Resumen:
span style="font-size: 11pt; line-height: 150%; font-family: "Arial", "sans-serif"; color: black;" lang="en">Triosephosphate isomerase (TPI), theglycolytic enzyme that catalyzes the isomerization of dihydroxyacetonephosphate (DHAP) to glyceraldehyde-3-phosphate (G3P), has been frequentlyidentified as a target of S-nitrosylation by proteomic studies. However, theeffect of S-nitrosylation on itsactivity has only been explored in plants and algae. Here, we describe the in vitro S-nitrosylation of human TPI(hTPI), and the effect of the modification on its enzymatic parameters.NO-incorporation into the enzyme cysteine residues occurred by a time-dependent S-transnitrosylation from both, S-nitrosocysteine (CySNO)and S-nitrosoglutathione (GSNO), with CySNO being the more efficient NO-donor.Bo