A pyridoxal-phosphate protein. The sulfur from free L-cysteine is first transferred to a cysteine residue in the active site, and then passed on to various other acceptors. The enzyme is involved in the biosynthesis of iron-sulfur clusters, thio-nucleosides in tRNA, thiamine, biotin, lipoate and pyranopterin (molybdopterin) . In Azotobacter vinelandii, this sulfur provides the inorganic sulfide required for nitrogenous metallocluster formation .
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
SYSTEMATIC NAME
IUBMB Comments
L-cysteine:acceptor sulfurtransferase
A pyridoxal-phosphate protein. The sulfur from free L-cysteine is first transferred to a cysteine residue in the active site, and then passed on to various other acceptors. The enzyme is involved in the biosynthesis of iron-sulfur clusters, thio-nucleosides in tRNA, thiamine, biotin, lipoate and pyranopterin (molybdopterin) [2]. In Azotobacter vinelandii, this sulfur provides the inorganic sulfide required for nitrogenous metallocluster formation [1].
the cysteine desulfurase Nfs1 and its scaffold protein partner IscU are down-regulated at both mRNA and protein levels when murine macrophages are physiologically stimulated with interferon-gamma
downregulation of enzyme at both mRNA and protein level by stimulation of macrophages with lipopolysaccharide. Lipopolysaccharide triggers a delayed decline of cysteine desulfurase protein and its protein partner IscU
LPS triggers a delayed decline of Nfs1, rather involving transcriptional events or mRNA instability, also the expression of IscU is down-regulated in LPS-stimulated macrophages
depletion of enzyme by gene silencing inhibits the activities of mitochondrial NADH-ubiquinone oxidoreductase and succinate-ubiquinone oxidoreductase of the respiratory chain, as well as aconitase of the Krebs cycle, with no alteration in their protein levels. in addition, activity of cytosolic xanthine oxidase is reduced and iron-regulatory protein-1 is converted from its 4Fe-4S aconitase form to its apo- or RNA-binding form
expression of cysteine desulfurase in enzyme-depleted heLa cells restores both growth and Fe/S protein activities to wild-type levels. No complementation of growth is observed when the murine enzyme is synthesized without its mitochondrial presequence