Cysteine desulfurase

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

L-cysteine + [enzyme]-cysteine ${\displaystyle \rightleftharpoons }$ L-alanine + [enzyme]-S-sulfanylcysteine

cysteine desulfurase
Identifiers
EC no.	2.8.1.7
Databases
IntEnz	IntEnz view
BRENDA	BRENDA entry
ExPASy	NiceZyme view
KEGG	KEGG entry
MetaCyc	metabolic pathway
PRIAM	profile
PDB structures	RCSB PDB PDBe PDBsum
Gene Ontology	AmiGO / QuickGO
Search PMC articles PubMed articles NCBI proteins

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.^[1]

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.^[2] 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.^[1]

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 1T3I.