Ya. Kots et al., GLYCERALDEHYDE-3-PHOSPHATE ACTIVATES AUTO-ADP-RIBOSYLATION OF GLYCERALDEHYDE-3-PHOSPHATE DEHYDROGENASE, FEBS letters, 324(1), 1993, pp. 33-36
Nitric oxide was recently demonstrated to stimulate ADP-ribosylation o
f 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 po
tent activator of ADP-ribosylation of the enzyme. GA3P was able to act
ivate ADP-ribosylation only in the presence of DTT. The action of GA3P
was associated with inhibition of GAPDH dehydrogenase activity. K(a)
for GA3P was at least 50-fold lower and maximal activation was somewha
t higher than these values for other aldehydes that were also able to
enhance GAPDH ADP-ribosylation in the presence of DTT. ADP-ribosylatio
n was blocked by carboxamidomethylation of the essential cysteine SH-g
roup. The bond between the prelabeled protein and ADP-ribose was resis
tant to hydrolysis with hydroxylamine and HgCl2, suggesting that a lys
ine epsilon-amino group is the target for ADP-ribosylation.