Results 151 to 160 of about 3,733 (181)

Hydrogen Sulfide Metabolism in the Skin: From Physiology to Malignancy. [PDF]

Int J Mol Sci
Tampa M, Nicolae I, Mitran MI, Mitran CI, Matei C, Georgescu SR, Capusa C, Ene CD.   +7 more
europepmc   +1 more source

Tissue-specific molecular regulation of aging mechanisms with methionine restriction in mice and the potential role of methionine sulfoxide reductase. [PDF]

J Gerontol A Biol Sci Med Sci
Thyne KM, Camones R, Salmon AB.
europepmc   +1 more source

Gasotransmitter signaling in the brain: New frontiers for therapeutics. [PDF]

Neurotherapeutics
Paul BD, Ignarro LJ, Lipton SA.
europepmc   +1 more source

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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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Steady-state kinetics of 3-mercaptopyruvate sulfurtransferase from bovine kidney

Archives of Biochemistry and Biophysics, 1978
Abstract Mammalian 3-mercaptopyruvate sulfurtransferase (EC 2.8.1.2), purified to apparent homogeneity by a new procedure, was studied by steady-state kinetic methods. The enzyme-catalyzed transfer of a sulfur atom from 3-mercaptopyruvate either to 2-mercaptoethanol or to a second molecule of 3-mercaptopyruvate was found to proceed by a sequential ...
R, Jarabak, J, Westley
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Vascular Endothelium Expresses 3-Mercaptopyruvate Sulfurtransferase and Produces Hydrogen Sulfide

Journal of Biochemistry, 2009
Hydrogen sulfide (H(2)S) has been recognized as a smooth muscle relaxant. Cystathionine gamma-lyase, which is localized to smooth muscle, is thought to be the major H(2)S-producing enzyme in the thoracic aorta. Here we show that 3-mercaptopyruvate sulfurtransferase (3MST) and cysteine aminotransferase (CAT) are localized to vascular endothelium in the ...
Norihiro, Shibuya, Yoshinori, Mikami, Yuka, Kimura, Noriyuki, Nagahara, Hideo, Kimura   +4 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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The effect of three α-keto acids on 3-mercaptopyruvate sulfurtransferase activity

Journal of Biochemical Toxicology, 1996
3-Mercaptopyruvate sulfurtransferase catalyzes the transfer of sulfur from 3-mercaptopyruvate to several possible acceptor molecules, one of which is cyanide. Because the transsulfuration of cyanide is the primary in vivo mechanism of detoxification, 3-mercaptopyruvate sulfurtransferase may function in the enzymatic detoxification of cyanide in vivo ...
D W, Porter, S I, Baskin
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Functional Analysis of 3-Mercaptopyruvate Sulfurtransferase Using Knockout Mice

Advanced Techniques in Biology & Medicine, 2015
3-mercaptopyruvate sulfurtransferase (MST) transfers sulfur from 3-mercaptopyruvate (3MP) or thiosulfate to a sulfur acceptor. We developed MST-knockout (MST-KO) mice to clarify the physiological role of MST. They showed increased anxiety-like behaviors.
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