Results 11 to 20 of about 1,145 (168)

Complete genome sequence of Priestia megaterium S188, a hydrogen sulfide-degrading bacterium [PDF]

open access: yesJournal of Animal Science and Technology
Priestia megaterium (formerly Bacillus megaterium) is a gram-positive, aerobic, spore-forming bacterium found in a wide range of environmental niches. Here, we report the complete genome sequence of P.
Sang Hoon Kim   +3 more
doaj   +2 more sources

The putative thiosulfate sulfurtransferases PspE and GlpE contribute to virulence of Salmonella Typhimurium in the mouse model of systemic disease. [PDF]

open access: yesPLoS 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.
Inke Wallrodt   +5 more
doaj   +5 more sources

Clonal Stabilization Reveals a DAO/3MST-Expressing MDCK Subpopulation With Robust d-Cysteine-Mediated H<sub>2</sub>S Production. [PDF]

open access: yesFASEB J
A subpopulation of MDCK (NBL‐2) cells, an epithelial cell line derived from the normal kidney, expresses DAO and 3MST. The DAO/3MST‐expressing cells are progressively eliminated during passaging; however, clonal isolation enables the establishment of sublines that maintain stable H2S production. Clonal cells co‐expressing DAO and 3MST therefore provide
Miyamoto A   +4 more
europepmc   +2 more sources

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

open access: yesFEBS Lett
Tuberculosis remains a global health challenge and new therapeutic targets are required. Here, we characterized SseA, a sulfurtransferase from Mycobacterium tuberculosis involved in macrophage infection, and its interaction with the newly identified protein SufEMtb that activates SseA enzymatic activity.
Di Napoli G   +10 more
europepmc   +2 more sources

Evaluation of the activity of cyanide-metabolizing sulfurtransferase enzymes in different tissues of turkey (Meleagris gallopavo) [PDF]

open access: yesThe Iranian Journal of Veterinary Science and Technology, 2015
This study was undertaken to estimate specific activities of rhodanese and 3-mercaptopyruvate sulfurtransferase (MST) in different tissues of turkey.
Kamal JalilianKabiri, Hassan Baghishani
doaj   +1 more source

Cytoplasmic sulfurtransferases in the purple sulfur bacterium Allochromatium vinosum: evidence for sulfur transfer from DsrEFH to DsrC. [PDF]

open access: yesPLoS ONE, 2012
While the importance of sulfur transfer reactions is well established for a number of biosynthetic pathways, evidence has only started to emerge that sulfurtransferases may also be major players in sulfur-based microbial energy metabolism.
Yvonne Stockdreher   +5 more
doaj   +1 more source

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

open access: yes, 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 (
Barriocanal-Casado, Eliana   +5 more
core   +4 more sources

Involvement of the Azotobacter vinelandii Rhodanese-Like Protein RhdA in the Glutathione Regeneration Pathway [PDF]

open access: yes, 2012
The phenotypic features of the Azotobacter vinelandii RhdA mutant MV474 (in which the rhdA gene was deleted) indicated that defects in antioxidant systems in this organism were related to the expression of the tandem-domain rhodanese RhdA.
Forlani, Fabio   +5 more
core   +4 more sources

The β-cyanoalanine pathway is involved in the response to water deficit in Arabidopsis thaliana. [PDF]

open access: yes, 2013
The β-cyanoalanine pathway is primarily responsible for detoxification of excess cyanide produced by plants. Recent evidence suggests that cyanide detoxification via this pathway may be involved in the response and tolerance to water deficit in plants ...
Ebbs, Stephen   +3 more
core   +2 more sources

Enzymatic activity of the Arabidopsis sulfurtransferase resides in the C-terminal domain but is boosted by the N-terminal domain and the linker peptide in the full-length enzyme [PDF]

open access: yes, 2005
Sulfurtransferases/rhodaneses are a group of enzymes widely distributed in plants, animals, and bacteria that catalyze the transfer of sulfur from a donor molecule to a thiophilic acceptor substrate.
Burow, M.   +2 more
core   +2 more sources

Home - About - Disclaimer - Privacy