Skip to main content
NCBI home page
Plant Physiology logoLink to Plant Physiology
. 1973 Jun;51(6):1142–1144. doi: 10.1104/pp.51.6.1142

Control of CO2 Fixation by Cell-free Extracts of Chlamydomonas reinhardtii

D D Davies 1, K D Patil 1
PMCID: PMC366421  PMID: 16658482

Abstract

Contrary to earlier reports, CO2 fixation by extracts of Chlamydomonas is inhibited by glutamate and aspartate. These amino acids and some organic acids are shown to be inhibitors of phosphoenolpyruvate carboxylase. Inorganic phosphate is shown to activate CO2 fixation, but there is a time lag before inorganic phosphate exerts its full activating effect.

Full text

PDF
1142

Selected References

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

  1. Chen J. H., Jones R. F. Multiple forms of phosphoenolpyruvate carboxylase from Chlamydomonas reeinhardtii. Biochim Biophys Acta. 1970 Aug 21;214(2):318–325. doi: 10.1016/0005-2795(70)90009-7. [DOI] [PubMed] [Google Scholar]
  2. Cánovas J. L., Kornberg H. L. Properties and regulation of phosphopyruvate carboxylase activity in Escherichia coli. Proc R Soc Lond B Biol Sci. 1966 Aug 16;165(999):189–205. doi: 10.1098/rspb.1966.0064. [DOI] [PubMed] [Google Scholar]
  3. Frieden C. Kinetic aspects of regulation of metabolic processes. The hysteretic enzyme concept. J Biol Chem. 1970 Nov 10;245(21):5788–5799. [PubMed] [Google Scholar]
  4. Jones R. F., Chen J. H. Amino acid stimulation of carbon dioxide fixation in cell-free extracts of Chlamydomonas reinhardtii. Plant Physiol. 1970 Nov;46(5):761–762. doi: 10.1104/pp.46.5.761. [DOI] [PMC free article] [PubMed] [Google Scholar]
  5. MONOD J., WYMAN J., CHANGEUX J. P. ON THE NATURE OF ALLOSTERIC TRANSITIONS: A PLAUSIBLE MODEL. J Mol Biol. 1965 May;12:88–118. doi: 10.1016/s0022-2836(65)80285-6. [DOI] [PubMed] [Google Scholar]
  6. Maruyama H., Easterday R. L., Chang H. C., Lane M. D. The enzymatic carboxylation of phosphoenolpyruvate. I. Purification and properties of phosphoenolpyruvate carboxylase. J Biol Chem. 1966 May 25;241(10):2405–2412. [PubMed] [Google Scholar]
  7. Sanwal B. D., Maeba P. Regulation of the activity of phosphoenolypyruvate carboxylase by fructose diphosphate. Biochem Biophys Res Commun. 1966 Jan 24;22(2):194–199. doi: 10.1016/0006-291x(66)90431-1. [DOI] [PubMed] [Google Scholar]
  8. Smith T. E. Partial purification and characteristics of potato phosphoenolpyruvate carboxylase. Arch Biochem Biophys. 1968 Apr;125(1):178–188. doi: 10.1016/0003-9861(68)90653-x. [DOI] [PubMed] [Google Scholar]
  9. Sueoka N. MITOTIC REPLICATION OF DEOXYRIBONUCLEIC ACID IN CHLAMYDOMONAS REINHARDI. Proc Natl Acad Sci U S A. 1960 Jan;46(1):83–91. doi: 10.1073/pnas.46.1.83. [DOI] [PMC free article] [PubMed] [Google Scholar]
  10. Ting I. P. CO(2) Metabolism in Corn Roots. III. Inhibition of P-enolpyruvate Carboxylase by l-malate. Plant Physiol. 1968 Dec;43(12):1919–1924. doi: 10.1104/pp.43.12.1919. [DOI] [PMC free article] [PubMed] [Google Scholar]

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

RESOURCES