Psychiatry related information on Tst

• The difference in the levels of rhodanese activity in the two types of rodents is discussed in relation to their dietary habits [1].

High impact information on Tst

• In this study, the N-terminal 23 residues of the matrix enzyme rhodanese could import several passenger proteins but were unable to import the mature form of mitochondrial aldehyde dehydrogenase (mALDH) [2].
• Further, rhodanese cross-reacts with anti-MST antibody [3].
• An active site cysteine residue (Cys246; site of formation of persulfide in catalysis) and an arginine residue (Arg185; substrate binding site) in rhodanese were also conserved in MST [3].
• The thermodynamic parameters of binding of the peptide RHD and of four of its double D-isomers were determined for 30 nm (SUVs) and 100 nm (LUVs) unilamellar vesicles composed of phosphatidylcholine/phosphatidylglycerol (3:1) using circular dichroism spectroscopy, fluorescence spectroscopy, and isothermal titration calorimetry [4].
• Computer-generated structural modelling of rat rhodanese indicated that few amino acid substitutions were present within close proximity to the active site or within the hinge region (connecting loop) between the A and B domains [5].

Biological context of Tst

• By screening a rat liver cDNA library with oligonucleotide probes complementary to portions of the published bovine rhodanese peptide sequence, rat rhodanese cDNA clones were obtained and sequenced [5].
• Influence of cassava diets on placental thiocyanate transfer, tissue rhodanese activity and performance of rats during gestation [6].
• Among female rats, Phase I DME genes were repressed at 0.3 and 1.0 gm/kg/day doses, while genes such as manganese superoxide dismutase, cytochrome P450 reductase, quinone oxidoreductase and thiosulfate sulfurtransferase demonstrated a dose-dependent increase in gene expression [7].
• Immobilized rhodanese: some aspects of anion inhibition kinetics and modulation by cations [8].

Anatomical context of Tst

• Incubation of mitochondria with sulfate and alpha-ketoglutaric acid caused a significant decrease in rhodanese activity [9].
• 6. These results, and previously reported nasal rhodanese activity data, indicate that inhaled organonitriles are substantially detoxicated in the nasal cavity [10].
• Variations in rhodanese activity in rat submandibular gland with time of day [11].

Associations of Tst with chemical compounds

• The sulfane sulfur pool, a source of sulfur transferred by rhodanese, can be augmented in vitro in guinea pig liver, but not in rat liver when 3-mercaptolactate-cysteine disulfide is used as a substrate of gamma-cystathionase [12].
• Cyanide is normally metabolized to thiocyanate (SCN-) by the sulfur-dependent enzyme rhodanese [13].
• However, the addition of sodium thiosulfate and rhodanese to the assay reactivated the cyanide-inhibited cytochrome oxidase [14].
• Cancer tissues contain the enzyme rhodanese in amounts comparable to that of liver and kidney and hence, cannot be attacked selectively by cyanide release through beta-glucosidase action on amygdalin [15].
• Kinetic studies revealed that Fraction I rat liver rhodanese catalyzes thiocyanate formation from thiosulfate and cyanide by a double displacement mechanism [9].

Other interactions of Tst

• Conversion of rhodanese to MST was tried by site-directed mutagenesis [3].
• The cyanide-metabolizing enzyme rhodanese in rat nasal respiratory and olfactory mucosa [16].

Analytical, diagnostic and therapeutic context of Tst

• Molecular cloning, sequencing and characterization of cDNA to rat liver rhodanese, a thiosulphate sulphurtransferase [5].
• Circular dichroism data indicated that a peptide corresponding to the region of fusion between rhodanese and mALDH had less structure than corresponding peptides from imported fusion proteins, suggesting that mALDH may alter the helix in the rhodanese signal sequence, thus preventing import [2].
• Rhodanese which detoxifes cyanide is also found to be inhibited in rats fed low protein diet while the inhibition was only marginal in the high protein fed groups [17].

References