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L-cysteine
L-alanine + H2S
L-cysteine
L-alanine + sulfur
DndA is able to directly activate apo-Fe DndC for its reconstitution as a fully functional [4Fe-4S] cluster protein (DndC) with unambiguously demonstrated ATP pyrophosphatase activity
-
-
?
L-cysteine
pyruvate + sulfide
L-cysteine + ?
?
-
in the presence of cysteine, IscSâs ability to bind iron improves significantly
-
-
?
L-cysteine + ?
L-alanine + ?
-
catalyzes the elimination of S from L-cysteine to yield L-alanine and elemental sulfur or H2S, depending on whether or not a reducing agent is added to the reaction mixture, provides sulfur for the assembly of ironâsulfur cluster
-
-
?
L-cysteine + acceptor
L-alanine + S-sulfanyl-acceptor
L-cysteine + acceptor
L-alanine + sulfide + ?
L-cysteine + c-ISCS
L-alanine + c-ISCS-SSH
-
-
-
-
?
L-cysteine + c-IscU
L-alanine + c-IscU-SSH
-
-
-
-
?
L-cysteine + CpNifS
L-alanine + CpNifS-SSH
-
-
-
-
?
L-cysteine + DndA
L-alanine + DndA-SSH
-
-
-
?
L-cysteine + enzyme-cysteine
L-alanine + enzyme-S-sulfanylcysteine
L-cysteine + IscS
L-alanine + IscS-SSH
L-cysteine + MOC3 protein
L-alanine + S-sulfanyl-MOC3 protein
-
-
-
-
?
L-cysteine + N,N-dimethyl-4-phenylenediamine
L-alanine + N,N-dimethyl-4-phenylenediamine sulfate
-
-
-
-
?
L-cysteine + RhdA
L-alanine + RhdA-SSH
L-cysteine + Slr0077
L-alanine + Slr0077-SSH
-
-
-
-
?
L-cysteine + SufE
L-alanine + S-sulfanyl-SufE
-
-
-
-
?
L-cysteine + SufE
L-alanine + SufE-SSH
-
-
-
?
L-cysteine + SufS
L-alanine + SufS-SSH
L-cysteine + [enzyme]-cysteine
L-alanine + [enzyme]-S-sulfanylcysteine
L-cysteine + [IscU]-cysteine
L-alanine + [IscU]-S-sulfanylcysteine
-
each enzyme subunit binds an IscU molecule and transfers sulfane sulfur generated from the conversion of cysteine to alanine to the cluster ligand cysteines of IscU. The enzyme binds preferentially to and stabilizes the D state of apo-IscU
-
-
?
L-cysteine + [SufU]-cysteine
L-alanine + [SufU]-S-sulfanylcysteine
L-cysteine + [ThiI]-cysteine
L-alanine + [ThiI]-S-sulfanylcysteine
-
-
-
-
?
L-cysteine sulfinic acid
L-alanine + sulfite
L-cysteine sulfinic acid + ?
?
cysteine desulfurase DndA catalyzes iron-sulfur cluster assembly by activation of apo-Fe DndC protein
-
-
?
L-cysteine sulfinic acid + DndA
?
-
-
-
?
L-cystine + Slr0077
pyruvate + Slr0077-SSH
-
cystine lyase of Slr0077
-
-
?
L-selenocysteine
L-alanine + selenium
L-selenocysteine + ?
?
-
-
-
?
L-selenocysteine + DndA
L-alanine + DndA-SSeH
-
-
-
?
L-selenocystine
?
-
-
-
-
?
additional information
?
-
L-cysteine

L-alanine + H2S
-
-
or formation of elemental sulfur, depending of presence of a reducing agent in the reaction mixture
-
?
L-cysteine
L-alanine + H2S
-
-
-
?
L-cysteine

pyruvate + sulfide
-
unlike other cysteine desulfurases the L-cysteine C-S-lyase from Synechocystis does not have a conserved cysteine residue at the active site
-
?
L-cysteine
pyruvate + sulfide
-
unlike other cysteine desulfurases the L-cysteine C-S-lyase from Synechocystis does not have a conserved cysteine residue at the active site
-
?
L-cysteine + acceptor

L-alanine + S-sulfanyl-acceptor
-
-
-
-
?
L-cysteine + acceptor
L-alanine + S-sulfanyl-acceptor
-
-
-
?
L-cysteine + acceptor
L-alanine + S-sulfanyl-acceptor
-
-
-
?
L-cysteine + acceptor
L-alanine + S-sulfanyl-acceptor
-
overall reaction
-
-
?
L-cysteine + acceptor
L-alanine + S-sulfanyl-acceptor
-
-
-
?
L-cysteine + acceptor
L-alanine + S-sulfanyl-acceptor
overall reaction
-
-
?
L-cysteine + acceptor
L-alanine + S-sulfanyl-acceptor
-
-
-
-
?
L-cysteine + acceptor
L-alanine + S-sulfanyl-acceptor
-
-
-
-
?
L-cysteine + acceptor
L-alanine + S-sulfanyl-acceptor
-
-
-
-
?
L-cysteine + acceptor
L-alanine + S-sulfanyl-acceptor
-
-
-
-
?
L-cysteine + acceptor
L-alanine + S-sulfanyl-acceptor
-
-
-
-
?
L-cysteine + acceptor
L-alanine + S-sulfanyl-acceptor
-
-
-
-
?
L-cysteine + acceptor
L-alanine + S-sulfanyl-acceptor
-
-
-
-
?
L-cysteine + acceptor
L-alanine + S-sulfanyl-acceptor
-
-
-
-
?
L-cysteine + acceptor

L-alanine + sulfide + ?
overall reaction, the enzyme shows a selenocysteine lyase activity approximately 280fold higher than its cysteine desulfurase activity. The desulfuration mechanism proposed for this enzyme seems to involve three different stages. At the beginning of the reaction, L-cysteine is quickly bound by the cofactor pyridoxal 5'-phosphate, shifting the UV-VIS spectrum of the enzyme. In this aldimine state, the L-cysteine sulfur atom is attacked by Cys384, resulting in persulfide formation. To regenerate the enzyme, this persulfide state must be resolved by transferring the sulphide to inorganic or organic acceptor molecules (accessory proteins, DTT or to other L-cysteine molecules)
-
-
?
L-cysteine + acceptor
L-alanine + sulfide + ?
overall reaction, the enzyme shows a selenocysteine lyase activity approximately 280fold higher than its cysteine desulfurase activity. The desulfuration mechanism proposed for this enzyme seems to involve three different stages. At the beginning of the reaction, L-cysteine is quickly bound by the cofactor pyridoxal 5'-phosphate, shifting the UV-VIS spectrum of the enzyme. In this aldimine state, the L-cysteine sulfur atom is attacked by Cys384, resulting in persulfide formation. To regenerate the enzyme, this persulfide state must be resolved by transferring the sulphide to inorganic or organic acceptor molecules (accessory proteins, DTT or to other L-cysteine molecules)
-
-
?
L-cysteine + enzyme-cysteine

