Glyceraldehyde‐3‐phosphate activates auto‐ADP‐ribosylation of glyceraldehyde‐3‐phosphate dehydrogenase

FEBS Letters

Bulargina, Tamara V.¹  Kots, Alexander Ya.¹  Severin, Eugene S.¹  Sergienko, Edward A.² 

[1] Department of Bioorganic Chemistry, School of Biology Moscow State University, Moscow 119899, Russian Federation;A.N. Belosersky Institute of Physico-Chemical Biology, Moscow State University, Moscow 119899, Russian Federation

关键词: ADP-ribosylation;    Glyceraldehyde-3-phosphate;    Glyceraldehyde-3-phosphate dehydrogenase;    GAPDH;    glyceraldehyde-3-phosphate dehydrogenase;    GA3P;    glyceraldehyde-3-phosphate;    DTT;    dithiothreitol;   

DOI  :  10.1016/0014-5793(93)81526-6

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

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. K _a 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 ε-amino group is the target for ADP-ribosylation.

【 授权许可】

Unknown