Skip to main content
NCBI home page
Plant Physiology logoLink to Plant Physiology
. 1987 Feb;83(2):311–315. doi: 10.1104/pp.83.2.311

Some Properties of Pea Mitochondrial Phospho-Pyruvate Dehydrogenase-Phosphatase 1

Jan A Miernyk 1,2, Douglas D Randall 1
PMCID: PMC1056354  PMID: 16665242

Abstract

Reactivation of the pea mitochondrial pyruvate dehydrogenase complex was the result of dephosphorylation catalyzed by phospho-pyruvate dehydrogenase-phosphatase, an intrinsic component of the complex. Phosphatase activity was dependent upon divalent metal ions, with Mg2+ more effective than Mn2+ or Co2+. The Michaelis constants for Mg2+, Mn2+, and Co2+ were 3.8, 1.7, and 1.4 millimolar, respectively. Neither the rate nor the extent of activation of the phosphatase by Mg2+ or Mn2+ was effected by up to 100 units per assay of megamodulin. Calcium ions did not activate pea mitochondrial phospho-pyruvate dehydrogenase-phosphatase, and low concentrations of Ca2+ antagonized activation by other divalent cations. Phosphatase activity was inhibited by fluoride and ortho-phosphate but not by molybdate or vanadate. Krebs cycle intermediates, adenylates, polyamines, amino acids, and phosphoamino acids were without effect upon pea mitochondrial phospho-pyruvate dehydrogenase-phosphatase activity in vitro.

Full text

PDF
311

Selected References

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

  1. Chernoff J., Li H. C. A major phosphotyrosyl-protein phosphatase from bovine heart is associated with a low-molecular-weight acid phosphatase. Arch Biochem Biophys. 1985 Jul;240(1):135–145. doi: 10.1016/0003-9861(85)90016-5. [DOI] [PubMed] [Google Scholar]
  2. Damuni Z., Humphreys J. S., Reed L. J. Stimulation of pyruvate dehydrogenase phosphatase activity by polyamines. Biochem Biophys Res Commun. 1984 Oct 15;124(1):95–99. doi: 10.1016/0006-291x(84)90921-5. [DOI] [PubMed] [Google Scholar]
  3. Denton R. M., Randle P. J., Bridges B. J., Cooper R. H., Kerbey A. L., Pask H. T., Severson D. L., Stansbie D., Whitehouse S. Regulation of mammalian pyruvate dehydrogenase. Mol Cell Biochem. 1975 Oct 31;9(1):27–53. doi: 10.1007/BF01731731. [DOI] [PubMed] [Google Scholar]
  4. Denton R. M., Randle P. J., Martin B. R. Stimulation by calcium ions of pyruvate dehydrogenase phosphate phosphatase. Biochem J. 1972 Jun;128(1):161–163. doi: 10.1042/bj1280161. [DOI] [PMC free article] [PubMed] [Google Scholar]
  5. Hucho F., Randall D. D., Roche T. E., Burgett M. W., Pelley J. W., Reed L. J. -Keto acid dehydrogenase complexes. XVII. Kinetic and regulatory properties of pyruvate dehydrogenase kinase and pyruvate dehydrogenase phosphatase from bovine kidney and heart. Arch Biochem Biophys. 1972 Jul;151(1):328–340. doi: 10.1016/0003-9861(72)90504-8. [DOI] [PubMed] [Google Scholar]
  6. Kuo W. N. Multiforms of megamodulin-dependent protein kinases from baker's yeast. Mol Cell Biochem. 1984 Sep;64(1):39–44. doi: 10.1007/BF00420926. [DOI] [PubMed] [Google Scholar]
  7. Kuo W. N. Stimulation of mammalian and yeast phosphoprotein phosphatases by megamodulins from various sources. Biochem Biophys Res Commun. 1983 Jul 18;114(1):403–409. doi: 10.1016/0006-291x(83)91641-8. [DOI] [PubMed] [Google Scholar]
  8. Lin Y. M. Calmodulin. Mol Cell Biochem. 1982 Jun 11;45(2):101–112. doi: 10.1007/BF00223504. [DOI] [PubMed] [Google Scholar]
  9. Menon A. S., Devi S. U., Ramasarma T. Fe2+-dependent modulation of 3-hydroxy-3-methylglutaryl CoA reductase by a cytosolic protein, fermodulin. Indian J Biochem Biophys. 1984 Feb;21(1):27–38. [PubMed] [Google Scholar]
  10. Miernyk J. A., Randall D. D. Some kinetic and regulatory properties of the pea mitochondrial pyruvate dehydrogenase complex. Plant Physiol. 1987 Feb;83(2):306–310. doi: 10.1104/pp.83.2.306. [DOI] [PMC free article] [PubMed] [Google Scholar]
  11. Miernyk J. A., Randall D. D. Some kinetic and regulatory properties of the pea mitochondrial pyruvate dehydrogenase complex. Plant Physiol. 1987 Feb;83(2):306–310. doi: 10.1104/pp.83.2.306. [DOI] [PMC free article] [PubMed] [Google Scholar]
  12. Pettit F. H., Roche T. E., Reed L. J. Function of calcium ions in pyruvate dehydrogenase phosphatase activity. Biochem Biophys Res Commun. 1972 Oct 17;49(2):563–571. doi: 10.1016/0006-291x(72)90448-2. [DOI] [PubMed] [Google Scholar]
  13. Randall D. D., Rubin P. M., Fenko M. Plant pyruvate dehydrogenase complex purification, characterization and regulation by metabolites and phosphorylation. Biochim Biophys Acta. 1977 Dec 8;485(2):336–349. doi: 10.1016/0005-2744(77)90169-3. [DOI] [PubMed] [Google Scholar]
  14. Rao K. P., Randall D. D. Plant pyruvate dehydrogenase complex: inactivation and reactivation by phosphorylation and dephosphorylation. Arch Biochem Biophys. 1980 Apr 1;200(2):461–466. doi: 10.1016/0003-9861(80)90377-x. [DOI] [PubMed] [Google Scholar]
  15. Reed L. J. Regulation of mammalian pyruvate dehydrogenase complex by a phosphorylation-dephosphorylation cycle. Curr Top Cell Regul. 1981;18:95–106. doi: 10.1016/b978-0-12-152818-8.50012-8. [DOI] [PubMed] [Google Scholar]
  16. Rubin P. M., Randall D. D. Regulation of plant pyruvate dehydrogenase complex by phosphorylation. Plant Physiol. 1977 Jul;60(1):34–39. doi: 10.1104/pp.60.1.34. [DOI] [PMC free article] [PubMed] [Google Scholar]
  17. Tabor C. W., Tabor H. Polyamines. Annu Rev Biochem. 1984;53:749–790. doi: 10.1146/annurev.bi.53.070184.003533. [DOI] [PubMed] [Google Scholar]

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

RESOURCES