L-alanine + enzyme-S-sulfanylcysteine
-
-
-
-
?
L-cysteine + enzyme-cysteine
L-alanine + enzyme-S-sulfanylcysteine
-
involved in the formation of Fe-S proteins
-
-
?
L-cysteine + IscS

L-alanine + IscS-SSH
-
-
-
-
?
L-cysteine + IscS
L-alanine + IscS-SSH
-
-
-
-
?
L-cysteine + RhdA

L-alanine + RhdA-SSH
-
-
-
-
?
L-cysteine + RhdA
L-alanine + RhdA-SSH
-
transfer of sulfur to rhodanese with formation of a covalent complex between IscS and RhdA
-
-
?
L-cysteine + SufS

L-alanine + SufS-SSH
-
-
-
-
?
L-cysteine + SufS
L-alanine + SufS-SSH
-
-
-
?
L-cysteine + [enzyme]-cysteine

L-alanine + [enzyme]-S-sulfanylcysteine
-
IscS has a high affinity for L-cysteine
-
-
?
L-cysteine + [enzyme]-cysteine
L-alanine + [enzyme]-S-sulfanylcysteine
-
-
-
?
L-cysteine + [enzyme]-cysteine
L-alanine + [enzyme]-S-sulfanylcysteine
-
-
-
-
?
L-cysteine + [enzyme]-cysteine
L-alanine + [enzyme]-S-sulfanylcysteine
-
-
-
?
L-cysteine + [enzyme]-cysteine
L-alanine + [enzyme]-S-sulfanylcysteine
-
-
-
?
L-cysteine + [enzyme]-cysteine
L-alanine + [enzyme]-S-sulfanylcysteine
-
-
-
-
?
L-cysteine + [enzyme]-cysteine
L-alanine + [enzyme]-S-sulfanylcysteine
-
catalyzes the conversion of cysteine to alanine and sulfane sulfur via the formation of a protein-bound cysteine persulfide intermediate on a conserved cysteine residue
-
-
?
L-cysteine + [enzyme]-cysteine
L-alanine + [enzyme]-S-sulfanylcysteine
-
intermediate is an enzyme-bound cysteinyl persulfide
-
-
?
L-cysteine + [enzyme]-cysteine
L-alanine + [enzyme]-S-sulfanylcysteine
-
-
-
-
?
L-cysteine + [enzyme]-cysteine
L-alanine + [enzyme]-S-sulfanylcysteine
-
-
-
-
?
L-cysteine + [enzyme]-cysteine
L-alanine + [enzyme]-S-sulfanylcysteine
-
-
-
-
?
L-cysteine + [enzyme]-cysteine
L-alanine + [enzyme]-S-sulfanylcysteine
-
-
-
-
?
L-cysteine + [enzyme]-cysteine
L-alanine + [enzyme]-S-sulfanylcysteine
-
-
-
?
L-cysteine + [enzyme]-cysteine
L-alanine + [enzyme]-S-sulfanylcysteine
-
-
-
-
?
L-cysteine + [enzyme]-cysteine
L-alanine + [enzyme]-S-sulfanylcysteine
-
-
-
?
L-cysteine + [enzyme]-cysteine
L-alanine + [enzyme]-S-sulfanylcysteine
-
-
-
-
?
L-cysteine + [enzyme]-cysteine
L-alanine + [enzyme]-S-sulfanylcysteine
-
-
?
L-cysteine + [enzyme]-cysteine
L-alanine + [enzyme]-S-sulfanylcysteine
-
iscS has cysteine desulfurase activity and mobilizes sulfur from cysteine for the repair of the [4Fe-4S] cluster in apo-dihydroxyacid dehydratase
-
-
?
L-cysteine + [enzyme]-cysteine
L-alanine + [enzyme]-S-sulfanylcysteine
-
Cys364 residue is essential for activity toward L-cysteine but not toward L-selenocyteine
-
-
?
L-cysteine + [enzyme]-cysteine
L-alanine + [enzyme]-S-sulfanylcysteine
-
IscS transfers the sulfur atom from L-cysteine to the C-terminal thiocarboxylate of the MoaD subunit in vitro
-
-
?
L-cysteine + [enzyme]-cysteine
L-alanine + [enzyme]-S-sulfanylcysteine
-
-
-
?
L-cysteine + [enzyme]-cysteine
L-alanine + [enzyme]-S-sulfanylcysteine
-
-
-
-
?
L-cysteine + [enzyme]-cysteine
L-alanine + [enzyme]-S-sulfanylcysteine
-
-
-
-
?
L-cysteine + [enzyme]-cysteine
L-alanine + [enzyme]-S-sulfanylcysteine
-
-
-
-
?
L-cysteine + [enzyme]-cysteine
L-alanine + [enzyme]-S-sulfanylcysteine
-
-
-
-
?
L-cysteine + [enzyme]-cysteine
L-alanine + [enzyme]-S-sulfanylcysteine
-
-
-
-
?
L-cysteine + [enzyme]-cysteine
L-alanine + [enzyme]-S-sulfanylcysteine
-
-
-
-
?
L-cysteine + [enzyme]-cysteine
L-alanine + [enzyme]-S-sulfanylcysteine
-
-
-
?
L-cysteine + [enzyme]-cysteine
L-alanine + [enzyme]-S-sulfanylcysteine
-
-
-
-
?
L-cysteine + [enzyme]-cysteine
L-alanine + [enzyme]-S-sulfanylcysteine
-
L-cysteine desulfuration requires a cysteine residue at the active site of the enzyme, but decomposition of L-selenocysteine and L-cysteine sufinic acid do not
-
-
?
L-cysteine + [enzyme]-cysteine
L-alanine + [enzyme]-S-sulfanylcysteine
-
-
-
-
?
L-cysteine + [enzyme]-cysteine
L-alanine + [enzyme]-S-sulfanylcysteine
-
-
-
?
L-cysteine + [SufU]-cysteine

