Results 11 to 20 of about 2,505 (224)

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

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   +4 more sources

Catalytic Site Cysteines of Thiol Enzyme: Sulfurtransferases [PDF]

open access: yesJournal of Amino Acids, 2011
Thiol enzymes have single- or double-catalytic site cysteine residues and are redox active. Oxidoreductases and isomerases contain double-catalytic site cysteine residues, which are oxidized to a disulfide via a sulfenyl intermediate and reduced to a ...
Nagahara, Noriyuki
core   +7 more sources

Plant mercaptopyruvate sulfurtransferases [PDF]

open access: bronzeEuropean Journal of Biochemistry, 2000
Mercaptopyruvate sulfurtransferase (MST, EC 2.8.1.2) and thiosulfate sulfurtransferase (TST, rhodanese, EC 2.8.1.1) are evolutionarily related enzymes that catalyze the transfer of sulfur ions from mercaptopyruvate and thiosulfate, respectively, to cyanide ions.
Tatsuo Nakamura   +2 more
semanticscholar   +5 more sources

The Expression and Activity of Rhodanese, 3-Mercaptopyruvate Sulfurtransferase, Cystathionine γ-Lyase in the Most Frequently Chosen Cellular Research Models [PDF]

open access: yesBiomolecules, 2021
This paper provides information concerning the activity and expression levels of three sulfurtransferases (STRs): rhodanese (TST, EC: 2.8.1.1), 3-mercaptopyruvate sulfurtransferase (MPST, EC: 2.8.1.2) and cystathionine γ-lyase (CTH, EC: 4.4.1.1) in ...
Marta Kaczor-Kamińska   +2 more
doaj   +2 more sources

Structural and functional characterization of sulfurtransferase from Frondihabitans sp. PAMC28461. [PDF]

open access: yesPLoS ONE
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

Enzymatic activity of the Arabidopsis sulfurtransferase resides in the C-terminal domain but is boosted by the N-terminal domain and the linker peptide in the full-length enzyme [PDF]

open access: green, 2005
Sulfurtransferases/rhodaneses are a group of enzymes widely distributed in plants, animals, and bacteria that catalyze the transfer of sulfur from a donor molecule to a thiophilic acceptor substrate.
Burow, M.   +2 more
core   +4 more sources

Oxidative Stress and Iron Addiction: A Comparative Study of 1321N1 Astrocytoma and T98G Glioblastoma Cells with Differential Expression of L-Cysteine-Metabolizing Enzymes [PDF]

open access: yesBiomolecules
Gliomas are central nervous system primary tumors that are distinguished by heterogeneity, broad-based infiltration, and metabolic reprogramming that sustains proliferation, invasion, and therapy refractoriness.
Halina Jurkowska   +5 more
doaj   +2 more sources

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

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

Changes in activity of three sulfurtransferases in response to exposure to cadmium, lead and mercury ions [PDF]

open access: yes, 2013
Cadmium, lead and mercury are environmentally persistent toxicants that affect tissues and cellular components or exert an effect on generation of reactive oxygen species causing a decreased level of available antioxidant reserves. Sulfurtransferases are
Kaczor-Kamińska, Marta   +2 more
core   +2 more sources

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