6D43
CHARACTERIZATION OF HUMAN TRIOSEPHOSPHATE ISOMERASE S-NITROSYLATION
Summary for 6D43
| Entry DOI | 10.2210/pdb6d43/pdb |
| Descriptor | Triosephosphate isomerase, ISOPROPYL ALCOHOL, ... (4 entities in total) |
| Functional Keywords | s-nitrosylation, isomerase, glycolysis, tim-barrel, dihydroxyacetone phosphate |
| Biological source | Homo sapiens (Human) More |
| Total number of polymer chains | 2 |
| Total formula weight | 52893.25 |
| Authors | Romero, J.M.,Carrizo, M.E.,Curtino, J.M. (deposition date: 2018-04-17, release date: 2018-05-16, Last modification date: 2024-10-23) |
| Primary citation | Romero, J.M.,Carrizo, M.E.,Curtino, J.A. Characterization of human triosephosphate isomerase S-nitrosylation. Nitric Oxide, 77:26-34, 2018 Cited by PubMed 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. PubMed: 29678765DOI: 10.1016/j.niox.2018.04.004 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.04 Å) |
Structure validation
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