L-alanine + [SufU]-S-sulfanylcysteine
-
-
-
-
?
L-cysteine + [SufU]-cysteine
L-alanine + [SufU]-S-sulfanylcysteine
-
the enzyme is able to reconstitute an Fe/S cluster on SufU
-
-
?
L-cysteine + [SufU]-cysteine
L-alanine + [SufU]-S-sulfanylcysteine
-
-
-
-
?
L-cysteine sulfinic acid

L-alanine + sulfite
-
-
-
-
?
L-cysteine sulfinic acid
L-alanine + sulfite
-
L-cysteine desulfuration requires a cysteine residue at the active site of the enzyme, but decomposition of L-selenocysteine and L-cysteine sufinic acid do not
-
?
L-selenocysteine

L-alanine + selenium
-
-
-
-
?
L-selenocysteine
L-alanine + selenium
-
-
-
-
?
L-selenocysteine
L-alanine + selenium
-
-
-
?
L-selenocysteine
L-alanine + selenium
-
-
-
-
?
L-selenocysteine
L-alanine + selenium
-
-
-
-
?
L-selenocysteine
L-alanine + selenium
-
-
-
?
L-selenocysteine
L-alanine + selenium
-
-
-
?
L-selenocysteine
L-alanine + selenium
-
Cys364 residue is essential for activity toward L-cysteine but not toward L-selenocyteine
-
-
?
L-selenocysteine
L-alanine + selenium
-
-
-
-
?
L-selenocysteine
L-alanine + selenium
-
-
-
-
?
L-selenocysteine
L-alanine + selenium
-
L-cysteine desulfuration requires a cysteine residue at the active site of the enzyme, but decomposition of L-selenocysteine and L-cysteine sufinic acid do not
-
-
?
L-selenocysteine
L-alanine + selenium
-
-
-
-
?
additional information

