Cysteine desulfurase
From Wikipedia, the free encyclopedia
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.
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[edit] Structural studies
As of late 2007, only one structure has been solved for this class of enzymes, with the PDB accession code 1T3I.
[edit] References
- IUBMB entry for 2.8.1.7
- BRENDA references for 2.8.1.7 (Recommended.)
- PubMed references for 2.8.1.7
- PubMed Central references for 2.8.1.7
- Google Scholar references for 2.8.1.7
- 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: . PMID 8464885.
- Mihara H, Esaki N (2002). "Bacterial cysteine desulfurases: their function and mechanisms". Appl. Microbiol. Biotechnol. 60: 12–23. doi: . 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: . PMID 12714048.