[HTML][HTML] Posttranslational Modification of Glyceraldehyde-3-phosphate Dehydrogenase by S-Nitrosylation and Subsequent NADH Attachment (∗)
S Mohr, JS Stamler, B Brüne - Journal of Biological Chemistry, 1996 - ASBMB
Nitric oxide (NO)-related activity has been associated with an NAD+-dependent modification
of the glycolytic enzyme, glyceraldehyde-3-phosphate dehydrogenase (GAPDH). However,
the mechanism by which NO effects covalent attachment of nucleotide and its role in
regulation of enzyme activity are controversial. Recent studies have shown that S-
nitrosylation of GAPDH (Cys 149) initiates subsequent modification by the pyridinium
cofactor. Here we show that NADH rather than NAD+ is the preferred substrate …
of the glycolytic enzyme, glyceraldehyde-3-phosphate dehydrogenase (GAPDH). However,
the mechanism by which NO effects covalent attachment of nucleotide and its role in
regulation of enzyme activity are controversial. Recent studies have shown that S-
nitrosylation of GAPDH (Cys 149) initiates subsequent modification by the pyridinium
cofactor. Here we show that NADH rather than NAD+ is the preferred substrate …