?
-
-
enzyme is involved in the iron-sulfur cluster assembly
-
-
?
additional information
?
-
-
enzyme catalyzes the formation of Fe-S clusters in a component protein of nitrogenase in the presence of cysteine and ferrous iron in vitro
-
-
?
additional information
?
-
-
enzyme is involved in selenoprotein biosynthesis
-
-
?
additional information
?
-
-
enzyme serves as a selenide delivery protein for the in vitro biosynthesis of selenophosphate
-
-
?
additional information
?
-
-
involved in the mobilization of iron or sulfur required for metallocluster formation
-
-
?
additional information
?
-
-
enzyme participates in the biosynthesis of the nitrogenase metalloclusters by providing the inorganic sulfur required for Fe-S core formation
-
-
?
additional information
?
-
-
NifS specifically mobilizes sulfur for the iron-sulfur (Fe-S) cluster maturation of nitrogenase
-
-
?
additional information
?
-
functions as scaffold for the assembly of [Fe-S] prior to their incorporation into apoproteins
-
-
?
additional information
?
-
-
functions as scaffold for the assembly of [Fe-S] prior to their incorporation into apoproteins
-
-
?
additional information
?
-
-
provides sulfur for [Fe-S] cluster synthesis via its cysteine desulfurase activity for the following enzymes: NADH dehydrogenase, succinate dehydrogenase, glutamate synthase, aconitase B, 6-phophogluconate dehydratase, fumarase A, isocitrate dehydrogenase
-
-
?
additional information
?
-
-
isc genes are involved in the formation of Fe-S clusters in various Fe-S proteins
-
-
?
additional information
?
-
-
enzyme is involved in selenoprotein biosynthesis
-
-
?
additional information
?
-
-
IscS plays a significant and specific role at the top of a potentially broad sulfur transfer cascade that is required for the biosynthesis of thiamine, NAD, [Fe-S] clusters and thionucleosides
-
-
?
additional information
?
-
-
acts as sulfurtransferase in biosynthesis of 4-thiouridine in tRNA
-
-
?
additional information
?
-
-
enzyme contributes to the biotin synthase reaction, probably by supplying sulfur to the BioB protein
-
-
?
additional information
?
-
-
facilitates the formation of the iron-sulfur cluster of ferredoxin in vitro
-
-
?
additional information
?
-
involved in biosynthesis of 2-thiouridine
-
-
?
additional information
?
-
-
involved in biosynthesis of 2-thiouridine
-
-
?
additional information
?
-
-
involved in biosynthesis of thionucleosides
-
-
?
additional information
?
-
-
involved in biosynthesis of thionucleosides
-
-
?
additional information
?
-
-
involved in thiamine biosynthesis, molybdopterin biosynthesis and tRNA modification
-
-
?
additional information
?
-
-
cysteine desulfurase together with L-cysteine can efficiently repair the nitric oxide-modified ferredoxin [2Fe-2S] cluster and the iron center in the dinitroxyl iron complex may be recycled for the reassembly of iron-sulfur clusters in proteins
-
-
?
additional information
?
-
-
SufA is able to bind sulfur atoms provided by the SufS-SufE complex
-
-
?
additional information
?
-
-
SufS and SufE proteins interact with the SufBCD protein complex to facilitate sulfur liberation from cysteine and donation for Fe-S cluster assembly
-
-
?
additional information
?
-
-
uridine phosphorylase (UPase) and cytidine deaminase (CDA) are significantly down-regulated in the iscS mutant, the expression level of the protein complex YeiT-YeiA is decreased in the iscS mutant, iscS plays an essential role in the expression of pyrimidine metabolism genes and provides a clue to the potential relationship between iscS and global gene regulation
-
-
?
additional information
?
-
-
IscS is involved in the sulfuration of MoaD subunit
-
-
?
additional information
?
-
-
[2Fe-2S]-ferredoxin interacts directly with the enzyme
-
-
?
additional information
?
-
-
IscS is essential for Fe-S cluster assembly in vivo
-
-
?
additional information
?
-
-
the enzyme is capable of donating the persulfide sulfur atoms to a variety of biosynthetic pathways for sulfur-containing biofactors, such as iron-sulfur clusters, thiamin, transfer RNA thionucleosides, biotin, and lipoic acid
-
-
?
additional information
?
-
-
IscS plays a significant and specific role at the top of a potentially broad sulfur transfer cascade that is required for the biosynthesis of thiamine, NAD, [Fe-S] clusters and thionucleosides
-
-
?
additional information
?
-
-
acts as sulfurtransferase in biosynthesis of 4-thiouridine in tRNA
-
-
?
additional information
?
-
-
isc genes are involved in the formation of Fe-S clusters in various Fe-S proteins
-
-
?
additional information
?
-
the enzyme is involved in Fe-S cluster assembly in haloarchaea
-
-
?
additional information
?
-
-
the enzyme is involved in Fe-S cluster assembly in haloarchaea
-
-
?
additional information
?
-
the enzyme is involved in Fe-S cluster assembly in haloarchaea
-
-
?
additional information
?
-
-
NFS1 acts as the sulfur donor for the C-terminal domain of MOCS3 protein (a cytosolic protein involved in molybdenum cofactor biosynthesis and tRNA thiolation)
-
-
?
additional information
?
-
-
enzyme participates in biotin synthase reaction, probably by supplying sulfur to the iron-sulfur cluster of biotin synthase
-
-
?
additional information
?
-
-
cysteine desulfurase participates in the biosynthesis of the iron-molybdenum cofactor of nitrogenase as the major provider of Fe-S clusters, but it is not essential to synthesize active nitrogenase
-
-
?
additional information
?
-
-
enzyme participates in biotin synthase reaction, probably by supplying sulfur to the iron-sulfur cluster of biotin synthase
-
-
?
additional information
?
-
-
the enzyme Lecsl has both cysteine sulfoxide lyase and cysteine desulfurase activity
-
-
?
additional information
?
-
-
HapE is a bifunctional enzyme which has both the cysteine desulfurase activity to produce alanine and the cysteine desulfhydrase activity to produce pyruvate and hydrogen sulfide
-
-
?
additional information
?
-
-
isc genes are involved in the formation of Fe-S clusters in various Fe-S proteins
-
-
?
additional information
?
-
-
enzyme NifS4 is involved in formation of the Mo-S ligand of Moco. It mobilizes sulfur by formation of a protein-bound persulfide intermediate and transfers this sulfur further to Moco. Moco is sulfurated before the insertion into xanthine dehydrogenase, while it is bound to XdhC
-
-
?
additional information
?
-
-
NifS4 is involved in the formation of the Mo=S ligand of molybdenum cofactor. NifS4 mobilizes sulfur from L-cysteine by formation of a protein-bound persulfide intermediate and transfers this sulfur further to molybdenum cofactor. Molybdenum cofactor is sulfurated before the insertion into XDH, while it is bound to XdhC
-
-
?
additional information
?
-
-
involved in the production of sulfur for the mormation of iron-sulfur clusters
-
-
?
additional information
?
-
-
-
-
-
?
additional information
?
-
-
enzyme is required for synthesis of both mitochondrial and cytosolic Fe/S proteins, biosynthesis of Fe/S clusters is initiated in the mitochondrial matrix by the cysteine desulfurase Nfs1p, which provides elemental sulfur for biogenesis
-
-
?
additional information
?
-
-
cysteine desulfurase is required for the proper post-translational modification of the lipoamide-containing mitochondrial subproteome in yeast
-
-
?
additional information
?
-
-
Nfs1 mediates assembly of the Fe-S cluster of both mitochondrial and cytosolic Fe-S proteins in the mitochondrial Fe-S assembly system
-
-
?
additional information
?
-
-
involved in biosynthesis of thionucleosides
-
-
?
additional information
?
-
-
the synthesis of 4-thiouridine and 5-methylaminomethyl-2-thiouridine occurs by a transfer of sulfur from enzyme IscS via various proteins to the target nucleoside in the tRNA, and no iron-sulfur cluster protein participates, whereas the synthesis of 2-thiocytidine and N6-(4-hydroxyisopentenyl)-2-methylthioadenosine is dependent on iron-sulfur cluster proteins, whose formation and maintenance depend on IscS
-
-
?
additional information
?
-
-
cysteine desulfurase DndA catalyzes iron-sulfur cluster assembly by activation of apo-Fe DndC protein
-
-
?
additional information
?
-
cysteine desulfurase DndA catalyzes iron-sulfur cluster assembly by activation of apo-Fe DndC protein
-
-
?
additional information
?
-
-
no substrate: L-cystine, L-selenocystine
-
-
?
additional information
?
-
no substrate: L-cystine, L-selenocystine
-
-
?
additional information
?
-
-
substrate specificity similar to that of Escherichia coli IscS
-
-
?
additional information
?
-
substrate specificity similar to that of Escherichia coli IscS
-
-
?
additional information
?
-
-
no substrates are L-cystine, L-selenocystine
-
-
?
additional information
?
-
no substrates are L-cystine, L-selenocystine
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
L-cysteine
L-alanine + sulfur
DndA is able to directly activate apo-Fe DndC for its reconstitution as a fully functional [4Fe-4S] cluster protein (DndC) with unambiguously demonstrated ATP pyrophosphatase activity
-
-
?
L-cysteine + acceptor
L-alanine + S-sulfanyl-acceptor
L-cysteine + enzyme-cysteine
L-alanine + enzyme-S-sulfanylcysteine
-
involved in the formation of Fe-S proteins
-
-
?
L-cysteine + IscS
L-alanine + IscS-SSH
L-cysteine + MOC3 protein
L-alanine + S-sulfanyl-MOC3 protein
-
-
-
-
?
L-cysteine + RhdA
L-alanine + RhdA-SSH
-
-
-
-
?
L-cysteine + Slr0077
L-alanine + Slr0077-SSH
-
-
-
-
?
L-cysteine + SufE
L-alanine + S-sulfanyl-SufE
-
-
-
-
?
L-cysteine + SufS
L-alanine + SufS-SSH
L-cysteine + [enzyme]-cysteine
L-alanine + [enzyme]-S-sulfanylcysteine
additional information
?
-
L-cysteine + acceptor

L-alanine + S-sulfanyl-acceptor
-
-
-
-
?
L-cysteine + acceptor
L-alanine + S-sulfanyl-acceptor
-
-
-
?
L-cysteine + acceptor
L-alanine + S-sulfanyl-acceptor
-
-
-
?
L-cysteine + acceptor
L-alanine + S-sulfanyl-acceptor
-
-
-
?
L-cysteine + acceptor
L-alanine + S-sulfanyl-acceptor
-
-
-
-
?
L-cysteine + acceptor
L-alanine + S-sulfanyl-acceptor
-
-
-
-
?
L-cysteine + acceptor
L-alanine + S-sulfanyl-acceptor
-
-
-
-
?
L-cysteine + acceptor
L-alanine + S-sulfanyl-acceptor
-
-
-
-
?
L-cysteine + acceptor
L-alanine + S-sulfanyl-acceptor
-
-
-
-
?
L-cysteine + acceptor
L-alanine + S-sulfanyl-acceptor
-
-
-
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?
L-cysteine + IscS

