[38] Nitric oxide-induced covalent modification of glycolytic enzyme glyceraldehyde-3-phosphate dehydrogenase
B Brüne, EG Lapetina - Methods in enzymology, 1996 - Elsevier
Publisher Summary This chapter describes the experiments that allow the identification of
the target amino acid of the substrate. Both nitric oxide (NO) donors and active NO
synthases (NOS) cause [32 P] NAD (H)-dependent automodification of the glycolytic enzyme
glyceraldehyde-3-phosphate dehydrogenase (GAPDH). This cyclic guanosine
monophospahte (cGMP)-independent action of NO involves a protein S-nitrosothiol
intermediate, which is followed by the covalent modification of GAPDH by [32 P] NAD+ or [32 …
the target amino acid of the substrate. Both nitric oxide (NO) donors and active NO
synthases (NOS) cause [32 P] NAD (H)-dependent automodification of the glycolytic enzyme
glyceraldehyde-3-phosphate dehydrogenase (GAPDH). This cyclic guanosine
monophospahte (cGMP)-independent action of NO involves a protein S-nitrosothiol
intermediate, which is followed by the covalent modification of GAPDH by [32 P] NAD+ or [32 …