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Redox modulation of a phosphatase from Anacystis nidulans

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Abstract

Ascorbic acid (AA) increased the phosphatase activity (pH 6.8) in 10,000 g supernatants from Anacystis nidulans. The enzyme activated by AA was deactivated by dehydroascorbic acid (DHAA). The modulation by AA/DHAA of phosphatase activity in Anacystis appears to be specific; a number of other redox compounds, known to modulate other enzymes, had no effect on the Anacystis phosphatase. A purified phosphatase preparation from Anacystis was also deactivated by DHAA. In contrast, the purified enzyme was not activated by AA, suggesting that a factor mediating the effect of AA was lost during purification. Another factor was found to protect the purified phosphatase against deactivation by DHAA. The enzyme was characterized as a phosphatase with a broad substrate specificity, an apparent molecular weight of 19,000, and a pH optimum of 6.0–7.0. Dialysis of the enzyme preparation against EDTA abolished the phosphatase activity which could be restored by Zn2+ ions and partially restored by Co2+ ions. Crude extracts also contained a latent enzyme, the phosphatase activity of which could be detected in the presence of Co2+ ions only. Zn2+ ions did not activate this enzymatically inactive protein. The Co2+-dependent phosphatase had an apparent mol. wt. of 40,000, a broad substrate specificity, and an alkaline pH-optimum. Infection of Anacystis cultures by cyanophage AS-1 resulted in a decrease in phosphatase activity. The enzyme present in 10,000 g supernatants from infected cells could not be modulated by the AA/DHAA system.

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Abbreviations

AA:

ascorbic acid

DEAE:

diethylamino ethyl

DHAA:

dehydroascorbic acid

EDTA:

ethylene-diaminetetra-acetate

G6PDH:

glucose-6-phosphate dehydrogenase

GSH:

reduced glutathione

GSSG:

oxidized glutathione

HMP:

hexose monophosphate

P i :

inorganic phosphorus

pNPP:

p-nitrophenylphosphate

pNP:

p-nitrophenol

Tris:

Tris(hydroxymethyl)-aminomethane

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Authors and Affiliations

  1. Institute of Plant Physiology, Biological Research Center, Hungarian Academy of Sciences, P.O. Box 521, H-6701, Szeged, Hungary

    M. Godeh, J. Udvardy & G. L. Farkas

Authors
  1. M. Godeh
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  2. J. Udvardy
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  3. G. L. Farkas
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Godeh, M., Udvardy, J. & Farkas, G.L. Redox modulation of a phosphatase from Anacystis nidulans . Planta 152, 408–414 (1981). https://doi.org/10.1007/BF00385356

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  • DOI: https://doi.org/10.1007/BF00385356

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