Jump to content
 







Main menu
   


Navigation  



Main page
Contents
Current events
Random article
About Wikipedia
Contact us
Donate
 




Contribute  



Help
Learn to edit
Community portal
Recent changes
Upload file
 








Search  

































Create account

Log in
 









Create account
 Log in
 




Pages for logged out editors learn more  



Contributions
Talk
 



















Contents

   



(Top)
 


1 Structure and mechanism  





2 Clinical relevance  





3 Human proteins  





4 Nomenclature  





5 References  





6 External links  














Rhodanese






Deutsch
Español
Français
Galego
Italiano



 

Edit links
 









Article
Talk
 

















Read
Edit
View history
 








Tools
   


Actions  



Read
Edit
View history
 




General  



What links here
Related changes
Upload file
Special pages
Permanent link
Page information
Cite this page
Get shortened URL
Download QR code
Wikidata item
 




Print/export  



Download as PDF
Printable version
 




In other projects  



Wikimedia Commons
 
















Appearance
   

 






From Wikipedia, the free encyclopedia
 


Rhodanese-like domain
Identifiers
SymbolRhodanese
PfamPF00581
InterProIPR001763
PROSITEPDOC00322
SCOP22ora / SCOPe / SUPFAM
OPM superfamily413
OPM protein2mpn
CDDcd00158
Membranome571
Available protein structures:
Pfam  structures / ECOD  
PDBRCSB PDB; PDBe; PDBj
PDBsumstructure summary
thiosulfate sulfurtransferase
Identifiers
EC no.2.8.1.1
CAS no.9026-04-4
Databases
IntEnzIntEnz view
BRENDABRENDA entry
ExPASyNiceZyme view
KEGGKEGG entry
MetaCycmetabolic pathway
PRIAMprofile
PDB structuresRCSB PDB PDBe PDBsum
Gene OntologyAmiGO / QuickGO
Search
PMCarticles
PubMedarticles
NCBIproteins

Rhodanese is a mitochondrial enzyme that detoxifies cyanide (CN) by converting it to thiocyanate (SCN, also known as "rhodanate").[1] In enzymatology, the common name is listed as thiosulfate sulfurtransferase (EC 2.8.1.1).[2] The diagram on the right shows the crystallographically-determined structure of rhodanese.

Itcatalyzes the following reaction:

thiosulfate + cyanide sulfite + thiocyanate

Structure and mechanism

[edit]

This reaction takes place in two steps. In the first step, thiosulfate is reduced by the thiol group on cysteine-247 1, to form a persulfide and a sulfite 2. In the second step, the persulfide reacts with cyanide to produce thiocyanate, re-generating the cysteine thiol 1.[3]

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

Rhodanese has an internal duplication. This domain is found as a single copy in other proteins, including phosphatases and ubiquitin C-terminal hydrolases.[5]

Clinical relevance

[edit]

This reaction is important for the treatment of exposure to cyanide, since the thiocyanate formed is around 1 / 200 as toxic.[6]:p. 15938 The use of thiosulfate solution as an antidote for cyanide poisoning is based on the activation of this enzymatic cycle.

Human proteins

[edit]

The human mitochondrial rhodanese gene is TST.

The following other human genes match the "Rhodanese-like" domain on InterPro, but are not the rodanase with its catalytic activity (see also the list of related families in #Structure and mechanism):

Nomenclature

[edit]

Although the standard nomenclature rules for enzymes indicate that their names are to end with the letters "-ase", rhodanese was first described in 1933,[7] prior to the 1955 establishment of the Enzyme Commission; as such, the older name had already attained widespread usage.

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".

References

[edit]
  1. ^ Cipollone R, Ascenzi P, Tomao P, Imperi F, Visca P (2008). "Enzymatic detoxification of cyanide: clues from Pseudomonas aeruginosa Rhodanese". Journal of Molecular Microbiology and Biotechnology. 15 (2–3): 199–211. doi:10.1159/000121331. PMID 18685272. S2CID 25431686.
  • ^ EC 2.8.1.1, at the International Union of Biochemistry and Molecular Biology
  • ^ Cipollone R, Ascenzi P, Tomao P, Imperi F, Visca P (2008). "Enzymatic detoxification of cyanide: clues from Pseudomonas aeruginosa Rhodanese". Journal of Molecular Microbiology and Biotechnology. 15 (2–3): 199–211. doi:10.1159/000121331. PMID 18685272. S2CID 25431686.
  • ^ "Thiosulphate sulfurtransferase, conserved site (IPR001307)". EMBL-EBI. InterPro.
  • ^ Gliubich F, Gazerro M, Zanotti G, Delbono S, Bombieri G, Berni R (August 1996). "Active site structural features for chemically modified forms of rhodanese". The Journal of Biological Chemistry. 271 (35): 21054–61. doi:10.1074/jbc.271.35.21054. PMID 8702871.
  • ^ Jaszczak E, Polkowska Ż, Narkowicz S, Namieśnik J (July 2017). "Cyanides in the environment-analysis-problems and challenges". Environmental Science and Pollution Research International. 24 (19): 15929–15948. doi:10.1007/s11356-017-9081-7. PMC 5506515. PMID 28512706.
  • ^ Cipollone R, Ascenzi P, Visca P (February 2007). "Common themes and variations in the rhodanese superfamily". IUBMB Life. 59 (2): 51–9. doi:10.1080/15216540701206859. PMID 17454295.
  • [edit]
    Retrieved from "https://en.wikipedia.org/w/index.php?title=Rhodanese&oldid=1188837829"

    Categories: 
    EC 2.8
    Protein domains
    Hidden categories: 
    Articles with short description
    Short description is different from Wikidata
    Commons category link from Wikidata
     



    This page was last edited on 8 December 2023, at 00:28 (UTC).

    Text is available under the Creative Commons Attribution-ShareAlike License 4.0; additional terms may apply. By using this site, you agree to the Terms of Use and Privacy Policy. Wikipedia® is a registered trademark of the Wikimedia Foundation, Inc., a non-profit organization.



    Privacy policy

    About Wikipedia

    Disclaimers

    Contact Wikipedia

    Code of Conduct

    Developers

    Statistics

    Cookie statement

    Mobile view



    Wikimedia Foundation
    Powered by MediaWiki