L-alanine + IscS-SSH
-
-
-
-
?
L-cysteine + IscS
L-alanine + IscS-SSH
-
-
-
-
?
L-cysteine + SufS

L-alanine + SufS-SSH
-
-
-
-
?
L-cysteine + SufS
L-alanine + SufS-SSH
-
-
-
?
L-cysteine + [enzyme]-cysteine

L-alanine + [enzyme]-S-sulfanylcysteine
-
-
-
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?
L-cysteine + [enzyme]-cysteine
L-alanine + [enzyme]-S-sulfanylcysteine
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-
-
-
?
L-cysteine + [enzyme]-cysteine
L-alanine + [enzyme]-S-sulfanylcysteine
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-
-
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?
L-cysteine + [enzyme]-cysteine
L-alanine + [enzyme]-S-sulfanylcysteine
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-
-
?
L-cysteine + [enzyme]-cysteine
L-alanine + [enzyme]-S-sulfanylcysteine
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-
725215, 645638, 645635, 645634, 645633, 645632, 645630, 645628, 645627, 645616, 645615 -
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?
L-cysteine + [enzyme]-cysteine
L-alanine + [enzyme]-S-sulfanylcysteine
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-
-
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?
L-cysteine + [enzyme]-cysteine
L-alanine + [enzyme]-S-sulfanylcysteine
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-
-
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?
L-cysteine + [enzyme]-cysteine
L-alanine + [enzyme]-S-sulfanylcysteine
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-
-
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?
L-cysteine + [enzyme]-cysteine
L-alanine + [enzyme]-S-sulfanylcysteine
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-
-
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?
L-cysteine + [enzyme]-cysteine
L-alanine + [enzyme]-S-sulfanylcysteine
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-
-
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?
L-cysteine + [enzyme]-cysteine
L-alanine + [enzyme]-S-sulfanylcysteine
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-
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?
additional information

?
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enzyme is involved in the iron-sulfur cluster assembly
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?
additional information
?
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enzyme catalyzes the formation of Fe-S clusters in a component protein of nitrogenase in the presence of cysteine and ferrous iron in vitro
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?
additional information
?
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enzyme is involved in selenoprotein biosynthesis
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?
additional information
?
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enzyme serves as a selenide delivery protein for the in vitro biosynthesis of selenophosphate
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?
additional information
?
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involved in the mobilization of iron or sulfur required for metallocluster formation
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?
additional information
?
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enzyme participates in the biosynthesis of the nitrogenase metalloclusters by providing the inorganic sulfur required for Fe-S core formation
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?
additional information
?
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functions as scaffold for the assembly of [Fe-S] prior to their incorporation into apoproteins
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?
additional information
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functions as scaffold for the assembly of [Fe-S] prior to their incorporation into apoproteins
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?
additional information
?
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uridine phosphorylase (UPase) and cytidine deaminase (CDA) are significantly down-regulated in the iscS mutant, the expression level of the protein complex YeiT-YeiA is decreased in the iscS mutant, iscS plays an essential role in the expression of pyrimidine metabolism genes and provides a clue to the potential relationship between iscS and global gene regulation
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?
additional information
?
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SufS and SufE proteins interact with the SufBCD protein complex to facilitate sulfur liberation from cysteine and donation for Fe-S cluster assembly
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?
additional information
?
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SufA is able to bind sulfur atoms provided by the SufS-SufE complex
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?
additional information
?
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involved in biosynthesis of thionucleosides
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?
additional information
?
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cysteine desulfurase together with L-cysteine can efficiently repair the nitric oxide-modified ferredoxin [2Fe-2S] cluster and the iron center in the dinitroxyl iron complex may be recycled for the reassembly of iron-sulfur clusters in proteins
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?
additional information
?
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involved in thiamine biosynthesis, molybdopterin biosynthesis and tRNA modification
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?
additional information
?
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[2Fe-2S]-ferredoxin interacts directly with the enzyme
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?
additional information
?
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involved in biosynthesis of thionucleosides
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?
additional information
?
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involved in biosynthesis of 2-thiouridine
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?
additional information
?
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involved in biosynthesis of 2-thiouridine
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?
additional information
?
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facilitates the formation of the iron-sulfur cluster of ferredoxin in vitro
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?
additional information
?
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enzyme contributes to the biotin synthase reaction, probably by supplying sulfur to the BioB protein
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?
additional information
?
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acts as sulfurtransferase in biosynthesis of 4-thiouridine in tRNA
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?
additional information
?
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IscS plays a significant and specific role at the top of a potentially broad sulfur transfer cascade that is required for the biosynthesis of thiamine, NAD, [Fe-S] clusters and thionucleosides
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?
additional information
?
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enzyme is involved in selenoprotein biosynthesis
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?
additional information
?
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provides sulfur for [Fe-S] cluster synthesis via its cysteine desulfurase activity for the following enzymes: NADH dehydrogenase, succinate dehydrogenase, glutamate synthase, aconitase B, 6-phophogluconate dehydratase, fumarase A, isocitrate dehydrogenase
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?
additional information
?
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isc genes are involved in the formation of Fe-S clusters in various Fe-S proteins
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?
additional information
?
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acts as sulfurtransferase in biosynthesis of 4-thiouridine in tRNA
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?
additional information
?
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IscS plays a significant and specific role at the top of a potentially broad sulfur transfer cascade that is required for the biosynthesis of thiamine, NAD, [Fe-S] clusters and thionucleosides
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?
additional information
?
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isc genes are involved in the formation of Fe-S clusters in various Fe-S proteins
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?
additional information
?
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the enzyme is involved in Fe-S cluster assembly in haloarchaea
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?
additional information
?
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the enzyme is involved in Fe-S cluster assembly in haloarchaea
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?
additional information
?
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the enzyme is involved in Fe-S cluster assembly in haloarchaea
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?
additional information
?
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enzyme participates in biotin synthase reaction, probably by supplying sulfur to the iron-sulfur cluster of biotin synthase
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?
additional information
?
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cysteine desulfurase participates in the biosynthesis of the iron-molybdenum cofactor of nitrogenase as the major provider of Fe-S clusters, but it is not essential to synthesize active nitrogenase
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?
additional information
?
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enzyme participates in biotin synthase reaction, probably by supplying sulfur to the iron-sulfur cluster of biotin synthase
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?
additional information
?
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the enzyme Lecsl has both cysteine sulfoxide lyase and cysteine desulfurase activity
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?
additional information
?
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isc genes are involved in the formation of Fe-S clusters in various Fe-S proteins
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?
additional information
?
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NifS4 is involved in the formation of the Mo=S ligand of molybdenum cofactor. NifS4 mobilizes sulfur from L-cysteine by formation of a protein-bound persulfide intermediate and transfers this sulfur further to molybdenum cofactor. Molybdenum cofactor is sulfurated before the insertion into XDH, while it is bound to XdhC
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?
additional information
?
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enzyme NifS4 is involved in formation of the Mo-S ligand of Moco. It mobilizes sulfur by formation of a protein-bound persulfide intermediate and transfers this sulfur further to Moco. Moco is sulfurated before the insertion into xanthine dehydrogenase, while it is bound to XdhC
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?
additional information
?
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involved in the production of sulfur for the mormation of iron-sulfur clusters
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?
additional information
?
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?
additional information
?
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cysteine desulfurase is required for the proper post-translational modification of the lipoamide-containing mitochondrial subproteome in yeast
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?
additional information
?
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enzyme is required for synthesis of both mitochondrial and cytosolic Fe/S proteins, biosynthesis of Fe/S clusters is initiated in the mitochondrial matrix by the cysteine desulfurase Nfs1p, which provides elemental sulfur for biogenesis
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?
additional information
?
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the synthesis of 4-thiouridine and 5-methylaminomethyl-2-thiouridine occurs by a transfer of sulfur from enzyme IscS via various proteins to the target nucleoside in the tRNA, and no iron-sulfur cluster protein participates, whereas the synthesis of 2-thiocytidine and N6-(4-hydroxyisopentenyl)-2-methylthioadenosine is dependent on iron-sulfur cluster proteins, whose formation and maintenance depend on IscS
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?
additional information
?
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involved in biosynthesis of thionucleosides
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?
additional information
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substrate specificity similar to that of Escherichia coli IscS
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?
additional information
?
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substrate specificity similar to that of Escherichia coli IscS
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?
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malfunction

