ArticleOxidative medicine and cellular longevity2013
Thiol redox sensitivity of two key enzymes of heme biosynthesis and pentose phosphate pathways: uroporphyrinogen decarboxylase and transketolase.
Article in Oxidative medicine and cellular longevity, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.
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Who cites it
11 citing papers in PubMed, 18 citations in OpenAlex.
- Molecular Mechanisms of Iron Metabolism and Overload.Biomedicines · 2025Review
- The interactome of the Bakers' yeast peroxiredoxin Tsa1 implicates it in redox regulation of intermediary metabolism, glycolysis, and zinc homeostasis.Metallomics : integrated biometal science · 2025Article
- Activation of Purine Biosynthesis Suppresses the Sensitivity ofInternational journal of molecular sciences · 2023Article
- New Avenues of Heme Synthesis Regulation.International journal of molecular sciences · 2022Review
- Ferrochelatase: Mapping the Intersection of Iron and Porphyrin Metabolism in the Mitochondria.Frontiers in cell and developmental biology · 2022Review
- Oxoisoaporphines and Aporphines: Versatile Molecules with Anticancer Effects.Molecules (Basel, Switzerland) · 2019Review
- Thioredoxin and glutaredoxin regulate metabolism through different multiplex thiol switches.Redox biology · 2019Article
- A comparison of the transcriptomes between diploid and autotetraploidPhysiology and molecular biology of plants : an international journal of functional plant biology · 2019Article
- Differential regulation of cysteine oxidative post-translational modifications in high and low aerobic capacity.Scientific reports · 2018Article
- Comparison of Whole Body SOD1 Knockout with Muscle-Specific SOD1 Knockout Mice Reveals a Role for Nerve Redox Signaling in Regulation of Degenerative Pathways in Skeletal Muscle.Antioxidants & redox signaling · 2018Article
- Redox regulation of metabolic and signaling pathways by thioredoxin and glutaredoxin in NOS-3 overexpressing hepatoblastoma cells.Redox biology · 2015Article
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4 authors at 3 institutions in 2 countries.
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Abstract
Uroporphyrinogen decarboxylase (Hem12p) and transketolase (Tkl1p) are key mediators of two critical processes within the cell, heme biosynthesis, and the nonoxidative part of the pentose phosphate pathway (PPP). The redox properties of both Hem12p and Tkl1p from Saccharomyces cerevisiae were investigated using proteomic techniques (SRM and label-free quantification) and biochemical assays in cell extracts and in vitro with recombinant proteins. The in vivo analysis revealed an increase in oxidized Cys-peptides in the absence of Grx2p, and also after treatment with H2O2 in the case of Tkl1p, without corresponding changes in total protein, demonstrating a true redox response. Out of three detectable Cys residues in Hem12p, only the conserved residue Cys52 could be modified by glutathione and efficiently deglutathionylated by Grx2p, suggesting a possible redox control mechanism for heme biosynthesis. On the other hand, Tkl1p activity was sensitive to thiol redox modification and although Cys622 could be glutathionylated to a limited extent, it was not a natural substrate of Grx2p. The human orthologues of both enzymes have been involved in certain cancers and possess Cys residues equivalent to those identified as redox sensitive in yeast. The possible implication for redox regulation in the context of tumour progression is put forward.
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