Results 181 to 190 of about 9,691 (231)
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Specificity studies of 3‐mercaptopyruvate sulfurtransferase
Journal of Biochemical Toxicology, 1995Abstract3‐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, 1990The 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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Periódico Tchê Química
Introduction: The global prevalence of type 2 diabetes mellitus (T2DM) continues to rise dramatically, necessitating reconsideration of underlying pathophysiological mechanisms.
Marwa Mustafa Mawajdeh +1 more
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Introduction: The global prevalence of type 2 diabetes mellitus (T2DM) continues to rise dramatically, necessitating reconsideration of underlying pathophysiological mechanisms.
Marwa Mustafa Mawajdeh +1 more
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Role of 3-mercaptopyruvate sulfurtransferase in cancer
Cellular SignallingXue-Li Wang +9 more
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Rhodanese (thiosulfate:cyanide sulfurtransferase) from frog Rana temporaria
Journal of Chromatography B: Biomedical Sciences and Applications, 2000The 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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3-Mercaptopyruvate sulfurtransferase: an enzyme at the crossroads of sulfane sulfur trafficking
Biological chemistry, 20203-Mercaptopyruvate sulfurtransferase (MPST) catalyzes the desulfuration of 3-mercaptopyruvate to generate an enzyme-bound hydropersulfide. Subsequently, MPST transfers the persulfide’s outer sulfur atom to proteins or small molecule acceptors.
B. Pedre, T. Dick
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On the molecular weight of thiosulfate sulfurtransferase
Biochimica et Biophysica Acta (BBA) - Protein Structure, 1975Bovine 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
1987Publisher 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 +3 more
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Circulation Research
Background: Heart failure with preserved ejection fraction (HFpEF) is among the leading causes of cardiovascular mortality and morbidity. Recent multi-omics data sets underscore severely impaired branched-chain amino acid (BCAA) catabolism in the ...
Zhen Li +8 more
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Background: Heart failure with preserved ejection fraction (HFpEF) is among the leading causes of cardiovascular mortality and morbidity. Recent multi-omics data sets underscore severely impaired branched-chain amino acid (BCAA) catabolism in the ...
Zhen Li +8 more
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Rhodanese domain-containing sulfurtransferases
2019Sulfur 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 +3 more
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