Thiosulfate sulfurtransferase deficiency promotes oxidative distress and aberrant NRF2 function in the brain [PDF]
Thiosulfate sulfurtransferase (TST, EC 2.8.1.1) was discovered as an enzyme that detoxifies cyanide by conversion to thiocyanate (rhodanide) using thiosulfate as substrate; this rhodanese activity was subsequently identified to be almost exclusively ...
Yang Luo +11 more
doaj +9 more sources
Thiosulfate sulfurtransferase prevents hyperglycemic damage to the zebrafish pronephros in an experimental model for diabetes [PDF]
Thiosulfate sulfurtransferase (TST, EC 2.8.1.1), also known as Rhodanese, was initially discovered as a cyanide detoxification enzyme. However, it was recently also found to be a genetic predictor of resistance to obesity-related type 2 diabetes ...
Zayana M. Al-Dahmani +12 more
doaj +8 more sources
Identification and characterization of a small molecule that activates thiosulfate sulfurtransferase and stimulates mitochondrial respiration. [PDF]
AbstractThe enzyme Thiosulfate sulfurtransferase (TST, EC 2.8.1.1), is a positive genetic predictor of diabetes type 2 and obesity. As increased TST activity protects against the development of diabetic symptoms in mice, an activating compound for TST may provide therapeutic benefits in diabetes and obesity.
Al-Dahmani ZM +14 more
europepmc +7 more sources
The Role of Thiosulfate Sulfurtransferase in Oxidative Stress for Type 2 Diabetes Mellitus [PDF]
BACKGROUND: Type 2 diabetes mellitus (T2DM) is associated with oxidative stress, leading to insulin resistance. Thiosulfate sulfurtransferase (TST) is mitochondrial enzyme involved in the reaction with cyanide, endogenous hydrogen sulfide (H₂S), and ...
M. M. Mawajdeh, T. A. Allwsh
doaj +3 more sources
Thiosulfate sulfurtransferase-like domain-containing 1 protein interacts with thioredoxin. [PDF]
Rhodanese domains are structural modules present in the sulfurtransferase superfamily. These domains can exist as single units, in tandem repeats, or fused to domains with other activities. Despite their prevalence across species, the specific physiological roles of most sulfurtransferases are not known.
Libiad M +6 more
europepmc +6 more sources
Systemic intracellular analysis for balancing complex biosynthesis in a transcriptionally deregulated Escherichia coli l‐Methionine producer [PDF]
l‐Methionine (l‐Met) has gained remarkable interest due to its multifaceted and versatile applications in the fields of nutrition, pharmaceuticals and clinical practice.
Claudia Harting +4 more
doaj +3 more sources
Transcriptomics of the Anthopleura Sea Anemone Reveals Unique Adaptive Strategies to Shallow‐Water Hydrothermal Vent [PDF]
The nonsymbiotic sea anemone Anthopleura nigrescens dominates the shallow‐water hydrothermal vents off the coast of Kueishan Island, Taiwan. These vents represent some of the world's most extreme environments, with recorded pH values as low as 1.52 and ...
Mei‐Fang Lin +2 more
doaj +3 more sources
Genetic identification of thiosulfate sulfurtransferase as an adipocyte-expressed antidiabetic target in mice selected for leanness. [PDF]
The discovery of genetic mechanisms for resistance to obesity and diabetes may illuminate new therapeutic strategies for the treatment of this global health challenge. We used the polygenic 'lean' mouse model, which has been selected for low adiposity over 60 generations, to identify mitochondrial thiosulfate sulfurtransferase (Tst; also known as ...
Morton NM +32 more
europepmc +9 more sources
Acidity of persulfides and its modulation by the protein environments in sulfide quinone oxidoreductase and thiosulfate sulfurtransferase. [PDF]
Persulfides (RSSH/RSS-) participate in sulfur metabolism and are proposed to transduce hydrogen sulfide (H2S) signaling. Their biochemical properties are poorly understood. Herein, we studied the acidity and nucleophilicity of several low molecular weight persulfides using the alkylating agent, monobromobimane.
Benchoam D +4 more
europepmc +5 more sources
Solution structure of a single-domain thiosulfate sulfurtransferase from Arabidopsis thaliana. [PDF]
AbstractWe describe the three‐dimensional structure of the product of Arabidopsis thaliana gene At5g66040.1 as determined by NMR spectroscopy. This protein is categorized as single‐domain sulfurtransferase and is annotated as a senescence‐associated protein (sen1‐like protein) and ketoconazole resistance protein (http://arabidopsis.org/info/genefamily ...
Cornilescu G +4 more
europepmc +5 more sources

