Inactivation of glucose-6-phosphate dehydrogenase by 4-hydroxy-2-nonenal. Selective modification of an active-site lysine.
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چکیده
منابع مشابه
Selective inactivation of alpha-ketoglutarate dehydrogenase and pyruvate dehydrogenase: reaction of lipoic acid with 4-hydroxy-2-nonenal.
Previous research has established that 4-hydroxy-2-nonenal (HNE), a highly toxic product of lipid peroxidation, is a potent inhibitor of mitochondrial respiration. HNE exerts its effects on respiration by inhibiting alpha-ketoglutarate dehydrogenase (KGDH). Because of the central role of KGDH in metabolism and emerging evidence that free radicals contribute to mitochondrial dysfunction associat...
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The glycolytic enzyme glyceraldehyde-3-phosphate dehydrogenase was irreversibly and (S)-selectively inactivated by the enantiomers of racemic 4-hydroxy-2(E)-nonenal (HNE), a reactive product released from biomembranes by lipid peroxidation in cells. Rates of the enzyme inactivations were 1.7, 3.0, and 6.0 M(-1).s(-1) for (R)-, racemic and (S)-HNEs respectively. In rat liver cytosol the HNE was ...
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Several observations have implicated oxidative stress and aggregation of the presynaptic protein-synuclein in the pathogenesis of PD.-Synuclein has been shown to have affinity for unsaturated fatty acids and membranes enriched in PUFAs, which are especially sensitive to oxidation under conditions of oxidative stress. One of the most important products of lipid oxidation is 4-hydroxynonenal (H...
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The increased glycation of structural proteins in diabetes has been intensely studied. Much less is known of the enzyme glycation. Glucose-6-phosphate dehydrogenase (GPGD) is an enzyme of considerable importance because it catalyses the first reaction in the hexose monophosphate shunt pathway and catalyses the formation of NADPH. The in vitro inactivation of glutathione reductase, p galactosida...
متن کاملModification of Cytochrome c by 4-hydroxy- 2-nonenal: evidence for histidine, lysine, and arginine-aldehyde adducts.
4-Hydroxy-2-nonenal (4HNE), a major secondary product of lipid peroxidation, has been associated with a number of disease states involving oxidative stress. Despite the recognized importance of post-translational modification of proteins by products such as 4HNE, little is known of the modification of cytochrome c by this reagent and its analysis by mass spectrometry. The purpose of this study ...
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ژورنال
عنوان ژورنال: Journal of Biological Chemistry
سال: 1993
ISSN: 0021-9258
DOI: 10.1016/s0021-9258(18)53699-1