関: thiosulfate sulfurtransferase

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出典(authority):フリー百科事典『ウィキペディア（Wikipedia）』「2015/05/27 23:45:20」(JST)

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Rhodanese is a mitochondrial enzyme that detoxifies cyanide (CN⁻) by converting it to thiocyanate (SCN⁻).^[1]

This reaction takes place in two steps. The diagram on the right shows the crystallographically-determined structure of rhodanese. In the first step, thiosulfate reacts with the thiol group on Cysteine-247 1, to form a disulfide 2. In the second step, the disulfide reacts with cyanide to produce thiocyanate, itself being converted back into the "normal" thiol 1.

This reaction is important for the treatment of exposure to cyanide, since the thiocyanate formed is less toxic.^{[medical citation needed]} The use of thiosulfate solution as an antidote for cyanide poisoning is based on the activation of this enzymatic cycle.

Rhodanese shares evolutionary relationship with a large family of proteins, including

Cdc25 phosphatase catalytic domain.
non-catalytic domains of eukaryotic dual-specificity MAPK-phosphatases
non-catalytic domains of yeast PTP-type MAPK-phosphatases
non-catalytic domains of yeast Ubp4, Ubp5, Ubp7
non-catalytic domains of mammalian Ubp-Y
Drosophila heat shock protein HSP-67BB
several bacterial cold-shock and phage shock proteins
plant senescence associated proteins
catalytic and non-catalytic domains of rhodanese (see <db_xref db="INTERPRO" dbkey="IPR001307" />).

Rhodanese has an internal duplication. This domain is found as a single copy in other proteins, including phosphatases and ubiquitin C-terminal hydrolases.^[2]

Human proteins containing this domain

CDC25A; CDC25B; CDC25C; DUSP; DUSP1; DUSP10; DUSP16; DUSP2; DUSP4; DUSP5; DUSP6; DUSP7; KAT; MKP7; MOCS3; MPST; TBCK; TSGA14; TST; USP8;

References

^ Cipollone R, Ascenzi P, Tomao P, Imperi F, Visca P (2008). "Enzymatic detoxification of cyanide: clues from Pseudomonas aeruginosa Rhodanese". J. Mol. Microbiol. Biotechnol. 15 (2-3): 199–211. doi:10.1159/000121331. PMID 18685272.
^ Gliubich F, Gazerro M, Zanotti G, Delbono S, Bombieri G, Berni R (1996). "Active site structural features for chemically modified forms of rhodanese". J. Biol. Chem. 271 (35): 21054–21061. doi:10.1074/jbc.271.35.21054. PMID 8702871.

F. Gliubich, M. Gazerro, G. Zanotti, S. Delbono, G. Bombieri, R. Berni (1996). "Active Site Structural Features for Chemically Modified Forms of Rhodanese". Journal of Biological Chemistry 271 (35): 21054–21061. doi:10.1074/jbc.271.35.21054. PMID 8702871.

External links

Rhodanese at the US National Library of Medicine Medical Subject Headings (MeSH)

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1. シアン化物中毒 cyanide poisoning

English Journal

Dose and time-dependent effects of cyanide on thiosulfate sulfurtransferase, 3-mercaptopyruvate sulfurtransferase, and cystathionine λ-lyase activities.

Singh P, Rao P, Bhattacharya R.Author information Division of Pharmacology and Toxicology, Defence Research and Development Establishment, Gwalior, 474 002, India.AbstractWe assessed the dose-dependent effect of potassium cyanide (KCN) on thiosulfate sulfurtransferase (TST), 3-mercaptopyruvate sulfurtransferase (3-MPST), and cystathionine λ-lyase (CST) activities in mice. The time-dependent effect of 0.5 LD50 KCN on cyanide level and cytochrome c oxidase (CCO), TST, 3-MPST, and CST activities was also examined. Furthermore, TST, 3-MPST, and CST activities were measured in stored mice cadavers. Hepatic and renal TST activity increased by 0.5 LD50 KCN but diminished by ≥2.0 LD50. After 0.5 LD50 KCN, the elevated hepatic cyanide level was accompanied by increased TST, 3-MPST, and CST activities, and CCO inhibition. Elevated renal cyanide level was only accompanied by increased 3-MPST activity. No appreciable change in enzyme activities was observed in mice cadavers. The study concludes that high doses of cyanide exert saturating effects on its detoxification enzymes, indicating their exogenous use during cyanide poisoning. Also, these enzymes are not reliable markers of cyanide poisoning in autopsied samples.
Journal of biochemical and molecular toxicology.J Biochem Mol Toxicol.2013 Dec;27(12):499-507. doi: 10.1002/jbt.21514. Epub 2013 Aug 8.
We assessed the dose-dependent effect of potassium cyanide (KCN) on thiosulfate sulfurtransferase (TST), 3-mercaptopyruvate sulfurtransferase (3-MPST), and cystathionine λ-lyase (CST) activities in mice. The time-dependent effect of 0.5 LD50 KCN on cyanide level and cytochrome c oxidase (CCO), TST,
PMID 23929717

The importance of the 45 S ribosomal small subunit-related complex for mitochondrial translation in Trypanosoma brucei.

