Crystalline Rhodanese. II. The Enzyme Catalyzed Reaction.

Sörbo, Bo; Lagerkvist, Ulf; Pesola, Rainer; Virtanen, Artturi I.; Sørensen, Nils Andreas

doi:10.3891/acta.chem.scand.07-1137

Cited by 104 publications

(56 citation statements)

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“…Thiosulfate:cyanide sulfurtransferase activity assay-The cyanide detoxification activity of TSTD1 was measured by a colorimetric assay as described previously with the following modifications (26). The reaction was performed at 37 ˚C and contained (1-50 mM) thiosulfate, (0.02-50 mM) potassium cyanide and 5-10 µg TSTD1 in 300 mM HEPES, pH 7.4 containing 150 mM NaCl (330 µl final volume).…”

Section: Methodsmentioning

confidence: 99%

“…Sulfurtransferases are ubiquitously distributed enzymes that function in a range of pathways including sulfur metabolism, iron-sulfur cluster formation, selenium metabolism, and cyanide detoxification (13,14,(25)(26)(27)(28). In humans, there are five sulfurtransferases including mitochondrial rhodanese and MST, which is found in the cytoplasmic and mitochondrial compartments (29,30).…”

Section: Hydrogen Sulfide (H 2 S)mentioning

confidence: 99%

“…Alternatively, the rhodanese domain can be present in a tandem repeat, as in rhodanese and MST, where the active sites are located in a cleft between the N-and C-terminal domains (14,15). Finally, rhodanese domains are fused to other protein domains as in Cdc25 phosphatase (20) or in the PRF and CstB proteins (23,24).Sulfurtransferases are ubiquitously distributed enzymes that function in a range of pathways including sulfur metabolism, iron-sulfur cluster formation, selenium metabolism, and cyanide detoxification (13,14,(25)(26)(27)(28). In humans, there are five sulfurtransferases including mitochondrial rhodanese and MST, which is found in the cytoplasmic and mitochondrial compartments (29,30).…”

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confidence: 99%

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Thiosulfate sulfurtransferase-like domain–containing 1 protein interacts with thioredoxin

Libiad

Motl

Akey

et al. 2018

Journal of Biological Chemistry

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ǂ These authors contributed equally to this work Rhodanese domains are structural modules present in the sulfurtransferase superfamily. These domains can exist as single units, in tandem repeats or fused to domains with other activities. Despite their prevalence across species, the specific physiological roles of most sulfurtransferases are not known. Mammalian rhodanese and mercaptopyruvate sulfurtransferase are perhaps the best-studied members of this protein superfamily and are involved in hydrogen sulfide metabolism. The relatively unstudied human thiosulfate sulfurtransferase like domain-containing 1 (TSTD1) protein, a single-domain cytoplasmic sulfurtransferase, was also postulated to play a role in the sulfide oxidation pathway using thiosulfate to form glutathione persulfide, for subsequent processing in the mitochondrial matrix. Prior kinetic analysis of TSTD1 was performed at pH 9.2, raising questions about relevance and the proposed model for TSTD1 function. In this study, we report a 1.04 Å resolution crystal structure of human TSTD1, which displays an exposed active site that is distinct from that of rhodanese and mercaptopyruvate sulfurtransferase. Kinetic studies with a combination of sulfur donors and acceptors reveal that TSTD1 exhibits a low K M for thioredoxin as a sulfane sulfur acceptor and that it utilizes thiosulfate inefficiently as a sulfur donor. The active site exposure and its interaction with thioredoxin, suggest that TSTD1 might play a role in sulfide-based signaling. The apical localization of TSTD1 in human colonic crypts, which interfaces with sulfide-releasing microbes, and the overexpression of TSTD1 in colon cancer, provides potentially intriguing clues as to its role in sulfide metabolism. Hydrogen sulfide (H 2 S)1 is an important signaling molecule with effects on multiple physiological processes including neuromodulation, inflammation and cardiac function (1-7). Maintaining healthy levels of H 2 S in mammalian cells requires tight control of its biosynthesis and its catabolism (8,9). H 2 S is produced endogenously by two enzymes in the transsulfuration pathway, cystathionine β-synthase and γ-cystathionase as well as by mercaptopyruvate sulfurtransferase (MST) (10-13). H 2 S is oxidized via the sulfide oxidation pathway to generate the end-products thiosulfate Protein persulfidation, a posttranslational modification of cysteine residues, is postulated to be a major mechanism by which H 2 S signals (17). However, the mechanism by which target proteins acquire this modification and the sulfur source(s) used in persulfidation reactions are unclear (18). Sulfurtransferases like rhodanese or the single rhodanese domain containing TSTD1 could potentially play a role in protein persulfidation because of their capacity to form an active site cysteine persulfide during their reaction cycle (18).The rhodanese superfamily members are distinguished by a structural module with an α/β topology in which α-helices surround a central five-stranded β-sheet core (19). At least three variations...

