cysteine desulfurase

{{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 $\rightleftharpoons$ 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

As of late 2007, only one structure had been solved for this class of enzymes, with the PDB accession code {{PDB link|1T3I}}.

References

{{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 }}

Category:EC 2.8.1

Category:Enzymes of known structure