Results 181 to 190 of about 2,387 (211)

Redox Regulation of Mammalian 3-Mercaptopyruvate Sulfurtransferase

2015
A cystine-catabolizing enzyme, 3-mercaptopyruvate sulfurtransferase catalyzes the trans-sulfuration reaction of mercaptopyruvate or thiosulfate to thiol-containing compounds or cyanide. During the catalytic process, persulfide is formed at the catalytic site cysteine residue and a sulfur-acceptor substrate donates the outer sulfur of the persulfide to ...
Hidenori Suzuki, Noriyuki Nagahara, Masatoshi Nagano, Takaaki Ito   +3 more
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Dose and Time-Dependent Effects of Cyanide on Thiosulfate Sulfurtransferase, 3-Mercaptopyruvate Sulfurtransferase, and Cystathionine λ-Lyase Activities

Journal of Biochemical and Molecular Toxicology, 2013
We assessed the dose-dependent effect of potassium cyanide (KCN) on thiosulfate sulfurtransferase (TST), 3-mercaptopyruvate sulfurtransferase (3-MPST), and cystathionine λ-lyase (CST) activities in mice. The time-dependent effect of 0.5 LD50 KCN on cyanide level and cytochrome c oxidase (CCO), TST, 3-MPST, and CST activities was also examined ...
Pooja Rao, Poonam Singh, Rahul Bhattacharya   +2 more
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[37] Thiosulfate: Cyanide sulfurtransferase (Rhodanese)

1981
Publisher Summary This chapter presents a procedure for the preparation of cyanide sulfurtransferase, which was discovered as the result of a search for the active principle in the tissues of animals known to be able to convert cyanide to the less toxic thiocyanate. The thiocyanate product is determined calorimetrically as its red complex with Fe(III)
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Thiosulfate sulfurtransferase (rhodanese) in forest soils

Folia Microbiologica, 1987
Concentrations of thiosulfate sulfurtransferase (rhodanese; EC 2.8.1.1) in soils of five types of forest stands (spruce and pine stands without ground vegetation, and mountain ash, birch and pine stands with grass cover) were followed. Soils from grassed stands contained much higher concentrations of the enzyme than soils without ground vegetation.
openaire   +2 more sources

Identification and characterization of a multi-domain sulfurtransferase in Phanerochaete chrysosporium

Biotechnology Letters, 2014
A sulfurtransferase gene (PcSft) with a coding region of 546 bp was cloned from the filamentous white-rot fungus Phanerochaere chrysosporium. The 181-amino acid protein contains a highly conserved "Rhodanese-like" domain and an ATP-binding site, with a molecular weight of 20.68 kDa. Semi-quantitative RT-PCR showed that the selective expression of PcSft
Yizheng Zhang, Zhongshan Wang, Quanju Xiang, Guangjun Wang, Haiyan Wang   +4 more
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Identity of β-mercaptopyruvate sulfurtransferase and rhodanese in human erythrocytes

Biochemical and Biophysical Research Communications, 1980
Summary Rhodanese and β-mercaptopyruvate sulfurtransferase activities as demonstrated after electrophoresis of human hemolyzates were the product of the same gene. The two activities of this enzyme were purified together and rhodanese activity was found to be a minor function of erythrocytic β-mercaptopyruvate sulfurtransferase.
Edward M. Scott, Rita C. Wright
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Characterization of the sulfurtransferase family from Oryza sativa L

Plant Physiology and Biochemistry, 2011
Sulfurtransferases (Str) comprise a group of enzymes widely distributed in archaea, eubacteria, and eukaryota which catalyze the transfer of a sulfur atom from suitable sulfur donors to nucleophilic sulfur acceptors. Neither the in vivo sulfur donors nor the acceptors of Str could be clearly identified in any of the organisms investigated so far.
Jutta Papenbrock, Sebastian Guretzki
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[38] 3-Mercaptopyruvate sulfurtransferase

1981
Publisher Summary 3-Mercaptopyruvate sulfurtransferase catalyzes the cleavage of a carbon–sulfur bond and the transfer of the sulfur atom from 3-mercaptopyruvate to any of a variety of thiophiles, including thiols, cyanide, sulfite, and sulfinates. This chapter deals with the purification of the 3-mercaptopyruvate sulfurtransferase from the bovine ...
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Rhodanese (thiosulfate:cyanide sulfurtransferase) from frog Rana temporaria

Journal of Chromatography B: Biomedical Sciences and Applications, 2000
The molecular mass of rhodanese from the mitochondrial fraction of frog Rana temporaria liver, equaling 8.7 kDa, was determined by high-performance size exclusion chromatography (HP-SEC). The considerable difference in molecular weight and the lack of common antigenic determinants between frog liver rhodanese and bovine rhodanese suggest the occurrence
Jerzy Czubak, Maria Wróbel
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sulfurtransferases

Catalysis from A to Z, 2020
X. Brannmjk
semanticscholar   +1 more source