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the disruption of the csd gene of Thermococcus kodakarensis, a facultative elemental sulfur-reducing hyperthermophilic archaeon, confers a growth defect evident only in the absence of sulfur. Growth can be restored by the addition of sulfur, but not sulfide
malfunction
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deleting the enzyme renders the cells microaerophilic and hypersensitive to oxidative stress. Moreover, the deletion mutant shows impaired Fe-S cluster-dependent enzyme activity
malfunction
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enzyme mutation leads to a defect in Fe-S synthesis
malfunction
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deleting the enzyme renders the cells microaerophilic and hypersensitive to oxidative stress. Moreover, the deletion mutant shows impaired Fe-S cluster-dependent enzyme activity
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metabolism

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the cysteine desulfurase Nfs1 is required for the increased protein Isu stability occurring after disruption of cluster formation on or transfer from protein Isu. Physical interaction between the Isu and Nfs1 proteins, not the enzymatic activity of Nfs1, is the important factor in increased stability
metabolism
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the enzyme plays an important role in environmental adaptation of the hyperthermophilic archaeon
metabolism
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the enzyme is the sulfur donor for M molybdenum cofactor biosynthesis. The enzyme is able to transfer sulfur to the C-terminal domain of MOCS3, a cytosolic protein involved in molybdenum cofactor biosynthesis and tRNA thiolation
metabolism
SufS protein physically interacts with the Anabaena sulfur acceptor E protein. In the presence of the Anabaena sulfur acceptor E protein, the catalytic efficiency increases 10fold. For sulfur mobilization, the Anabaena sulfur acceptor E protein partners only SufS and not other cysteine desulfurases from Nostoc sp. The conserved cysteine of the SufS or the Anabaena sulfur acceptor E protein is essential for activity but not for their physical association
physiological function