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Section: Methodsmentioning

confidence: 99%

Section: Hydrogen Sulfide (H 2 S)mentioning

confidence: 99%

mentioning

confidence: 99%

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Thiosulfate sulfurtransferase-like domain–containing 1 protein interacts with thioredoxin

Libiad

Motl

Akey

et al. 2018

Journal of Biological Chemistry

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“…A sample of 150 mg of two times crystallised enzyme was subjected to the carboxymethylation procedure described by DeToma and Westley [7] for the liver rhodanese, using [ 14C]-iodoacetic acid (25 mCi/mmole, Radiochemical Centre, Amersham). Time course of the reaction was followed by measuring the enzymatic activity according to the method of Sorbo [9]; complete inactivation was achieved after 45 min. Radioactivity assay performed after extensive dialysis against water plus 1 mM mercaptoethanol showed that one mole of iodoacetic acid was incorporated per mole of inactive monomer.…”

Section: Methodsmentioning

confidence: 99%

The amino acid sequence around the reactive cysteinyl residue of bovine kidney rhodanese

Bossa¹,

Cannella²,

Federici³

et al. 1973

FEBS Letters

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“…One rhodanese unit was taken as the amount of enzyme, which under the given condition produced an optical density reading of 1.08 at 460 nm per min (Sorbo, 1953). Protein concentrations were determined by the method of Bradford (1976) using bovine serum albumin (BSA) as the standard.…”

Section: Enzyme and Protein Assaysmentioning

confidence: 99%

Properties of rhodanese from the liver of tilapia, Oreochromis niloticus, in Asejire Lake, Nigeria

Atere¹,

Agboola²,

Gafar³

et al. 2014

Afr. J. Biochem. Res.

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The study investigates the purification and characterisation of rhodanese from the liver of the tilapia fish (Oreochromis niloticus) collected from Asejire Lake in Nigeria. This was with a view to understanding the biochemical basis of the survival of the fish in cyanide polluted water. Rhodanese was isolated and purified from liver tissue homogenate of tilapia using CM-Sephadex ion exchange chromatography and Sephadex G-75 gel filtration. The specific activity of the enzyme was 56.86 U/mg. The K m values for KCN and Na 2 S 2 O 3 as substrates were 0.1240 ± 0.0021 mM and 0.0516 ± 0.0097 mM, respectively. The apparent molecular weight was estimated by gel filtration on a Sephacyl S-400 column to be 35,460 Da. The optimal activity was found at pH 6.5 and the temperature optimum was 40°C. The rhodanese enzyme showed that the activity of the enzyme was not affected by MgCl 2 , KCl, NH 4 Cl, MnCl 2 and CaCl 2 while AlCl 3 , inhibited the enzyme.

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Crystalline Rhodanese. II. The Enzyme Catalyzed Reaction.

Cited by 104 publications

References 0 publications

Thiosulfate sulfurtransferase-like domain–containing 1 protein interacts with thioredoxin

Thiosulfate sulfurtransferase-like domain–containing 1 protein interacts with thioredoxin

The amino acid sequence around the reactive cysteinyl residue of bovine kidney rhodanese

Properties of rhodanese from the liver of tilapia, Oreochromis niloticus, in Asejire Lake, Nigeria

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