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. 2018 Jul 1;77:26-34.
doi: 10.1016/j.niox.2018.04.004. Epub 2018 Apr 17.

Characterization of Human Triosephosphate Isomerase S-nitrosylation

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Characterization of Human Triosephosphate Isomerase S-nitrosylation

Jorge Miguel Romero et al. Nitric Oxide. .

Abstract

Triosephosphate isomerase (TPI), the glycolytic enzyme that catalyzes the isomerization of dihydroxyacetone phosphate (DHAP) to glyceraldehyde-3-phosphate (G3P), has been frequently identified as a target of S-nitrosylation by proteomic studies. However, the effect of S-nitrosylation on its activity 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. Both X-ray crystal structure and mass spectrometry analyses showed that only Cys217 was S-nitrosylated. hTPI S-nitrosylation produced a 30% inhibition of the Vmax of the DHAP conversion to G3P, without affecting the Km for DHAP. This is the first study describing features of human TPI S-nitrosylation.

Keywords: Nitric oxide; S-nitrosocysteine; S-nitrosoglutathione; S-nitrosylation; Triosephosphate isomerase.

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