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Chromogenic and fluorigenic substrates for sulfurtransferases

Methods in Enzymology, 1987
Publisher Summary This chapter discusses the chromogenic and fluorigenic substrates for sulfurtransferases. The enzymes rhodanese (thiosulfate : cyanide sulfurtransferase; thiosulfate sulfurtransferase) and thiosulfate reductase catalyze reactions in which a sulfane sulfur atom is transferred from inorganic thiosulfate anion or other suitable donor ...
John Westley, J Westley
exaly   +3 more sources

On the molecular weight of thiosulfate sulfurtransferase

Biochimica et Biophysica Acta (BBA) - Protein Structure, 1975
Bovine liver thiosulfate sulfurtransferase (rhodanese) (EC 2.8.1.1) HAS BEEN REPORTED TO EXIST IN SOLUTION IN A RAPID, PH-dependent equilibrium between monomeric and dimeric forms of molecular weights 18 500 and 37 000 (Volini, M., DeToma, F. and Westley, J. (1967), J. Biol. Chem. 242, 5220).
L M, Ellis, C K, Woodward
openaire   +2 more sources

A physical characterization of sulfane sulfurtransferase

Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology, 1990
The bacterial enzyme sulfane sulfurtransferase has been studied using spectroscopic techniques. The enzyme was characterized in terms of its near-UV absorption spectrum, molar ellipticity, intrinsic fluorescence spectra and the effects of general and ionic quenching reagents upon its fluorescence.
B A, Aird, P M, Horowitz
openaire   +2 more sources

Biosynthesis of Chuangxinmycin Featuring a Deubiquitinase‐like Sulfurtransferase

Angewandte Chemie, 2021
AbstractThe knowledge on sulfur incorporation mechanism involved in sulfur‐containing molecule biosynthesis remains limited. Chuangxinmycin is a sulfur‐containing antibiotic with a unique thiopyrano[4,3,2‐cd]indole (TPI) skeleton and selective inhibitory activity against bacterial tryptophanyl‐tRNA synthetase.
Xingwang Zhang   +18 more
openaire   +2 more sources

Specificity studies of 3‐mercaptopyruvate sulfurtransferase

Journal of Biochemical Toxicology, 1995
Abstract3‐Mercaptopyruvate sulfurtransferase (E.C. 2.8.1.2; MST) is an enzyme believed to function in the endogenous cyanide (CN) detoxification system because it is capable of transferring sulfur from 3‐mercaptopyruvate (3‐MP) to CN, forming the less toxic thiocyanate (SCN). To date, 3‐MP is the only known sulfur‐donor substrate for MST.
D W, Porter, S I, Baskin
openaire   +2 more sources

Methods for in situ visualization and assay of sulfurtransferases

Analytical Biochemistry, 1987
The dansyl derivative 5-dimethylamino-1-naphthalene thiosulfonate (DANTS) can serve as a sulfane sulfur-donor substrate for several of the sulfurtransferases, the reaction being dependent on the acceptor substrates supplied. Enzymatic cleavage of the sulfur-sulfur bond of DANTS releases the intrinsic fluorescence of the molecule, with an emission ...
B A, Aird, J, Lane, J, Westley
openaire   +2 more sources

The presence of an inhibitor of tRNA sulfurtransferase in Morris hepatomas

Biochemical and Biophysical Research Communications, 1975
Summary A tRNA sulfurtransferase has been isolated from the 160, 000 g supernatant of Buffalo rat liver and a number of Morris hepatomas. This enzyme catalyzes the transfer of labeled sulfur from [36S]β-mercaptopyruvate to tRNA in the presence of ATP and magnesium ion.
T W, Wong, M A, Harris, H P, Morris
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Encapsulation of thiosulfate: Cyanide sulfurtransferase by mouse erythrocytes

Toxicology and Applied Pharmacology, 1986
Murine carrier erythrocytes, prepared by hypotonic dialysis, were employed in the encapsulation of several compounds including [14C]sucrose, [3H]inulin, and bovine thiosulfate:cyanide sulfurtransferase (rhodanese), a mitochondrial enzyme which converts cyanide to thiocyanate.
P, Leung   +5 more
openaire   +2 more sources

Role of 3-mercaptopyruvate sulfurtransferase in cancer

Cellular Signalling
The enzyme 3-mercaptopyruvate sulfurtransferase (3-MST) is widely distributed across different biological entities and is essential for the production of hydrogen sulfide (H₂S). This enzyme functions both in the cytosol and mitochondria, and 3-MST mediates the reaction of 3-mercaptopyruvate (3-MP) with dihydrolipoic acid and thioredoxin to generate ...
Xue-Li, Wang   +9 more
openaire   +2 more sources

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