[HTML][HTML] Nitric oxide-induced S-glutathionylation and inactivation of glyceraldehyde-3-phosphate dehydrogenase
S Mohr, H Hallak, A de Boitte, EG Lapetina… - Journal of Biological …, 1999 - ASBMB
S-Nitrosylation of protein thiol groups by nitric oxide (NO) is a widely recognized protein
modification. In this study we show that nitrosonium tetrafluoroborate (BF 4 NO), a NO+
donor, modified the thiol groups of glyceraldehyde-3-phosphate dehydrogenase (GAPDH)
byS-nitrosylation and caused enzyme inhibition. The resultant protein-S-nitrosothiol was
found to be unstable and to decompose spontaneously, thereby restoring enzyme activity. In
contrast, the NO-releasing compound S-nitrosoglutathione (GSNO) promoted S …
modification. In this study we show that nitrosonium tetrafluoroborate (BF 4 NO), a NO+
donor, modified the thiol groups of glyceraldehyde-3-phosphate dehydrogenase (GAPDH)
byS-nitrosylation and caused enzyme inhibition. The resultant protein-S-nitrosothiol was
found to be unstable and to decompose spontaneously, thereby restoring enzyme activity. In
contrast, the NO-releasing compound S-nitrosoglutathione (GSNO) promoted S …