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Information on EC 2.8.1.7 - cysteine desulfurase
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2.8.1.7 cysteine desulfuraseIUBMB Comments
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 .
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Word Map
- 2.8.1.7
-
iron-sulfur
- fe-s
- iscu
- persulfide
- frataxin
-
nifs-like
- friedreich
- sufe
- moco
-
plp-dependent
-
sulfane
-
molybdoenzymes
-
thionucleosides
-
desulfuration
- 2-thiouridine
- nifu
-
35scysteine
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
Reaction Schemes
Synonyms
c-ISCS, CD0387, CpNifS, CSD, CsdA, CsdB, CysD, cysteine desulfurase, cysteine desulphurase, cysteine:SufU sulfurtransferase, 
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
CSD
CsdA
CsdB
cysteine desulfurase
cysteine desulphurase
cysteine:SufU sulfurtransferase
cysteinedesulfurylase
-
-
-
-
DndA
IscS
L-cysteine desulfurase
Nfs
Nfs1
Nfs2
NIFS
SufS
CSD
-
-
-
-
CsdB
-
-
-
-
IscS
-
-
-
-
Nfs1
-
-
-
-
NIFS
-
-
-
-
SufS
-
-
-
-
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
L-cysteine + [enzyme]-cysteine = L-alanine + [enzyme]-S-sulfanylcysteine
(1a)
-
-
-
[enzyme]-S-sulfanylcysteine + acceptor = [enzyme]-cysteine + S-sulfanyl-acceptor
(1b)
-
-
-
L-cysteine + acceptor = L-alanine + S-sulfanyl-acceptor
overall reaction
-
-
-
L-cysteine + acceptor = L-alanine + S-sulfanyl-acceptor
mechanism
-
L-cysteine + acceptor = L-alanine + S-sulfanyl-acceptor
mechanism
-
L-cysteine + acceptor = L-alanine + S-sulfanyl-acceptor
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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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
sulfur atom transfer
sulfur atom transfer
-
-
-
-
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PATHWAY SOURCE
PATHWAYS
KEGG
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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].
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CAS REGISTRY NUMBER
COMMENTARY
149371-08-4
-
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
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 + 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 + ?
?
-
in the presence of cysteine, IscS’s 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 iron–sulfur cluster
-
-
?
L-cysteine + N,N-dimethyl-4-phenylenediamine
L-alanine + N,N-dimethyl-4-phenylenediamine sulfate
-
-
-
-
?
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 + [ThiI]-cysteine
L-alanine + [ThiI]-S-sulfanylcysteine
-
-
-
-
?
L-cysteine sulfinic acid + ?
?
cysteine desulfurase DndA catalyzes iron-sulfur cluster assembly by activation of apo-Fe DndC protein
-
-
?
L-cystine + Slr0077
pyruvate + Slr0077-SSH
-
cystine lyase of Slr0077
-
-
?
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 + 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 + RhdA
L-alanine + RhdA-SSH
-
transfer of sulfur to rhodanese with formation of a covalent complex between IscS and RhdA
-
-
?
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 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
-
Cys364 residue is essential for activity toward L-cysteine but not toward L-selenocyteine
-
-
?
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
-
-
?
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
?
-
Q8WQX4
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 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
?
-
-
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.
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
L-cysteine
L-alanine + sulfur
Q460H9
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 + enzyme-cysteine
L-alanine + enzyme-S-sulfanylcysteine
-
involved in the formation of Fe-S proteins
-
-
?
L-cysteine + acceptor
L-alanine + S-sulfanyl-acceptor
-
-
-
-
?
L-cysteine + acceptor
L-alanine + S-sulfanyl-acceptor
-
-
-
-
?
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
P25745
-
-
-
?
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
-
-
-
-
?
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
?
-
-
functions as scaffold for the assembly of [Fe-S] prior to their incorporation into apoproteins
-
-
-
additional information
?
-
Q8WQX4
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
?
-
P25745
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
?
-
-
[2Fe-2S]-ferredoxin interacts directly with the enzyme
-
-
-
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
?
-
D4GYV5
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
?
-
D4GYV5
the enzyme is involved in Fe-S cluster assembly in haloarchaea
-
-
-
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
?
-
-
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
?
-
-
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
?
-
-
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
?
-
Q460H9
substrate specificity similar to that of Escherichia coli IscS
-
-
-
additional information
?