Ridlon L, Škodová I, Pan S, Lukeš J, Maslov DA.Author information From the Department of Biology, University of California, Riverside, California 92521.AbstractThe mitochondrial 45 S SSU* complex in Trypanosoma brucei contains the 9 S SSU ribosomal RNA, a set of SSU ribosomal proteins, several pentatricopeptide repeat (PPR) proteins, and proteins not typically found in ribosomes, including rhodanese domain protein (Rhod) and a 200-kDa coiled-coil protein. To investigate the function of this complex, PPR29, Rhod, 200-kDa protein, and mitochondrial ribosomal protein S17 were knocked down by RNAi in procyclic T. brucei. A growth retardation phenotype, a reduction in the amount of the 45 S SSU* complexes, and the preferential inhibition of synthesis of the cytochrome c oxidase subunit I over apocytochrome b were observed as early as day 2 postinduction of RNAi. On the contrary, the down-regulation of mitochondrial ribosomal protein L3 drastically reduced the amount of the large subunit and indiscriminately inhibited mitochondrial translation. The relative amounts of translation-competent, long poly(AU)-tailed cytochrome c oxidase subunit I and edited apocytochrome b mRNAs were selectively reduced by ablation of the 45 S SSU* complex. The formation of the 80 S translation complexes, identified by association of the long-tailed mRNAs with the mitoribosomes, was also disrupted. On the other hand, the relative amount of long-tailed edited RPS12 mRNA was not substantially affected, and there was no noticeable effect on the RPS12 translation complexes. In bloodstream trypanosomes, the amount of the 45 S complexes was drastically reduced compared with procyclics. We propose that the 45 S SSU* complex represents a factor required for normal mitochondrial translation that may have selective effects on different mRNAs.
The Journal of biological chemistry.J Biol Chem.2013 Nov 15;288(46):32963-78. doi: 10.1074/jbc.M113.501874. Epub 2013 Oct 2.
The mitochondrial 45 S SSU* complex in Trypanosoma brucei contains the 9 S SSU ribosomal RNA, a set of SSU ribosomal proteins, several pentatricopeptide repeat (PPR) proteins, and proteins not typically found in ribosomes, including rhodanese domain protein (Rhod) and a 200-kDa coiled-coil protein.
PMID 24089529

Nuclear magnetic resonance approaches for characterizing interactions between the bacterial chaperonin GroEL and unstructured proteins.

Nishida N, Yagi-Utsumi M, Motojima F, Yoshida M, Shimada I, Kato K.Author information Graduate School of Pharmaceutical Sciences, The University of Tokyo, 7-3-1 Hongo, Bunkyo-ku, Tokyo 113-0033, Japan.AbstractGroEL-protein interactions were characterized by stable isotope-assisted nuclear magnetic resonance (NMR) spectroscopy using chemically denatured bovine rhodanese and an intrinsically disordered protein, α-synuclein, as model ligands. NMR data indicated that proteins tethered to GroEL remain largely unfolded and highly mobile, enabling identification of the interaction hot spots displayed on intrinsically disordered proteins.
Journal of bioscience and bioengineering.J Biosci Bioeng.2013 Aug;116(2):160-4. doi: 10.1016/j.jbiosc.2013.02.012. Epub 2013 Apr 6.
GroEL-protein interactions were characterized by stable isotope-assisted nuclear magnetic resonance (NMR) spectroscopy using chemically denatured bovine rhodanese and an intrinsically disordered protein, α-synuclein, as model ligands. NMR data indicated that proteins tethered to GroEL remain largel
PMID 23567152

Japanese Journal

3P-062 微生物における新規チオ硫酸代謝経路の同定(発酵生理学,発酵工学,一般講演)

日本生物工学会大会講演要旨集 67, 286, 2015-09-25
NAID 110010009477

Nuclear magnetic resonance approaches for characterizing interactions between the bacterial chaperonin GroEL and unstructured proteins(ENZYMOLOGY, PROTEIN ENGINEERING, AND ENZYME TECHNOLOGY)

Journal of bioscience and bioengineering 116(2), 160-164, 2013-08
NAID 110009657195

Conflicting two hypotheses on reductive selenite assimilation in Escherichia coli (特集:セレン研究の最前線)

Biomedical research on trace elements 20(3), 226-231, 2009-10-01
NAID 10025620223

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リンク元	「thiosulfate sulfurtransferase」「ロダネーゼ」

「thiosulfate sulfurtransferase」

Available protein structures:
Pfam	structures
PDB	RCSB PDB; PDBe; PDBj
PDBsum	structure summary

Rhodanese-like domain
Identifiers
Symbol	Rhodanese
Pfam	PF00581
InterPro	IPR001763
PROSITE	PDOC00322
SCOP	2ora
SUPERFAMILY	2ora
Available protein structures:
Pfam	structures
PDB	RCSB PDB; PDBe; PDBj
PDBsum	structure summary