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IscS is the primary physiological sulfur-donating enzyme for the generation of the thiocarboxylate of molybdopterin synthase in molybdopterin biosynthesis
physiological function
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the enzyme provides the sulfur for molybdenum cofactor biosynthesis in human cytosol. The enzyme plays a crucial role in the mitochondrial iron-sulfur cluster biosynthesis and in the thiomodification of mitochondrial and cytosolic tRNAs
physiological function
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the csd gene is necessary for iron-sulfur cluster biosynthesis in the absence of sulfur
physiological function
the enzyme is involved in Fe-S cluster assembly in haloarchaea
physiological function
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the enzyme is a potential virulence factor of Mycoplasma pneumoniae being responsible for haemolysis
physiological function
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the enzyme is involved in iron-sulfur cluster biogenesis and oxidative stress defence
physiological function
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the enzyme is required for the repressor function of rhizobial iron regulator RirA and oxidative resistance in Agrobacterium tumefaciens
physiological function
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cysteine desulfurase (IscS, EC 2.8.1.7), not 3-MST, is the primary source of endogenous H2S in Escherichia coli under anaerobic conditions. A significant decrease in H2S production under anaerobic conditions is observed in Escherichia coli upon deletion of IscS, but not in 3-MST-deficient bacteria. The H2S-producing activity of recombinant IscS using L-cysteine as a substrate exhibits an approximately 2.6fold increase in the presence of dithiothreitol. The activity of IscS is regulated under the different redox conditions and the midpoint redox potential is -329 mV. H2S production from IscS is regulated under oxidative and reductive stress. A mutant strain lacking a chromosomal copy of the IscS-encoding gene iscS shows significant growth defects and low levels of ATP under both aerobic and anaerobic conditions
physiological function
deletion of isoform causes a severe growth defect in the presence of 2% oxygen. The mutation delays colonization in a conventional mouse model of Clostridioides difficile infection and fails to colonize in a germfree model, which has higher intestinal oxygen levels
physiological function
ferredoxins FDX1 and FDX2 in both their reduced and oxidized states interact with the protein complex responsible for mitochondrial iron-sulfur cluster assembly, which contains cysteine desulfurase (NFS1), ISD11 (LYRM4), and acyl carrier protein (Acp). Reduced FDX1 and FDX2 each donate electrons to the cysteine desulfurase complex in vitro and facilitate iron-sulfur cluster assembly. Ferredoxin Both FDX1 and FDX2 stimulate cysteine desulfurase activity. FDX2 binds more tightly to the cysteine desulfurase complex than FDX1 does. The reduced form of each ferredoxin becomes oxidized in the presence of the cysteine desulfurase complex when L-cysteine is added, leading to its conversion to L-alanine and the generation of sulfide
physiological function
overexpression of the SufS protein causes reduced formation of reactive oxygen species on exposure to hydrogen peroxide
physiological function
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SspA can form a complex with SspD, an ATP diphosphatase
physiological function
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the gene product of CPSIT_0959 is expressed midcycle and secreted into the infected cellular cytoplasm via the type III secretion system. Recombinant CPSIT_0959 protein possesses cysteine desulfurase and PLP-binding activity, and helps chlamydial replication. CPSIT_0959 protein improves the infectivity of offspring elementary bodies and seems to promote the replication by its product, which is inhibited by PLP-dependent enzymes inhibitors. CPSIT_0959 protein increases expression of Bim and tBid, and decreases the mitochondrial membrane potential of host mitochondria to induce apoptosis in the late cycle for release of offspring
physiological function
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the growth of Escherichia coli is promoted by over-expressing SufS in vivo or by directly adding recombinant SufS to the medium. The highest cell density of Escherichia coli of 3.5 times that of the control is found when SufS is overexpressed in the presence of sodium thiosulfate
physiological function
-
the enzyme is involved in iron-sulfur cluster biogenesis and oxidative stress defence
-
physiological function
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deletion of isoform causes a severe growth defect in the presence of 2% oxygen. The mutation delays colonization in a conventional mouse model of Clostridioides difficile infection and fails to colonize in a germfree model, which has higher intestinal oxygen levels
-
physiological function
-
cysteine desulfurase (IscS, EC 2.8.1.7), not 3-MST, is the primary source of endogenous H2S in Escherichia coli under anaerobic conditions. A significant decrease in H2S production under anaerobic conditions is observed in Escherichia coli upon deletion of IscS, but not in 3-MST-deficient bacteria. The H2S-producing activity of recombinant IscS using L-cysteine as a substrate exhibits an approximately 2.6fold increase in the presence of dithiothreitol. The activity of IscS is regulated under the different redox conditions and the midpoint redox potential is -329 mV. H2S production from IscS is regulated under oxidative and reductive stress. A mutant strain lacking a chromosomal copy of the IscS-encoding gene iscS shows significant growth defects and low levels of ATP under both aerobic and anaerobic conditions
-
physiological function
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the growth of Escherichia coli is promoted by over-expressing SufS in vivo or by directly adding recombinant SufS to the medium. The highest cell density of Escherichia coli of 3.5 times that of the control is found when SufS is overexpressed in the presence of sodium thiosulfate
-
physiological function
-
the enzyme is involved in Fe-S cluster assembly in haloarchaea
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microbatch-under-oil method, using 20% (w/v) PEG 3000, 0.2 M sodium chloride, 0.1 M HEPES pH 7.5
hanging drop vapor diffusion method, using 0.2 M calcium acetate, 0.1 sodium cacodylate pH 6.5, 40% (v/v) PEG 300
comparison of Helicobacter pylori isoform NifS (type I enzyme) and Bacillus subtilis isoform SufS (type II enzyme). For both, the thiol group of the PLP-L-cysteine external aldimine is stabilized by the conserved histidine adjacent to PLP through a polar interaction, orientating the thiol group for subsequent nucleophilic attack by a conserved cysteine residue on the catalytic loop in the state of PLP-L-cysteine ketimine, which is formed from the PLP-L-cysteine aldimine. In the type I enzyme, conformational and topological change of the loop is necessary for nucleophilic attack by the cysteine. The loop in type II cysteine desulfurase enzymes shows no large conformational change. It might orient the thiol group of the catalytic cysteine for nucleophilic attack toward PLP-L-cysteine
homodimer in complex with pyrodoxal 5'-phosphate, alanine, and Cys361-persulfide, sitting drop vapor diffusion method, using 0.1 M HEPES, pH 7.5, 50% (w/v) PEG 400
structure of the SufS homodimer which adopts a state in which the two monomers are rotated relative to their resting state, displacing a beta-hairpin from its typical position blocking transpersulfurase access to the SufS active site. The active-site beta-hairpin is likely to require adjacent structural elements to function as a beta-latch regulating access to the SufS active site
structure of a SufS Cys-aldimine, a SufS Cys-ketimine and structure of mutant H123A which shows loss of the pi-pi stacking or H-bonding interactions from His-123
structures of SufS including a structure containing an inward-facing persulfide intermediate on residue C364. Structures of SufS variants with substitutions at the dimer interface show changes in dimer geometry, a conserved beta-hairpin structure may play a role in mediating interactions with SufE
hanging drop vapor diffusion method, complexed with L-propargylglycine
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CsdA and CsdACsdE complex, hanging drop vapor diffusion method, using 20-30% (w/v) PEG 8000, 0.05 M potassium di-hydrogen phosphate, and 0.1 M MES, pH 6.5 (or pH 5.5), or 20-30% (w/v) PEG 8000, 0.05 M sodium di-hydrogen phosphate, and 0.1 M MES, pH 6.5 (or 0.1 M Tris, pH 8.5)
structures of SufS including a structure containing an inward-facing persulfide intermediate on residue C364. Structures of SufS variants with substitutions at the dimer interface show changes in dimer geometry, a conserved beta-hairpin structure may play a role in mediating interactions with SufE
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comparison of Helicobacter pylori isoform NifS (type I enzyme) and Bacillus subtilis isoform SufS (type II enzyme). For both, the thiol group of the PLP-L-cysteine external aldimine is stabilized by the conserved histidine adjacent to PLP through a polar interaction, orientating the thiol group for subsequent nucleophilic attack by a conserved cysteine residue on the catalytic loop in the state of PLP-L-cysteine ketimine, which is formed from the PLP-L-cysteine aldimine. In the type I enzyme, conformational and topological change of the loop is necessary for nucleophilic attack by the cysteine. The loop in type II cysteine desulfurase enzymes shows no large conformational change. It might orient the thiol group of the catalytic cysteine for nucleophilic attack toward PLP-L-cysteine
the cysteine desulfurase complex consists of a catalytic subunit (NFS1), LYR protein (ISD11), and acyl carrier protein (ACP). A pair of ISD11 subunits form the dimeric core of the complex. The quaternary structure results in an incompletely formed substrate channel and solvent-exposed pyridoxal 5'-phosphate cofactor. The 4'-phosphopantetheine-conjugated acyl-group of ACP occupies the hydrophobic core of ISD11. In a a lock-and-keymodel ISD11 proteins associate with acyl-ACP as a mechanism for fatty acid biosynthesis to coordinate the expression, Fe-S cofactor maturation, and activity of the respiratory complexes
homology modeling of structure
C327S mutant in complex with pyridoxal 5'-phosphate and in the absence of L-cysteine, hanging drop vapor diffusion method, using 20% (w/v) PEG 3350, 0.1 M sodium acetate, pH 5.5, and 0.2 M ammonium citrate
structures of CDS, including native internal aldimine, gem-diamine with alanine, internal aldimine structure with existing alanine, and internal aldimine with persulfide-bound Cys356 structures. The catalytic intermediate structures show the dihedral angle rotation of Schiff-base linkage relative to the PLP pyridine ring
structure of mutant C314S in complex with substrate, cysteine, and cofactor, pyridoxal phosphate, at a resolution of 1.80 A. A conformational change is observed in the active site region toward the cysteine substrate to move them close to each other to facilitate the nucleophilic attack
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C384S
the variant mimicks the resting state of the enzyme
C325A
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no cysteine desulfurase activity
C369S
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no enzyme activity
E96A
about 6fold decrease in kcat/Km value, mutant displays altered dimer geometries
R379A
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significant loss of activity towards L-selenocysteine
S326A
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mutant defective in Fe-S biosynthesis in vivo but functional in persulfide formation and transfer in vitro
E250A
about 7fold decrease in kcat/Km value, mutant displays altered dimer geometries
E96A
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about 6fold decrease in kcat/Km value, mutant displays altered dimer geometries
L333A
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mutant defective in Fe-S biosynthesis in vivo but functional in persulfide formation and transfer in vitro
R92A
about 3fold decrease in kcat/Km value, dimer geometry is identical to that of wild-type
C358A
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CSD mutant, activity towards L-cysteine is almost completely abolished, activity toward L-selenocysteine is much less affected
C328A
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IscS mutant, activity towards L-cysteine is almost completely abolished, activity toward L-selenocysteine is much less affected
S326A
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mutant defective in Fe-S biosynthesis in vivo but functional in persulfide formation and transfer in vitro
-
L333A
-
mutant defective in Fe-S biosynthesis in vivo but functional in persulfide formation and transfer in vitro
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C374S
complete loss of sulfur desulfurase activity
C421A
-
the mutant has a background desulfurase activity level compared to the wild type enzyme
C327S
no residual cysteine desulfurase activity, mutant is not able to reactivate apo-Fe DndC protein
C327S
sited-directed mutagenesis, no cysteine desulfurase activity, no ability to reactivate the apo-Fe DndC
C372A
active enzyme via a second pathway
C326A
-
inactive,the mutant enzyme is incapable of nucleophilic attack on the sulfur of the substrate L-cysteine
C314S
-
loss of actalytic activity
C361A

