Regular ArticleGlyceraldehyde-3-Phosphate Dehydrogenase Inactivation by Peroxynitrite☆
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2021, Free Radical Biology and MedicineCitation Excerpt :Peroxynitrite can directly interact with the transition metal centres of proteins to inhibit their activity, as shown for heme containing proteins Cytochrome C [47] and iNOS [48] or non-heme proteins Aconitase [49] and eNOS [50]. In addition, peroxynitrite can directly modify cysteine by thiol oxidation, such as in several glycolytic [51] and mitochondrial [52] key proteins, which demonstrated the crucial role of peroxynitrite in cell metabolism control. Due to the capacity of peroxynitrite to oxidize low-molecular-weight thiols as GSH, it can be scavenged by this antioxidant molecule and its toxic impact is highly related to intracellular GSH concentration [53].
Formation of protein cross-links by singlet oxygen-mediated disulfide oxidation
2021, Redox BiologyCitation Excerpt :This is a potentially important factor for GAPDH, as Cys149 is known to have a low pKa (5.5–6.0, due to the presence of a nearby His residue that acts as a proton acceptor [65,66]), and is part of the active site of this enzyme. Cys149 has been reported previously to contain an extremely reactive SH-group, and this residue is a major target for oxidative damage [67,68]. Cys 244 is also reported to have a low pKa, though the value is not known, as a result of electrostatic effects and formation of an ion-pair with neighboring basic amino acids [66,69].
Ionizing radiation-induced proteomic oxidation in Escherichia coli
2020, Molecular and Cellular ProteomicsCitation Excerpt :Target theory does not predict such extreme and specific targeting of GAPDH, suggesting that irreversible oxidation of Cys151 may have a biologically significant role downstream of this initial oxidation event. The unusual reactivity of this buried catalytic Cys residue with H2O2 and reactive nitrogen species (RNS) has been extensively documented (53–65, 67, 78–81). However, this study provides the first evidence that GAPDH may be the primary protein target of the oxidizing environment created by acute irradiation.
Short-chain lipid peroxidation products form covalent adducts with pyruvate kinase and inhibit its activity in vitro and in breast cancer cells
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Boyer, P. D.
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