes were activated synergistically by reduced thioredoxin f and thier respective substrates.

Kalanchoë FBPase could be partially activated by Mg2+ at concentrations greater than 10 millimolar; however, such activation was considerably less than that observed in the presence of reduced thioredoxin and Ca2+, especially in the pH range between 7.8 and 8.3. In contrast to FBPase, Kalanchoë SBPase exhibited an absolute requirement for a dithiol such as reduced thioredoxin irrespective of Mg2+ concentration. However, like FBPase, increased Mg2+ concentrations enhanced the thioredoxin-linked activation of this enzyme.

In conjunction with these studies, an NADP-linked malate dehydrogenase (NADP-MDH) was identified in cell-free preparations of Kalanchoë leaves which required reduced thioredoxin m for activity.

These results indicate that Kalanchoë FBPase, SBPase, and NADP-MDH share physical and regulatory properties with their equivalents in C3 and C4 plants. In contrast to previous evidence, all three enzymes appear to have the capacity to be photoregulated in chloroplasts of CAM plants, thereby providing a means for the functional segregation of glucan synthesis and degradation.

Full text

PDF
883

Images in this article

880Fig. 2
on p.880

Selected References

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

  1. Anderson L. E., Chin H. M., Gupta V. K. Modulation of Chloroplast Fructose-1,6-bisphosphatase Activity by Light. Plant Physiol. 1979 Sep;64(3):491–494. doi: 10.1104/pp.64.3.491. [DOI] [PMC free article] [PubMed] [Google Scholar]
  2. Buchanan R. B., Schfürmann P., Wolosiuk R. A. Appearance of sedoheptulose 1,7-diphosphatase activity on conversion of chloroplast fructose 1,6-diphosphatase from dimer form to monomer form. Biochem Biophys Res Commun. 1976 Apr 19;69(4):970–978. doi: 10.1016/0006-291x(76)90468-x. [DOI] [PubMed] [Google Scholar]
  3. Charles S. A., Halliwell B. Action of calcium ions on spinach (Spinacia oleracea) chloroplast fructose bisphosphatase and other enzymes of the Calvin cycle. Biochem J. 1980 Jun 15;188(3):775–779. doi: 10.1042/bj1880775. [DOI] [PMC free article] [PubMed] [Google Scholar]
  4. Cséke C., Nishizawa A. N., Buchanan B. B. Modulation of chloroplast phosphofructokinase by NADPH : a mechanism for linking light to the regulation of glycolysis. Plant Physiol. 1982 Sep;70(3):658–661. doi: 10.1104/pp.70.3.658. [DOI] [PMC free article] [PubMed] [Google Scholar]
  5. Cséke C., Weeden N. F., Buchanan B. B., Uyeda K. A special fructose bisphosphate functions as a cytoplasmic regulatory metabolite in green leaves. Proc Natl Acad Sci U S A. 1982 Jul;79(14):4322–4326. doi: 10.1073/pnas.79.14.4322. [DOI] [PMC free article] [PubMed] [Google Scholar]
  6. Frieden C. Protein-protein interaction and enzymatic activity. Annu Rev Biochem. 1971;40:653–696. doi: 10.1146/annurev.bi.40.070171.003253. [DOI] [PubMed] [Google Scholar]
  7. Gupta V. K., Anderson L. E. Light modulation of the activity of carbon metabolism enzymes in the crassulacean Acid metabolism plant kalanchoë. Plant Physiol. 1978 Mar;61(3):469–471. doi: 10.1104/pp.61.3.469. [DOI] [PMC free article] [PubMed] [Google Scholar]
  8. Hertig C. M., Wolosiuk R. A. Studies on the hysteretic properties of chloroplast fructose-1,6-bisphosphatase. J Biol Chem. 1983 Jan 25;258(2):984–989. [PubMed] [Google Scholar]
  9. Heuer B., Hansen M. J., Anderson L. E. Light modulation of phosphofructokinase in pea leaf chloroplasts. Plant Physiol. 1982 Jun;69(6):1404–1406. doi: 10.1104/pp.69.6.1404. [DOI] [PMC free article] [PubMed] [Google Scholar]
  10. Hutcheson S. W., Buchanan B. B. Enzyme Regulation in Crassulacean Acid Metabolism Photosynthesis : Studies on the Ferredoxin/Thioredoxin System of KalanchoE daigremontiana. Plant Physiol. 1983 Jul;72(3):870–876. doi: 10.1104/pp.72.3.870. [DOI] [PMC free article] [PubMed] [Google Scholar]
  11. Jacquot J. P., Buchanan B. B. Enzyme Regulation in C(4) Photosynthesis : PURIFICATION AND PROPERTIES OF THIOREDOXIN-LINKED NADP-MALATE DEHYDROGENASE FROM CORN LEAVES. Plant Physiol. 1981 Aug;68(2):300–304. doi: 10.1104/pp.68.2.300. [DOI] [PMC free article] [PubMed] [Google Scholar]
  12. Kelly G. J., Latzko E. Chloroplast Phosphofructokinase: II. Partial Purification, Kinetic and Regulatory Properties. Plant Physiol. 1977 Aug;60(2):295–299. doi: 10.1104/pp.60.2.295. [DOI] [PMC free article] [PubMed] [Google Scholar]
  13. Marcus F., Edelstein I., Nishizawa A. N., Buchanan B. B. Limited proteolysis of chloroplast fructose 1,6-bisphosphatase by subtilisin. Biochem Biophys Res Commun. 1980 Dec 31;97(4):1304–1310. doi: 10.1016/s0006-291x(80)80008-8. [DOI] [PubMed] [Google Scholar]
  14. Nishizawa A. N., Buchanan B. B. Enzyme regulation in C4 photosynthesis. Purification and properties of thioredoxin-linked fructose bisphosphatase and sedoheptulose bisphosphatase from corn leaves. J Biol Chem. 1981 Jun 25;256(12):6119–6126. [PubMed] [Google Scholar]
  15. Preiss J., Biggs M. L., Greenberg E. The effect of magnesium ion concentration on the pH optimum of the spinach leaf alkaline fructose diphosphatase. J Biol Chem. 1967 May 10;242(9):2292–2294. [PubMed] [Google Scholar]
  16. Woodrow I. E., Walker D. A. Light-mediated activation of stromal sedoheptulose bisphosphatase. Biochem J. 1980 Dec 1;191(3):845–849. doi: 10.1042/bj1910845. [DOI] [PMC free article] [PubMed] [Google Scholar]
  17. Zimmermann G., Kelly G. J., Latzko E. Efficient purification and molecular properties of spinach chloroplast fructose 1,6-bisphosphatase. Eur J Biochem. 1976 Nov 15;70(2):361–367. doi: 10.1111/j.1432-1033.1976.tb11025.x. [DOI] [PubMed] [Google Scholar]

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

RESOURCES