-
the mutant is able to interact with SufU and to equally binds cysteine, but it does not generate alanine or sulfide in the presence of SufU, cysteine, and dithiothreitiol
C361A
-
the mutant is able to interact with SufU and to equally binds cysteine, but it does not generate alanine or sulfide in the presence of SufU, cysteine, and dithiothreitiol
-
H123A

-
decreased specific activity towards L-selenocysteine
H123A
mutation abolishes the ability of SufS to generate persulfide from L-cysteine. His123 acts to protonate the Ala-enamine intermediate
H55A

-
normal activity towards L-selenocysteine and L-cysteine
H55A
about 3fold increase in kcat/Km value
C364A

mutation abolishes the ability of SufS to generate persulfide from L-cysteine. Cys364 is essential for positioning the Cys-aldimine for Calpha deprotonation
C364A
-
CsdB mutant, activity towards L-cysteine is almost completely abolished, activity toward L-selenocysteine is much less affected
C327S

inactive
C327S
-
no residual cysteine desulfurase activity, mutant is not able to reactivate apo-Fe DndC protein
additional information

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plants with reduced cysteine desulfurase expression due to RNA interference exhibit chlorosis, a disorganized chloroplast structure, and stunted growth and eventually become necrotic and die before seed set. Photosynthetic electron transport and carbon dioxide assimilation are severely impaired. Silencing of chloroplastic cysteine desulfurase decreases the abundance of all chloroplastic Fe/S proteins tested, mitochondrial proteins and respiratory chain are not affected
additional information
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chloroplastic NifS-like protein (CpNifS)-knockdown plants, reduced CpNifS expression exhibits chlorosis, a disorganized chloroplast structure, and stunted growth, photosynthetic electron transport and carbon dioxide assimilation are severely impaired. The silencing of CpNifS decreases the abundance of all chloroplastic Fe-S proteins tested, CpNifS silencing has no effects on mitochondrial Fe-S protein levels or respiration, suggesting that the mitochondrial Fe-S biogenesis machinery does not depend on CpNifS
additional information
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deletion of the iscS gene, tRNA from this mutant contains less than 5% of the level of sulfur found in the parent strain
additional information
-
deletion of the iscS gene results in a mutant strain that lacks 4-thiouridine in its tRNA
additional information
-
deletion of the iscS gene results in a mutant strain that lacks 4-thiouridine in its tRNA
-
additional information
-
depletion of cysteine desulfurase in HeLa cells by small interfering RNA approach results in a drastic growth retardation and striking morphological changes of mitochondria. Activities of both mitochondrial and cytosolic Fe/S proteins are strongly impaired
additional information
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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
additional information
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
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identification of proteins with increased amounts in a mutant lacking cysteine desulfurase activity. Proteins include lipoamide-containing enzyme complexes: subunits of the mitochondrial alpha-ketoglutarate dehydrogenase, pyruvate dehydroganse, and glycine cleavage system complexes
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selection of mutants defective either in the synthesis of a thiolated nucleoside 5-methylaminomethyl-2-thiouridine specific for the iron-sulfur protein-independent pathway or in the synthesis of a thiolated nucleoside N6-(4-hydroxyisopentenyl)-2-methylthioadenosine specific for the iron-sulfur protein-dependent pathway. Alterations in the C-terminal region of enzyme reduce the level of only N6-(4-hydroxyisopentenyl)-2-methylthioadenosine
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