Results 11 to 20 of about 3,023 (198)

Acidity of persulfides and its modulation by the protein environments in sulfide quinone oxidoreductase and thiosulfate sulfurtransferase. [PDF]

J Biol Chem
Persulfides (RSSH/RSS-) participate in sulfur metabolism and are proposed to transduce hydrogen sulfide (H2S) signaling. Their biochemical properties are poorly understood. Herein, we studied the acidity and nucleophilicity of several low molecular weight persulfides using the alkylating agent, monobromobimane.
Benchoam D, Cuevasanta E, Roman JV, Banerjee R, Alvarez B.   +4 more
europepmc   +4 more sources

Systemic intracellular analysis for balancing complex biosynthesis in a transcriptionally deregulated Escherichia coli l-Methionine producer. [PDF]

Microb Biotechnol
Metabolomic analysis revealed potential bottlenecks in the complex methionine biosynthesis of an E. coli producer strain. A genetic engineering strategy was designed to overcome these bottlenecks. Abstract l‐Methionine (l‐Met) has gained remarkable interest due to its multifaceted and versatile applications in the fields of nutrition, pharmaceuticals ...
Harting C, Teleki A, Braakmann M, Jankowitsch F, Takors R.   +4 more
europepmc   +3 more sources

Solution structure of a single-domain thiosulfate sulfurtransferase from Arabidopsis thaliana. [PDF]

Protein Sci, 2006
AbstractWe describe the three‐dimensional structure of the product of Arabidopsis thaliana gene At5g66040.1 as determined by NMR spectroscopy. This protein is categorized as single‐domain sulfurtransferase and is annotated as a senescence‐associated protein (sen1‐like protein) and ketoconazole resistance protein (http://arabidopsis.org/info/genefamily ...
Cornilescu G, Vinarov DA, Tyler EM, Markley JL, Cornilescu CC.   +4 more
europepmc   +7 more sources

CoQ deficiency causes disruption of mitochondrial sulfide oxidation, a new pathomechanism associated with this syndrome [PDF]

EMBO Molecular Medicine, 2017
Coenzyme Q (CoQ) is a key component of the mitochondrial respiratory chain, but it also has several other functions in the cellular metabolism. One of them is to function as an electron carrier in the reaction catalyzed by sulfide:quinone oxidoreductase (
Agustín Hidalgo‐Gutiérrez, Ashby MN, Darío Acuña‐Castroviejo, Eliana Barriocanal‐Casado, Felix Distelmaier, Germaine Escames, Holger Prokisch, Juan Duarte, Julio Chaves‐Serrano, Luis C López, Markus Schuelke, Marta Luna‐Sánchez, Miguel Romero, Ramy KA Sayed, Tatjana M Hildebrandt, Ángela Santos‐Fandila   +15 more
core   +5 more sources

H$_{2}$S, polysulfides, and enzymes : physiological and pathological aspec [PDF]

Biomolecules, 2020
We have been studying the general aspects of the functions of H$_{2}$S and polysulfides, and the enzymes involved in their biosynthesis, for more than 20 years.
Noriyuki Nagahara
core   +3 more sources

Mycobacterium tuberculosis CysA2 is a dual sulfurtransferase with activity against thiosulfate and 3-mercaptopyruvate and interacts with mammalian cells [PDF]

Scientific Reports, 2019
AbstractCyanide is a toxic compound that is converted to the non-toxic thiocyanate by a rhodanese enzyme. Rhodaneses belong to the family of transferases (sulfurtransferases), which are largely studied. The sulfur donor defines the subfamily of these enzymes as thiosulfate:cyanide sulfurtransferases or rhodaneses (TSTs) or 3-mercaptopyruvate ...
Ana Carolina Ramos Moreno, C. C. N. Cambui, Andrea Balan, Melissa Regina Fessel, A. N. Meza, A. N. Meza   +5 more
openaire   +4 more sources

Rhodanese (thiosulfate: cyanide sulfurtransferase) in the digestive tract of chicken at different stages of development

Poultry Science, 1997
This study was undertaken to investigate the relationships between stage of embryonic development and early posthatch growth and the level of rhodanese (thiosulfate:cyanide sulfurtransferase) activity in different regions of the digestive tract and liver of chickens. The embryos were studied at 14, 17, and 20 d and chickens were 1, 2, and 3 wk old. All
Mahmoud Aminlari, A Azarafrooz, Soghra Gholami, Taleb Vaseghi   +3 more
openaire   +4 more sources

Studies of functionally important structural flexibility of thiosulfate sulfurtransferase

Biophysical Journal, 1980
The enzyme thiosulfate sulfurtransferase (TST; rhodanese; EC 2.8.1.1) catalyzes the transfer of the outer sulfur of thiosulfate (S/sub 2/O/sub 3//sup - -/) to a variety of nucleophilic acceptors such as cyanide (CN/sup -/). During the course of this reaction the enzyme cycles through two stable isolatable catalytic intermediates: the free enzyme, (E ...
Paul M. Horowitz
openaire   +4 more sources

Role of hydrogen sulfide in health and disease. [PDF]

MedComm (2020)
Abstract In the past, hydrogen sulfide (H2S) was recognized as a toxic and dangerous gas; in recent years, with increased research, we have discovered that H2S can act as an endogenous regulatory transmitter. In mammals, H2S‐catalyzing enzymes, such as cystathionine‐β‐synthase, cystathionine‐γ‐lyase, and 3‐mercaptopyruvate sulfurtransferase, are ...
Jin YQ, Yuan H, Liu YF, Zhu YW, Wang Y, Liang XY, Gao W, Ren ZG, Ji XY, Wu DD.   +9 more
europepmc   +2 more sources

The Putative Thiosulfate Sulfurtransferases PspE and GlpE Contribute to Virulence of Salmonella Typhimurium in the Mouse Model of Systemic Disease [PDF]

PLoS ONE, 2013
The phage-shock protein PspE and GlpE of the glycerol 3-phosphate regulon of Salmonella enterica serovar Typhimurium are predicted to belong to the class of thiosulfate sulfurtransferases, enzymes that traffic sulfur between molecules. In the present study we demonstrated that the two genes contribute to S.
Wallrodt, Inke, Jelsbak, Lotte, Thorndahl, Lotte, Thomsen, Line Elnif, Lemire, Sebastien, Olsen, John Elmerdahl   +5 more
openaire   +8 more sources