Abstract
Glyceraldehyde-3-phosphate dehydrogenase (EC 1.2.1.13; GAPDH) from the cyanobacteriumAnacystis nidulans was activated up to five-fold by reduced glutathione (GSH) in the physiological concentration range (0.1–2 mM GSH). Non-physiological reductants, like dithiothreitol (DTT) and β-mercaptoethanol, also activated the enzyme. Oxidized glutathione (GSSG) had no effect on the cyanobacterial GAPDH but treatment with H2O2 led to a rapid, reversible deactivation of both untreated and GSH-treated enzyme preparations. GSH reversed the inhibition induced by H2O2. An oligomeric form of the enzyme (apparentM r∼440,000) was dissociated by GSH into a lower-M r, more active enzyme form (M r∼200,000). The enzyme was shown to obey regular Michaelis-Menten kinetics. The activation of GAPDH by GSH was associated with a decrease inK m and an increase inV max values of the enzyme for 3-phosphoglycerate. GSH had virtually no effect on a GAPDH preparation isolated from corn chloroplasts and studied for comparison.
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Abbreviations
- GAPDH:
-
glyceraldehyde-3-phosphate dehydrogenase
- GSH:
-
reduced glutathione
- GSSG:
-
oxidized glutathione
- DTT:
-
dithiothreitol
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Udvardy, J., Balogh, Á. & Farkas, G.L. Modulation of glyceraldehyde-3-phosphate dehydrogenase inAnacystis nidulans by glutathione. Arch. Microbiol. 133, 2–5 (1982). https://doi.org/10.1007/BF00943760
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DOI: https://doi.org/10.1007/BF00943760