関: rhodanese

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In enzymology, a thiosulfate sulfurtransferase (EC 2.8.1.1) is an enzyme that catalyzes the chemical reaction

thiosulfate + cyanide sulfite + thiocyanate

Thus, the two substrates of this enzyme are thiosulfate and cyanide, whereas its two products are sulfite and thiocyanate.

This enzyme belongs to the family of transferases, specifically the sulfurtransferases, which transfer sulfur-containing groups. The systematic name of this enzyme class is thiosulfate:cyanide sulfurtransferase. Other names in common use include thiosulfate cyanide transsulfurase, thiosulfate thiotransferase, rhodanese, and rhodanase.

Structural studies

As of late 2007, 11 structures have been solved for this class of enzymes, with PDB accession codes 1BOH, 1BOI, 1DP2, 1E0C, 1H4K, 1H4M, 1ORB, 1RHD, 1RHS, 1UAR, and 2ORA.

References

Sorbo BH; Lagerkvist, Ulf; Pesola, Rainer; Virtanen, Artturi I.; Sörensen, Nils Andreas (1953). "Crystalline rhodanese. I. Purification and physicochemical examination". Acta Chem. Scand. 7: 1129–1136. doi:10.3891/acta.chem.scand.07-1129.
Sorbo BH; Lagerkvist, Ulf; Pesola, Rainer; Virtanen, Artturi I.; Sörensen, Nils Andreas (1953). "Crystalline rhodanese. II. The enzyme catalyzed reaction". Acta Chem. Scand. 7: 1137–1145. doi:10.3891/acta.chem.scand.07-1137.
Westley J and Green JR (1959). "Crystalline beef kidney rhodanese". J. Biol. Chem. 234: 2325–6. PMID 13844173.
Thiosulfate Sulfurtransferase at the US National Library of Medicine Medical Subject Headings (MeSH)

Molecular and Cellular Biology portal

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English Journal

Structural and biochemical analyses indicate that a bacterial persulfide dioxygenase-rhodanese fusion protein functions in sulfur assimilation.

Motl N1, Skiba MA1,2, Kabil O1, Smith JL1,2, Banerjee R3.
The Journal of biological chemistry.J Biol Chem.2017 Aug 25;292(34):14026-14038. doi: 10.1074/jbc.M117.790170. Epub 2017 Jul 6.
PMID 28684420

Tum1 is involved in the metabolism of sterol esters in Saccharomyces cerevisiae.

Uršič K1,2, Ogrizović M1, Kordiš D1, Natter K3, Petrovič U4,5.
BMC microbiology.BMC Microbiol.2017 Aug 22;17(1):181. doi: 10.1186/s12866-017-1088-1.
PMID 28830344

Improved fermentative L-cysteine overproduction by enhancing a newly identified thiosulfate assimilation pathway in Escherichia coli.

Kawano Y1, Onishi F2, Shiroyama M1, Miura M3, Tanaka N1, Oshiro S1, Nonaka G2, Nakanishi T4, Ohtsu I5,6.
Applied microbiology and biotechnology.Appl Microbiol Biotechnol.2017 Jul 29. doi: 10.1007/s00253-017-8420-4. [Epub ahead of print]
PMID 28756590

Japanese Journal

Induction of Rhodanese, a Detoxification Enzyme, in Livers from Mice after Long-term Irradiation with Low-dose-rate Gamma-rays

Journal of radiation research 49(6), 661-666, 2008-11-16
NAID 110006985826

生体内含硫無機化合物の定量法並びにイオウ転移酵素の測定法の開発と,結合型イオウの生理学的機能評価

藥學雜誌 128(6), 881-900, 2008-06-01
NAID 110006687002

Rhodanese (thiosulfate : cyanide sulfurtransferase) from frog Rana temporaria

Journal of chromatography. B, Biomedical applications 746(2), 315-318, 2000-09-15
NAID 10012268488

「チオ硫酸イオウ転移酵素」

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thiosulfate sulfurtransferase
Identifiers
EC number	2.8.1.1
CAS number	9026-04-4
Databases
IntEnz	IntEnz view
BRENDA	BRENDA entry
ExPASy	NiceZyme view
KEGG	KEGG entry
MetaCyc	metabolic pathway
PRIAM	profile
PDB structures	RCSB PDB PDBe PDBsum
Gene Ontology	AmiGO / EGO
Search
PMC	articles
PubMed	articles
NCBI	proteins