Glyceraldehyde-3-phosphate activates auto-ADP-ribosylation of glyceraldehyde-3-phosphate dehydrogenase.
Nitric oxide was recently demonstrated to stimulate ADP-ribosylation of glyceraldehyde-3-phosphate dehydrogenase (GAPDH). Our studies on the effect of glyceraldehyde-3-phosphate (GA3P), the natural substrate of dehydrogenase activity of GAPDH, indicated GA3P to be another very potent activator of ADP-ribosylation of the enzyme. GA3P was able to activate ADP-ribosylation only in the presence of DTT. The action of GA3P was associated with inhibition of GAPDH dehydrogenase activity. Ka for GA3P was at least 50-fold lower and maximal activation was somewhat higher than these values for other aldehydes that were also able to enhance GAPDH ADP-ribosylation in the presence of DTT. ADP-ribosylation was blocked by carboxamidomethylation of the essential cysteine SH-group. The bond between the prelabeled protein and ADP-ribose was resistant to hydrolysis with hydroxylamine and HgCl2, suggesting that a lysine epsilon-amino group is the target for ADP-ribosylation.
Kots AYa
Department of Bioorganic Chemistry, School of Biology, Moscow State University, Russian Federation.
Sergienko
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Bulargina
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Severin
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D000246:Adenosine Diphosphate Ribose / Q000378:metabolism*; D000447:Aldehydes / Q000378:metabolism / Q000494:pharmacology; D000818:Animals; D004229:Dithiothreitol / Q000494:pharmacology; D005986:Glyceraldehyde 3-Phosphate / Q000378:metabolism / Q000494:pharmacology*; D005987:Glyceraldehyde-3-Phosphate Dehydrogenases / Q000378:metabolism*; D007700:Kinetics; D009132:Muscles / Q000201:enzymology; D009243:NAD / Q000378:metabolism*; D009599:Nitroprusside / Q000494:pharmacology; D011817:Rabbits; D013379:Substrate Specificity
D000447:Aldehydes; D009243:NAD; D005986:Glyceraldehyde 3-Phosphate; D009599:Nitroprusside; D000246:Adenosine Diphosphate Ribose; D005987:Glyceraldehyde-3-Phosphate Dehydrogenases; D004229:Dithiothreitol