In
enzymology, a
cysteine desulfurase 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 .
References
- Zheng L, White RH, Cash VL, Jack RF, Dean DR "Cysteine desulfurase activity indicates a role for NIFS in metallocluster biosynthesis". Proc. Natl. Acad. Sci. U. S. A. 90 2754–8.
- Mihara H, Esaki N "Bacterial cysteine desulfurases: their function and mechanisms". Appl. Microbiol. Biotechnol. 60 12–23.
- Frazzon J, Dean DR "Formation of iron-sulfur clusters in bacteria: an emerging field in bioinorganic chemistry". Curr. Opin. Chem. Biol. 7 166–73.
External links
Gene Ontology (GO) codes