Results 131 to 140 of about 3,761 (182)

Mycobacterium tuberculosis sulfurtransferase SseA is activated by its neighboring gene product Rv3284. [PDF]

FEBS Lett
Di Napoli G, Fissore A, Salladini E, Raccuia E, Oliaro-Bosso S, Ruggiero A, Berisio R, Medina M, Velazquez-Campoy A, Adinolfi S, Marengo M.   +10 more
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Draft genome sequence of <i>Dongia</i> sp. strain agr-C8, isolated from the rhizosphere of <i>Phragmites australis</i> using a droplet-based cultivation method. [PDF]

Microbiol Resour Announc
Iwashita T, Kanno M, Ota Y, Matsukura S, Morita M, Sasaki A, Noda N, Nishioka T, Hirakata Y, Tamaki H.   +9 more
europepmc   +1 more source

The Impact of Endogenous Hydrogen Sulfide on Bacterial Resistance. [PDF]

Infect Drug Resist
Liu J, Qi Y, Xiao X, Zhang Y.
europepmc   +1 more source

Hydrogen sulfide ameliorates peritoneal fibrosis: inhibition of high mobility group box-1 expression to block the activation of the transforming growth factor-beta/Smad3 pathway. [PDF]

Med Gas Res
Liu L, Huang W, Ming J, Cai F, Wang H, Lai X, Guo Z.   +6 more
europepmc   +1 more source

Clonal Stabilization Reveals a DAO/3MST-Expressing MDCK Subpopulation With Robust d-Cysteine-Mediated H₂S Production. [PDF]

FASEB J
Miyamoto A, Ueno H, Kimura H, Nakagawa T, Shibuya N.   +4 more
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
openaire   +2 more sources

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
openaire   +2 more sources

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
openaire   +2 more sources