Mycobacterium tuberculosis sulfurtransferase SseA is activated by its neighboring gene product Rv3284. [PDF]
Tuberculosis remains a global health challenge and new therapeutic targets are required. Here, we characterized SseA, a sulfurtransferase from Mycobacterium tuberculosis involved in macrophage infection, and its interaction with the newly identified protein SufEMtb that activates SseA enzymatic activity.
Di Napoli G +10 more
europepmc +4 more sources
Thiosulfate-cyanide sulfurtransferase a mitochondrial essential enzyme: from cell metabolism to the biotechnological applications [PDF]
Thiosulfate: cyanide sulfurtransferase (TST), also named rhodanese, is an enzyme widely distributed in both prokaryotes and eukaryotes, where it plays a relevant role in mitochondrial function. TST enzyme is involved in several biochemical processes such
Arciero I., Buonvino S., Melino S.
core +5 more sources
Unraveling the role of 3-mercaptopyruvate sulfurtransferase-derived hydrogen sulfide in triple-negative breast cancer chemoresistance [PDF]
BackgroundTriple-negative breast cancer (TNBC) frequently develops resistance to chemotherapy. Cancer-supporting roles of the endogenous gaseous mediator hydrogen sulfide (H2S) have been identified.
Sousanna Hakim +9 more
doaj +2 more sources
Cyanide overproduction impairs cellular bioenergetics in Down syndrome [PDF]
Cyanide exerts its toxic effects primarily by inhibiting mitochondrial Complex IV (Cytochrome c oxidase, CCOx). Recent studies have shown that mammalian cells can endogenously produce cyanide from glycine via a lysosomal pathway.
Maria Petrosino +7 more
doaj +2 more sources
Structural and functional characterization of sulfurtransferase from Frondihabitans sp. PAMC28461. [PDF]
Sulfurtransferases transfer of sulfur atoms from thiols to acceptors like cyanide. They are categorized as thiosulfate sulfurtransferases (TSTs) and 3-mercaptopyruvate sulfurtransferases (MSTs). TSTs transfer sulfur from thiosulfate to cyanide, producing
Hackwon Do +9 more
doaj +2 more sources
Functional potential of archaeal KEGG enzymes in the Moringa oleifera rhizosphere revealed by metagenomic analysis [PDF]
Background Archaea are a major domain of life that inhabit diverse and often extreme environments, contributing to biogeochemical cycles and participating in nutrient cycling within plant rhizospheric soils.
Lina Baz
doaj +2 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 +3 more sources
Discovery of a small molecule allosteric activator of human thiosulfate sulfurtransferase [PDF]
Recent studies showed that thiosulfate sulfurtransferase (TST) is one of the few peripherally expressed genes that has been identified as a genetic risk factor for metabolic health, with clear evidence of a negative correlation with the development of ...
Al Dahmani-Al Zakwani, Zayana
core +2 more sources
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 +2 more sources
Bridging the Gap in Cancer Research: Sulfur Metabolism of Leukemic Cells with a Focus on L-Cysteine Metabolism and Hydrogen Sulfide-Producing Enzymes [PDF]
Leukemias are cancers of the blood-forming system, representing a significant challenge in medical science. The development of leukemia cells involves substantial disturbances within the cellular machinery, offering hope in the search for effective ...
Konrad Kaleta +4 more
doaj +2 more sources

