cysteine desulfurase
{{Short description|Class of enzymes}}
{{infobox enzyme
| Name = cysteine desulfurase
| EC_number = 2.8.1.7
| CAS_number =
| GO_code = 0031071
| image =
| width =
| caption =
}}
In enzymology, a cysteine desulfurase ({{EC number|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. One group of authors has given it the acronym hapE, for hydrogen sulfide, alanine, and pyruvate producing enzyme.{{Cite journal |last1=Großhennig |first1=Stephanie |last2=Ischebeck |first2=Till |last3=Gibhardt |first3=Johannes |last4=Busse |first4=Julia |last5=Feussner |first5=Ivo |last6=Stülke |first6=Jörg |date=April 2016 |title=Hydrogen sulfide is a novel potential virulence factor of Mycoplasma pneumoniae : characterization of the unusual cysteine desulfurase/desulfhydrase HapE |url=https://onlinelibrary.wiley.com/doi/10.1111/mmi.13300 |journal=Molecular Microbiology |language=en |volume=100 |issue=1 |pages=42–54 |doi=10.1111/mmi.13300 |pmid=26711628 |issn=0950-382X}}
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.
Function
Bacteria contain cysteine desulfurases to form iron sulfur clusters in proteins.{{cite journal | vauthors = 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 | issue = 1–2 | s2cid = 23172939 }}
However recently it has been shown that the enzyme, which produces hydrogen sulfide from cysteine, is also a virulence factor, namely for M.pneumoniae, in that it causes both α-hemolysis and β-haemolysis of red blood cells.
In mammals, the enzyme participates in thiamine metabolism.
Structural studies
References
{{reflist|1}}
- {{cite journal | vauthors = 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 | issue = 7 | pmc = 46174 | bibcode = 1993PNAS...90.2754Z | doi-access = free }}
- {{cite journal | vauthors = 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 | issue = 2 }}
{{Sulfur-containing group transferases}}
{{Enzymes}}
{{Portal bar|Biology|border=no}}
Category:Enzymes of known structure
{{2.8-enzyme-stub}}