ArticleProtein science : a publication of the Protein Society2010
Mechanism of glyceraldehyde-3-phosphate dehydrogenase inactivation by tyrosine nitration.
Article in Protein science : a publication of the Protein Society, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.
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Who cites it
12 citing papers in PubMed, 28 citations in OpenAlex.
- Protein Tyrosine Amination: Detection, Imaging, and Chemoproteomic Profiling with Synthetic Probes.Journal of the American Chemical Society · 2024Article
- REST Protects Dopaminergic Neurons from Mitochondrial and α-Synuclein Oligomer Pathology in an Alpha Synuclein Overexpressing BAC-Transgenic Mouse Model.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2021Article
- Mass Spectrometry-Based Protein Footprinting for Higher-Order Structure Analysis: Fundamentals and Applications.Chemical reviews · 2020Review
- Switchable Nitroproteome States ofFrontiers in microbiology · 2019Article
- Down regulation of NO signaling in Trypanosoma cruzi upon parasite-extracellular matrix interaction: changes in protein modification by nitrosylation and nitration.PLoS neglected tropical diseases · 2015Article
- Radicalization of Glyceraldehyde-3-Phosphate Dehydrogenase by HOCl in Living Cells.Enzyme engineering (Los Angeles, Calif.) · 2015Article
- Neurovascular and neurometabolic derailment in aging and Alzheimer's disease.Frontiers in aging neuroscience · 2015Review
- Identification of glyceraldehyde 3-phosphate dehydrogenase sequence and expression profiles in tree shrew (Tupaia belangeri).PloS one · 2014Article
- Tyrosine modifications in aging.Antioxidants & redox signaling · 2012Review
- Amyloid beta modulated the selectivity of heme-catalyzed protein tyrosine nitration: an alternative mechanism for selective protein nitration.Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry · 2012Article
- Selective vulnerability of synaptic signaling and metabolism to nitrosative stress.Antioxidants & redox signaling · 2012Review
- In vivo protein tyrosine nitration in Arabidopsis thaliana.Journal of experimental botany · 2011Article
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Authors and funding
2 authors at 2 institutions in 1 country.
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Abstract
Glyceraldehyde-3-phosphate dehydrogenase (GAPDH) is a multifaceted protein that is involved in numerous processes including glycolysis, translational silencing, transcriptional regulation of specific genes, and acting as a nitric oxide sensor. The precise mechanism on how GAPDH is targeted to these different roles is unclear but believed to involve specific posttranslational modification to the protein. Numerous studies have demonstrated that GAPDH is a target for tyrosine nitration. However, the site of modification and the molecular consequence have not been defined. Rabbit GAPDH with a reversibly protected catalytic cysteine was nitrated in vitro with tetranitromethane, resulting in complete loss of GAPDH catalytic activity. Nitration was estimated as 0.32 mol of nitrotyrosine residue per mole of GAPDH. Mass spectrometry analysis of nitrated GAPDH indicated that Tyr311 and Tyr317 were the sole sites of nitration. The X-ray crystal structure revealed that the distances between Tyr311 and Tyr317 and the cofactor nicotinamide adenine dinucleotide (NAD(+)) were less than 7.2 and 3.7 A, respectively, implying that nitration of these two residues may affect NAD(+) binding. This possibility was assessed using an NAD(+) binding assay, which showed that nitrated GAPDH was incapable of binding NAD(+). Thus, these results strongly suggest that Tyr311 and Tyr317 nitration prohibits NAD(+) binding, leading to the loss of catalytic activity.
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