Rhodanese as a thioredoxin oxidase

Nandi, Dhirendra L.; Horowitz, Paul M.; Westley, John

doi:10.1016/s1357-2725(99)00035-7

Cited by 110 publications

(90 citation statements)

References 25 publications

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“…These data together suggest that the leishmanial MST is a cytosolic enzyme. This is consistent with analysis using PSORT, 4 which indicated that the leishmanial sulfurtransferases lack any characteristic mitochondrial or other targeting sequence.…”

Section: Table I Activities Of Recombinant Lmajmst and Lmexmstsupporting

confidence: 88%

“…doxin reductase, and 5 g T. vaginalis thioredoxin 2 in 0.1 M phosphate buffer, pH 7.0, was incubated at 37°C for 5 min. A constant absorbance, as reported by Nandi et al (4), was not achieved, as the thioredoxin reductase-thioredoxin system used has a low NADPH oxidase activity. 2 0.1 g of recombinant sulfurtransferase was added, and the reaction was started by the addition of 5 mM 3-mercaptopyruvate or thiosulfate.…”

Section: Cultivation Of L Major and L Mexicana-promastigotes Of L mentioning

confidence: 82%

“…Sulfurtransferases may also play a part in the management of the cytotoxicity of reactive oxygen species in aerobic tissues (4). Bovine rhodanese has a 1000-fold higher affinity for the reduced form of thioredoxin than for cyanide and so may function in peroxide detoxification (4,10).…”

mentioning

confidence: 99%

“…Bovine rhodanese has a 1000-fold higher affinity for the reduced form of thioredoxin than for cyanide and so may function in peroxide detoxification (4,10). A reaction analogous to that of sulfane-loaded sulfurtransferase with thioredoxin is also thought to be a critical step in the synthesis of thiouridine (7,11,12), and the formation of thiocarboxylate during thiamine biosynthesis by the multidomain protein ThiI of Escherichia coli (7,12).…”

mentioning

confidence: 99%

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3-Mercaptopyruvate Sulfurtransferase of LeishmaniaContains an Unusual C-terminal Extension and Is Involved in Thioredoxin and Antioxidant Metabolism

Williams

Kelly

Mottram

et al. 2003

Journal of Biological Chemistry

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Cytosolic 3-mercaptopyruvate sulfurtransferases (EC 2.8.1.2) of Leishmania major and Leishmania mexicana have been cloned, expressed as active enzymes in Escherichia coli, and characterized. The leishmanial singlecopy genes predict a sulfurtransferase that is structurally peculiar in possessing a C-terminal domain of some 70 amino acids. Homologous genes of Trypanosoma cruzi and Trypanosoma brucei encode enzymes with a similar C-terminal domain, suggesting that this feature, not known in any other sulfurtransferase, is a characteristic of trypanosomatid parasites. Short truncations of the C-terminal domain resulted in misfolded inactive proteins, demonstrating that the domain plays some key role in facilitating correct folding of the enzymes. The leishmanial recombinant enzymes exhibited high activity toward 3-mercaptopyruvate and catalyzed the transfer of sulfane sulfur to cyanide to form thiocyanate. They also used thiosulfate as a substrate and reduced thioredoxin as the accepting nucleophile, the latter being oxidized. The enzymes were expressed in all life cycle stages, and the expression level was increased under peroxide or hypo-sulfur stress. The results are consistent with the enzymes having an involvement in the synthesis of sulfur amino acids per se or iron-sulfur centers of proteins and the parasite's management of oxidative stress.

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Section: Table I Activities Of Recombinant Lmajmst and Lmexmstsupporting

confidence: 88%

Section: Cultivation Of L Major and L Mexicana-promastigotes Of L mentioning

confidence: 82%

mentioning

confidence: 99%

mentioning

confidence: 99%

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3-Mercaptopyruvate Sulfurtransferase of LeishmaniaContains an Unusual C-terminal Extension and Is Involved in Thioredoxin and Antioxidant Metabolism

Williams

Kelly

Mottram

et al. 2003

Journal of Biological Chemistry

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“…However, it has been reported that MST can both oxidize thioredoxin, a key intermediate in cellular redox reactions, and react with peroxides and that this may be a physiologically significant mechanism for combating oxidative challenges [41,42]. Recently, it has been reported that overexpression of ALDH-2 confers lung epithelial cell resistance to hyperoxia-induced cell death in part by reducing intracellular and mitochondrialderived ROS production [43].…”

Section: Discussionmentioning

confidence: 99%