Results 131 to 140 of about 1,145 (168)

Chromogenic substrates for sulfurtransferases

Analytical Biochemistry, 1985
The azo dye 4-(dimethylamino)-4'-azobenzene (DAB) thiosulfonate anion can serve as a sulfur-donor substrate for rhodanese (thiosulfate: cyanide sulfurtransferase, EC 2.8.1.1) and for thiosulfate reductase (EC unassigned) with cyanide anion and GSH, respectively, as acceptor substrates.
M R, Burrous, J, Westley
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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, Xiaokun Xu, Cai You, Chaofan Yang, Jiawei Guo, Moli Sang, Ce Geng, Fangyuan Cheng, Lei Du, Yuemao Shen, Sheng Wang, Haidong Lan, Fan Yang, Yuezhong Li, Ya‐Jie Tang, Youming Zhang, Xiaoying Bian, Shengying Li, Wei Zhang   +18 more
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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
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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
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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
M, Wróbel, J, Czubak
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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
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Chromogenic and fluorigenic substrates for sulfurtransferases

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 ...
M R, Burrous, J, Lane, A, Westley, J, Westley   +3 more
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Rhodanese domain-containing sulfurtransferases

2019
Sulfur is an essential element for the growth and development of plants, which synthesize cysteine and methionine from the reductive assimilation of sulfate. Besides its incorporation into proteins, cysteine is the building block for the biosynthesis of numerous sulfur-containing molecules and cofactors.
Selles, Benjamin, Moseler, Anna-Maria, Rouhier, Nicolas, Couturier, Jérémy   +3 more
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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 ...
Noriyuki, Nagahara, Masatoshi, Nagano, Takaaki, Ito, Hidenori, Suzuki   +3 more
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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, L E, Ray, C, Sander, J L, Way, D M, Sylvester, J L, Way   +5 more
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