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. 1976 Feb;57(2):310–314. doi: 10.1104/pp.57.2.310

Nicotinamide Adenine Dinucleotide-specific “Malic” Enzyme in Kalanchoë daigremontiana and Other Plants Exhibiting Crassulacean Acid Metabolism 1

Peter Dittrich a
PMCID: PMC542014  PMID: 16659473

Abstract

NAD-specific “malic” enzyme (EC 1.1.1.39) has been isolated and purified 1200-fold from leaves of Kalanchoë daigremontiana. Kinetic studies of this enzyme, which is activated 14-fold by CoA, acetyl-CoA, and SO42−, suggest allosteric properties. Cofactor requirements show an absolute specificity for NAD and for Mn2+, which cannot be replaced by NADP or Mg2+. For maintaining enzyme activity in crude leaf extracts a thiol reagent, Mn2+, and PVP-40 were required. The latter could be omitted from purified preparations. By sucrose density gradient centrifugation NAD-malic enzyme could be localized in mitochondria. A survey of plants with crassulacean acid metabolism revealed the presence of NAD-malic enzyme in all 31 plants tested. Substantial levels of this enzyme (121-186 μmole/hr·mg of Chl) were detected in all members tested of the family Crassulaceae. It is proposed that NAD-malic enzyme in general supplements activity of NADP-malic enzyme present in these plants and may be specifically employed to increase internal concentrations of CO2 for recycling during cessation of gas exchange in periods of severe drought.

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Selected References

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

  1. Dittrich P., Campbell W. H., Black C. C. Phosphoenolpyruvate carboxykinase in plants exhibiting crassulacean Acid metabolism. Plant Physiol. 1973 Oct;52(4):357–361. doi: 10.1104/pp.52.4.357. [DOI] [PMC free article] [PubMed] [Google Scholar]
  2. Macrae A. R. Isolation and properties of a 'malic' enzyme from cauliflower bud mitochondria. Biochem J. 1971 May;122(4):495–501. doi: 10.1042/bj1220495. [DOI] [PMC free article] [PubMed] [Google Scholar]
  3. Sugiyama T. Occurrence of Pyruvate Orthophosphate Dikinase in the Succulent Plant, Kalanchoë daigremontiana Hamet. et. Perr. Plant Physiol. 1975 Nov;56(5):605–607. doi: 10.1104/pp.56.5.605. [DOI] [PMC free article] [PubMed] [Google Scholar]
  4. Szarek S. R., Johnson H. B., Ting I. P. Drought Adaptation in Opuntia basilaris: Significance of Recycling Carbon through Crassulacean Acid Metabolism. Plant Physiol. 1973 Dec;52(6):539–541. doi: 10.1104/pp.52.6.539. [DOI] [PMC free article] [PubMed] [Google Scholar]
  5. Szarek S. R., Ting I. P. Seasonal Patterns of Acid Metabolism and Gas Exchange in Opuntia basilaris. Plant Physiol. 1974 Jul;54(1):76–81. doi: 10.1104/pp.54.1.76. [DOI] [PMC free article] [PubMed] [Google Scholar]
  6. Takeo K., Murai T., Nagai J., Katsuki H. Allosteric activation of DPN-linked malic enzyme from Escherichia coli by aspartate. Biochem Biophys Res Commun. 1967 Dec 15;29(5):717–722. doi: 10.1016/0006-291x(67)90276-8. [DOI] [PubMed] [Google Scholar]
  7. Wintermans J. F., de Mots A. Spectrophotometric characteristics of chlorophylls a and b and their pheophytins in ethanol. Biochim Biophys Acta. 1965 Nov 29;109(2):448–453. doi: 10.1016/0926-6585(65)90170-6. [DOI] [PubMed] [Google Scholar]

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