Thiols mediate superoxide-dependent NADH modification of glyceraldehyde-3-phosphate dehydrogenase
J Rivera-Nieves, WC Thompson, RL Levine… - Journal of Biological …, 1999 - ASBMB
Glyceraldehyde-3-phosphate dehydrogenase (GAPDH) is covalently modified by NAD in the
presence of nitric oxide (NO) and dithiothreitol. Replacement of NAD with NADH in the
presence of SIN-1 (3-morpholinosydnonimine) and dithiothreitol increased modification 25-
fold. We now demonstrate that in contrast to NO-mediated attachment of NAD, covalent
attachment of NADH to GAPDH proceeds in the presence of low molecular weight thiols,
independent of NO. Removal of oxygen and transition metal ions inhibited modification …
presence of nitric oxide (NO) and dithiothreitol. Replacement of NAD with NADH in the
presence of SIN-1 (3-morpholinosydnonimine) and dithiothreitol increased modification 25-
fold. We now demonstrate that in contrast to NO-mediated attachment of NAD, covalent
attachment of NADH to GAPDH proceeds in the presence of low molecular weight thiols,
independent of NO. Removal of oxygen and transition metal ions inhibited modification …
