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. 1969 Feb;44(2):262–266. doi: 10.1104/pp.44.2.262

Relative Activities of NAD- and NADP-Isocitric Dehydrogenases in Bean Mitochondria Modified by Glycerol or NADP 1

Yukio Yamamoto a
PMCID: PMC396072  PMID: 4388200

Abstract

Mitochondria from cotyledons of Vigna sesquipedalis (L.) Fruwirth (starchy seed) showed no NAD-isocitric dehydrogenase (NAD-IDH) activity by the methods which have been known to be useful for the detection of NAD-IDH in mitochondria of plants including castor bean and alaska pea. When the Vigna cotyledon mitochondria were treated with glycerol, NAD-IDH activity appeared and NADP-isocitric dehydrogenase (NADP-IDH) activity was inhibited. The inhibition of mitochondrial NADP-IDH by glycerol was overcome by the addition of excess NADP.

On the other hand, NADP-IDH activity in the soluble fraction of cell components was only slightly inhibited by glycerol and no NAD-IDH activity was elicited.

It was postulated that NADP-IDH in mitochondria is converted to NAD-IDH by glycerol and back to NADP-IDH with NADP by the alteration in the spatial configuration of the enzyme. However, there could be 2 proteins as the other possibility.

The NADP-IDH in the soluble fraction which is not subject to such alteration is different from the mitochondrial NADP-IDH.

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Selected References

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

  1. CHEN R. F., PLAUT G. W. ACTIVATION AND INHIBITION OF DPN-LINKED ISOCITRATE DEHYDROGENASE OF HEART BY CERTAIN NUCLEOTIDES. Biochemistry. 1963 Sep-Oct;2:1023–1032. doi: 10.1021/bi00905a020. [DOI] [PubMed] [Google Scholar]
  2. DAVIES D. D. Some aspects of plant mitochondria. Proc R Soc Lond B Biol Sci. 1954 Mar 25;142(907):155–160. doi: 10.1098/rspb.1954.0014. [DOI] [PubMed] [Google Scholar]
  3. ERNSTER L., NAVAZIO F. The cytoplasmic distribution of isocitric dehydrogenases. Exp Cell Res. 1956 Aug;11(2):483–486. doi: 10.1016/0014-4827(56)90124-0. [DOI] [PubMed] [Google Scholar]
  4. GOEBELL H., KLINGENBERG M. DPN-SPEZIFISCHE ISOCITRAT-DEHYDROGENASE DER MITOCHONDRIEN. I. KINETISCHE EIGENSSCHAFTEN, VORKOMMEN UND FUNKTION DER DPN-SPEZIFISCHEN ISOCITRAT-DEHYDROGENASE. Biochem Z. 1964 Sep 28;340:441–464. [PubMed] [Google Scholar]
  5. HOGEBOOM G. H., SCHNEIDER W. C. Biochemistry of cellular particles. Annu Rev Biochem. 1956;25:201–224. doi: 10.1146/annurev.bi.25.070156.001221. [DOI] [PubMed] [Google Scholar]
  6. HOGEBOOM G. H., SCHNEIDER W. C. Cytochemical studies of mammalian tissues. III. Isocitric dehydrogenase and triphosphopyridine nucleotide-cytochrome c reductase of mouse liver. J Biol Chem. 1950 Oct;186(2):417–427. [PubMed] [Google Scholar]
  7. KLINGENBERG M., GOEBELL H., WENSKE G. DPN-SPECIFIC ISOCITRATE-DEHYDROGENASE OF MITOCHONDRIA. II. PH-DEPENDENCE OF THE KINETICS AND THE MECHANISM OF ACTIVATION. Biochem Z. 1965 Feb 8;341:199–223. [PubMed] [Google Scholar]
  8. KORNBERG A., PRICER W. E., Jr Di- and triphosphopyridine nucleotide isocitric dehydrogenases in yeast. J Biol Chem. 1951 Mar;189(1):123–136. [PubMed] [Google Scholar]
  9. Kaplan N. O., Swartz M. N., Frech M. E., Ciotti M. M. PHOSPHORYLATIVE AND NONPHOSPHORYLATIVE PATHWAYS OF ELECTRON TRANSFER IN RAT LIVER MITOCHONDRIA. Proc Natl Acad Sci U S A. 1956 Aug;42(8):481–487. doi: 10.1073/pnas.42.8.481. [DOI] [PMC free article] [PubMed] [Google Scholar]
  10. LOWRY O. H., ROSEBROUGH N. J., FARR A. L., RANDALL R. J. Protein measurement with the Folin phenol reagent. J Biol Chem. 1951 Nov;193(1):265–275. [PubMed] [Google Scholar]
  11. Levy H. R., Raineri R. R., Nevaldine B. H. On the structure and catalytic function of mammary glucose 6-phosphate dehydrogenase. J Biol Chem. 1966 May 25;241(10):2181–2187. [PubMed] [Google Scholar]
  12. PURVIS J. L. Pathway of oxidation of isocitrate by mitochondria and the role of the transhydrogenase reaction. Biochim Biophys Acta. 1961 Sep 2;52:148–155. doi: 10.1016/0006-3002(61)90912-x. [DOI] [PubMed] [Google Scholar]
  13. RAGLAND T. E., HACKETT D. P. COMPARTMENTATION OF NICOTINAMIDE DINUCLEOTIDE DEHYDROGENASES AND TRANSHYDROGENASES IN NONPHOTOSYNTHETIC PLANT TISSUES. Arch Biochem Biophys. 1964 Dec;108:479–489. doi: 10.1016/0003-9861(64)90430-8. [DOI] [PubMed] [Google Scholar]
  14. Ragland T. E., Hackett D. P. Radioactive Tracer Studies of the Metabolic Fates of Intracellularly Generated NADH and NADPH in Higher Plant Tissues. Plant Physiol. 1965 Nov;40(6):1191–1197. doi: 10.1104/pp.40.6.1191. [DOI] [PMC free article] [PubMed] [Google Scholar]
  15. VIGNAIS P. V., VIGNAIS P. M. [Role of di- and triphosphopyridine nucleotides in the mitochondrial oxidation of isocitrate]. Biochim Biophys Acta. 1961 Mar 4;47:515–528. doi: 10.1016/0006-3002(61)90545-5. [DOI] [PubMed] [Google Scholar]
  16. Yamamoto Y. Pyridine Nucleotide Content in the Higher Plant. Effect of Age of Tissue. Plant Physiol. 1963 Jan;38(1):45–54. doi: 10.1104/pp.38.1.45. [DOI] [PMC free article] [PubMed] [Google Scholar]

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