Results 11 to 20 of about 840 (125)

The Human Mercaptopyruvate Sulfurtransferase TUM1 Is Involved in Moco Biosynthesis, Cytosolic tRNA Thiolation and Cellular Bioenergetics in Human Embryonic Kidney Cells [PDF]

open access: yesBiomolecules, 2023
Sulfur is an important element that is incorporated into many biomolecules in humans. The incorporation and transfer of sulfur into biomolecules is, however, facilitated by a series of different sulfurtransferases.
Moses Olalekan Ogunkola   +3 more
doaj   +4 more sources

Insights into the Versatile Sulfur Metabolism of Sulfurovum sp. MH2-6 Isolated from Deep-Sea Hydrothermal Vent Environments [PDF]

open access: yesMicroorganisms
In deep-sea hydrothermal ecosystems, inorganic sulfur compounds serve as key energy sources for microbes through oxidation, reduction, or disproportionation reactions.
Liang Cui   +5 more
doaj   +2 more sources

Cytoplasmic sulfurtransferases in the purple sulfur bacterium Allochromatium vinosum: evidence for sulfur transfer from DsrEFH to DsrC. [PDF]

open access: yesPLoS ONE, 2012
While the importance of sulfur transfer reactions is well established for a number of biosynthetic pathways, evidence has only started to emerge that sulfurtransferases may also be major players in sulfur-based microbial energy metabolism.
Yvonne Stockdreher   +5 more
doaj   +2 more sources

The putative thiosulfate sulfurtransferases PspE and GlpE contribute to virulence of Salmonella Typhimurium in the mouse model of systemic disease. [PDF]

open access: yesPLoS ONE, 2013
The phage-shock protein PspE and GlpE of the glycerol 3-phosphate regulon of Salmonella enterica serovar Typhimurium are predicted to belong to the class of thiosulfate sulfurtransferases, enzymes that traffic sulfur between molecules.
Inke Wallrodt   +5 more
doaj   +2 more sources

Recent Advances in Our Understanding of the Biosynthesis of Sulfur Modifications in tRNAs [PDF]

open access: yesFrontiers in Microbiology, 2018
Sulfur is an essential element in all living organisms. In tRNA molecules, there are many sulfur-containing nucleosides, introduced post-transcriptionally, that function to ensure proper codon recognition or stabilization of tRNA structure, thereby ...
Naoki Shigi
doaj   +2 more sources

Possible Roles of Plant Sulfurtransferases in Detoxification of Cyanide, Reactive Oxygen Species, Selected Heavy Metals and Arsenate [PDF]

open access: yesMolecules, 2015
Plants and animals have evolved various potential mechanisms to surmount the adverse effects of heavy metal toxicity. Plants possess low molecular weight compounds containing sulfhydryl groups (-SH) that actively react with toxic metals.
Parvin Most, Jutta Papenbrock
doaj   +2 more sources

Multidirectional Changes in Parameters Related to Sulfur Metabolism in Frog Tissues Exposed to Heavy Metal-Related Stress

open access: yesBiomolecules, 2020
The investigations showed changes of the cystathionine γ-lyase (CTH), 3-mercaptopyruvate sulfurtransferase (MPST) and rhodanese (TST) activity and gene expression in the brain, heart, liver, kidney, skeletal muscles and testes in frogs Pelophylax ...
Marta Kaczor-Kamińska   +2 more
doaj   +1 more source

Evaluation of the activity of cyanide-metabolizing sulfurtransferase enzymes in different tissues of turkey (Meleagris gallopavo) [PDF]

open access: yesThe Iranian Journal of Veterinary Science and Technology, 2015
This study was undertaken to estimate specific activities of rhodanese and 3-mercaptopyruvate sulfurtransferase (MST) in different tissues of turkey.
Kamal JalilianKabiri, Hassan Baghishani
doaj   +1 more source

The crystal structure of Leishmania major 3-mercaptopyruvate sulfurtransferase : A three-domain architecture with a serine protease-like triad at the active site

open access: yes, 2003
Leishmania major 3-mercaptopyruvate sulfurtransferase is a crescent-shaped molecule comprising three domains. The N-terminal and central domains are similar to the thiosulfate sulfurtransferase rhodanese and create the active site containing a ...
Williams, Roderick   +9 more
core   +3 more sources

The "Rhodanese" fold and catalytic mechanism of 3-mercaptopyruvate sulfurtransferases: Crystal structure of SseA from Escherichia coli

open access: yes, 2004
3-Mercaptopyruvate sulfurtransferases (MSTs) catalyze, in vitro, the transfer of a sulfur atom from substrate to cyanide, yielding pyruvate and thiocyanate as products.
BORDO D.   +6 more
core   +3 more sources

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