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Properties of Phosphoglycolate Phosphatase from Chlamydomonas reinhardtii and Anacystis nidulans

H. David Husic and N. E. Tolbert
Plant Physiology
Vol. 79, No. 2 (Oct., 1985), pp. 394-399
Stable URL: http://www.jstor.org/stable/4269531
Page Count: 6
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Since scans are not currently available to screen readers, please contact JSTOR User Support for access. We'll provide a PDF copy for your screen reader.
Properties of Phosphoglycolate Phosphatase from Chlamydomonas reinhardtii and Anacystis nidulans
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Abstract

The levels of activity of 2-phosphoglycolate phosphatase in the green algae, Chlamydomonas reinhardtii and Chlorella vulgaris, were in the range of 37 to 60 micromoles per milligram chlorophyll per hour and in the blue-green algae, Anacystis nidulans and Anabaena variabilis were 204 to 310 micromoles per milligram chlorophyll per hour. The activity in each species was similar regardless of whether the algae were grown with air or 5% CO2 in air. The enzyme purified 530-fold from Chlamydomonas was stable, had a broad pH optimum between 6 and 8.5, and was specific for the hydrolysis of P-glycolate with a Km of 23 micromolar. The enzyme purified 18-fold from Anacystis was labile, had a sharp pH optimum at 6.3, and was also specific for P-glycolate with a Km of 94 micromolar. The molecular weight of the enzyme from Chlamydomonas was estimated to be 92,000 by gel filtration. The phosphatase from both sources required a divalent cation for activity. The Chlamydomonas enzyme was most effectively activated by Co2+, but was also activated by Mg2+ (Ka = 30 micromolar), Mn2+, and Zn2+. The Anacystis enzyme was most effectively activated by Mg2+ (Ka = 140 micromolar), and was also activated by Co2+ and Mn2+, but not by Zn2+. Anions were also required for maximum activity of the enzyme from both sources. The Chlamydomonas enzyme was activated about 2-to 3-fold by chloride (Ka = 140 micromolar), bromide, nitrate, bicarbonate (Ka = 600 micromolar) and formate. The Anacystis enzyme was activated over 10-fold by chloride (Ka = 870 micromolar), bromide, iodide, and nitrate, but was not activated by bicarbonate or formate. The properties of the algal enzymes were similar to those previously reported for higher plants. The levels and kinetic properties of the enzyme seemed sufficient to account for the flux through the glycolate pathway that occurs in these algae. The phosphatase was not associated with the ribulose 1,5-bisphosphate carboxylase/oxygenase responsible for P-glycolate formation in the carboxysomes of Anacystis.

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