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{{Enzyme references|EC_number=2.8.1.7|IUBMB_EC_number=2/8/1/7}}
{{Enzyme references|EC_number=2.8.1.7|IUBMB_EC_number=2/8/1/7}}
* {{cite journal | author = Zheng L, White RH, Cash VL, Jack RF, Dean DR | date = 1993 | title = Cysteine desulfurase activity indicates a role for NIFS in metallocluster biosynthesis | journal = Proc. Natl. Acad. Sci. U. S. A. | volume = 90 | pages = 2754–8 | pmid = 8464885 }}
* {{cite journal | author = Zheng L, White RH, Cash VL, Jack RF, Dean DR | date = 1993 | title = Cysteine desulfurase activity indicates a role for NIFS in metallocluster biosynthesis | journal = Proc. Natl. Acad. Sci. U. S. A. | volume = 90 | pages = 2754–8 | pmid = 8464885 | doi = 10.1073/pnas.90.7.2754 }}
* {{cite journal | author = Mihara H, Esaki N | date = 2002 | title = Bacterial cysteine desulfurases: their function and mechanisms | journal = Appl. Microbiol. Biotechnol. | volume = 60 | pages = 12–23 | pmid = 12382038 }}
* {{cite journal | author = Mihara H, Esaki N | date = 2002 | title = Bacterial cysteine desulfurases: their function and mechanisms | journal = Appl. Microbiol. Biotechnol. | volume = 60 | pages = 12–23 | pmid = 12382038 | doi = 10.1007/s00253-002-1107-4 }}
* {{cite journal | author = Frazzon J, Dean DR | date = 2003 | title = Formation of iron-sulfur clusters in bacteria: an emerging field in bioinorganic chemistry | journal = Curr. Opin. Chem. Biol. | volume = 7 | pages = 166–73 | pmid = 12714048 }}
* {{cite journal | author = Frazzon J, Dean DR | date = 2003 | title = Formation of iron-sulfur clusters in bacteria: an emerging field in bioinorganic chemistry | journal = Curr. Opin. Chem. Biol. | volume = 7 | pages = 166–73 | pmid = 12714048 | doi = 10.1016/S1367-5931(03)00021-8 }}


==External links==
==External links==

Revision as of 23:15, 9 June 2008

In enzymology, a cysteine desulfurase (EC 2.8.1.7) is an enzyme that catalyzes the chemical reaction

L-cysteine + [enzyme]-cysteine L-alanine + [enzyme]-S-sulfanylcysteine

Thus, the two substrates of this enzyme are L-cysteine and [[[enzyme]-cysteine]], whereas its two products are L-alanine and [[[enzyme]-S-sulfanylcysteine]].

This enzyme belongs to the family of transferases, specifically the sulfurtransferases, which transfer sulfur-containing groups. The systematic name of this enzyme class is L-cysteine:[enzyme cysteine] sulfurtransferase. Other names in common use include IscS, NIFS, NifS, SufS, and cysteine desulfurylase. This enzyme participates in thiamine metabolism.

Structural studies

As of late 2007, only one structure has been solved for this class of enzymes, with the PDB accession code 1T3I.

References

Template:Enzyme references

  • Zheng L, White RH, Cash VL, Jack RF, Dean DR (1993). "Cysteine desulfurase activity indicates a role for NIFS in metallocluster biosynthesis". Proc. Natl. Acad. Sci. U. S. A. 90: 2754–8. doi:10.1073/pnas.90.7.2754. PMID 8464885.{{cite journal}}: CS1 maint: multiple names: authors list (link)
  • Mihara H, Esaki N (2002). "Bacterial cysteine desulfurases: their function and mechanisms". Appl. Microbiol. Biotechnol. 60: 12–23. doi:10.1007/s00253-002-1107-4. PMID 12382038.
  • Frazzon J, Dean DR (2003). "Formation of iron-sulfur clusters in bacteria: an emerging field in bioinorganic chemistry". Curr. Opin. Chem. Biol. 7: 166–73. doi:10.1016/S1367-5931(03)00021-8. PMID 12714048.

Template:Enzyme links

Gene Ontology (GO) codes

Template:GO code links