Skip to main content
NCBI home page
Plant Physiology logoLink to Plant Physiology
. 1991 Mar;95(3):693–698. doi: 10.1104/pp.95.3.693

Purification and Characterization of Phosphoglycolate Phosphatase from the Cyanobacterium Coccochloris peniocystis1

Eric G Norman 1, Brian Colman 1
PMCID: PMC1077593  PMID: 16668041

Abstract

The properties and role of the enzyme phosphoglycolate phosphatase in the cyanobacterium Coccochloris peniocystis have been investigated. Phosphoglycolate phosphatase was purified 92-fold and had a native molecular mass of approximately 56 kilodaltons. The enzyme demonstrated a broad pH optimum of pH 5.0 to 7.5 and showed a relatively low apparent affinity for substrate (Km = 222 micromolar) when compared to that from higher plants. The enzyme required both an anion and divalent cation for activity. Mn2+ and Mg2+ were effective divalent cations while Cl− was the most effective anion tested. The enzyme was specific for phosphoglycolate and did not show any activity toward a variety of organic phosphate esters. Growth of the cells on high CO2 and transfer to air did not result in any significant change in phosphoglycolate phosphatase activity. Competitive inhibition of C. peniocystis triose phosphate isomerase by phosphoglycolate was demonstrated (Ki = 12.9 micromolar). These results indicate the presence of a specific noninducible phosphoglycolate phosphatase whose sole function may be to hydrolyze phosphoglycolate and prevent phosphoglycolate inhibition of triose phosphate isomerase.

Full text

PDF
693

Selected References

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

  1. Anderson L. E. Chloroplast and cytoplasmic enzymes. II. Pea leaf triose phosphate isomerases. Biochim Biophys Acta. 1971 Apr 14;235(1):237–244. doi: 10.1016/0005-2744(71)90051-9. [DOI] [PubMed] [Google Scholar]
  2. Christeller J. T., Tolbert N. E. Phosphoglycolate phosphatase. Effect of cation and pH on activity. J Biol Chem. 1978 Mar 25;253(6):1786–1790. [PubMed] [Google Scholar]
  3. Christeller J. T., Tolbert N. E. Phosphoglycolate phosphatase. Purification and properties. J Biol Chem. 1978 Mar 25;253(6):1780–1785. [PubMed] [Google Scholar]
  4. Codd G. A., Stewart W. D. Pathways of glycollate metabolism in the blue-green alga Anabaena cylindrica. Arch Mikrobiol. 1973 Dec 4;94(1):11–28. doi: 10.1007/BF00414075. [DOI] [PubMed] [Google Scholar]
  5. Coleman J. R., Colman B. Inorganic Carbon Accumulation and Photosynthesis in a Blue-green Alga as a Function of External pH. Plant Physiol. 1981 May;67(5):917–921. doi: 10.1104/pp.67.5.917. [DOI] [PMC free article] [PubMed] [Google Scholar]
  6. Husic H. D., Tolbert N. E. Anion and divalent cation activation of phosphoglycolate phosphatase from leaves. Arch Biochem Biophys. 1984 Feb 15;229(1):64–72. doi: 10.1016/0003-9861(84)90130-9. [DOI] [PubMed] [Google Scholar]
  7. Husic H. D., Tolbert N. E. Properties of Phosphoglycolate Phosphatase from Chlamydomonas reinhardtii and Anacystis nidulans. Plant Physiol. 1985 Oct;79(2):394–399. doi: 10.1104/pp.79.2.394. [DOI] [PMC free article] [PubMed] [Google Scholar]
  8. 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]
  9. Marcus Y., Harel E., Kaplan A. Adaptation of the Cyanobacterium Anabaena variabilis to Low CO(2) Concentration in Their Environment. Plant Physiol. 1983 Jan;71(1):208–210. doi: 10.1104/pp.71.1.208. [DOI] [PMC free article] [PubMed] [Google Scholar]
  10. Markwell M. A., Haas S. M., Bieber L. L., Tolbert N. E. A modification of the Lowry procedure to simplify protein determination in membrane and lipoprotein samples. Anal Biochem. 1978 Jun 15;87(1):206–210. doi: 10.1016/0003-2697(78)90586-9. [DOI] [PubMed] [Google Scholar]
  11. RICHARDSON K. E., TOLBERT N. E. Phosphoglycolic acid phosphatase. J Biol Chem. 1961 May;236:1285–1290. [PubMed] [Google Scholar]
  12. Suzuki K., Marek L. F., Spalding M. H. A Photorespiratory Mutant of Chlamydomonas reinhardtii. Plant Physiol. 1990 May;93(1):231–237. doi: 10.1104/pp.93.1.231. [DOI] [PMC free article] [PubMed] [Google Scholar]
  13. Wolfenden R. Binding of substrate and transition state analog to trisephosphate isomerase. Biochemistry. 1970 Aug 18;9(17):3404–3407. doi: 10.1021/bi00819a018. [DOI] [PubMed] [Google Scholar]

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

RESOURCES