-
-
substrate specificity similar to that of Escherichia coli IscS
-
-
-
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
pyridoxamine 5'-phosphate
the enzyme contains pyridoxamine 5'-phosphate which is catalytically inactive in the cysteine desulfurase reaction, leading to a lack of cysteine desulfurase activity
pyridoxal 5'-phosphate
adding pyridoxal 5'-phosphate to IscS produces an enzyme that displays in vitro L-cysteine desulfurase activity
pyridoxal 5'-phosphate
-
-
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Iron
KCl
0-0.5 M KCl gives optimal activities at around 55-60°C. When the KCl concentration is increased to 2.5-3 M, this optimum temperature shifts to between 70-75°C
Iron
-
iron alone or iron together with sulfide binds to IscS to make IscS-iron or IscS-iron-sulfide complexes. The formation of such complexes allows the activity of IscS to be modulated effectively
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
4-chloromercuribenzoate
-
preincubation dramatically inhibits enzyme activity
dithiothreitol
activity is strongly dependent on the presence of dithiothreitol, with activity increasing up to 46% when the reductant is present in the reaction mixture. Concentrations higher than 5 mM cause an inhibitory effect
Fe2+
-
the low desulfurase activity is caused by the modification of IscS rather than by the formation of FeS in the solution
interferon-gamma
-
downregulation of cysteine desulfurase and its protein partner IscU at both mRNA and protein level by stimulation of macrophages with interferon-gamma; 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
-
lipopolysaccharide
-
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
N-ethylmaleimide
-
preincubation dramatically inhibits enzyme activity
N-iodoacetyl-N'-(5-sulfo-1-naphthyl)ethylenediamine
-
up to 90% inhibition at 5 mM
additional information
-
the SufU C41A variant inhibits SufS in presence of native Suf, while the variants C66A and C128A do not show any competitive effect
-
additional information
-
desulfurase activity is gradually inhibited as the amount of iron and sulfide bound to IscS increases. When 2Fe-2S binds IscS, about 20% of the activity is inhibited, when 8Fe-8S adheres to IscS, about 70% of the activity is inhibited. Thus, the cell is able to modulate its desulfurase activity with the formation of an IscS-iron-sulfide complex
-
additional information
-
CyaYdoes not inhibit the desulfurase activity of Isc
-
additional information
-
exposure of cells to exogenous sources of NO does not alter Nfs1 expression; exposure of macrophages to exogenous sources of nitric oxide does not alter enzyme expression
-
additional information
-
the preformed Nfs1p-Isd11p complex is more resistant to N-ethylmaleimide than the uncomplexed Nfs1p protein
-
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
Isd11p
-
Isd11p is required for the cysteine desulfurase activity of Nfs1p
-
protein Isd11
-
forms a stable complex with Nfs1, prone to aggregation in the absence of Isd11
-
Suf protein family
-
SufE protein can stimulate up to 8fold, addition of the SufBCD complex further stimulates up to 32fold
-
SufE protein
-
the enzyme requires the SufE partner protein to transfer the persulfide to the Fe-S cluster scaffold
-
dithiothreitol
activity is strongly dependent on the presence of dithiothreitol, with activity increasing up to 46% when the reductant is present in the reaction mixture. Concentrations higher than 5 mM cause an inhibitory effect
frataxin
frataxin modulates isoform Nfs1m kinetics, increasing Vmax and decreasing the S0.5 value for L-cysteine
-
frataxin
-
frataxin or a mutant Fe-S scaffold protein (Isu1Sup) with frataxin-bypassing ability stimulates L-cysteine binding to the enzyme
-
pyruvate
-
increases activity of CSD towards L-selenocysteine, but not towards L-cysteine
SufE
-
binding of SufE, a member of the SUF protein system, to SufS stimulates the cysteine desulfurase activity of SufS by 50fold
-
SufE
-
binding of SufE, a member of the SUF protein system, to SufS stimulates the cysteine desulfurase activity of SufS by 50fold
-
additional information
-
in presence of purified recombiant chloroplast protein CpSufE, Vmax value of cysteine desulfurase CpNifS increases over 40fold and the Km value towards cysteine decreases to half. CpSufE addition decreases the affinity of enzyme for selenocysteine, and a mutant CpSufE lacking the single cysteine is not able to stimulate CpNifS
-
additional information
-
the enzyme requires the presence of sulfurtransferases such as SufE proteins for optimal activity
-
additional information
the enzyme requires the presence of sulfurtransferases such as SufE proteins for optimal activity
-
additional information
-
SufE participates in allosteric regulation of the enzyme activity
-
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DISEASE
TITLE OF PUBLICATION
LINK TO PUBMED
Anemia, Hypochromic
Chloroplast iron-sulfur cluster protein maturation requires the essential cysteine desulfurase CpNifS.
Darier Disease
Histochemical study of oxidative enzymes and cysteine desulfurase in familiar benign chronic pemphigus and Darier's disease.
Friedreich Ataxia
Mammalian frataxin controls sulfur production and iron entry during de novo Fe4S4 cluster assembly.
Infections
Envelope protein complexes of Mycobacterium avium subsp. paratuberculosis and their antigenicity.
Pemphigus
Histochemical study of oxidative enzymes and cysteine desulfurase in familiar benign chronic pemphigus and Darier's disease.
Pemphigus, Benign Familial
Histochemical study of oxidative enzymes and cysteine desulfurase in familiar benign chronic pemphigus and Darier's disease.
Tuberculosis
The cysteine desulfurase IscS of Mycobacterium tuberculosis is involved in iron-sulfur cluster biogenesis and oxidative stress defence.
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.003
[SufU]-cysteine
-
in 50 mM MOPS (pH 7.4), temperature not specified in the publication
-
0.086
L-cysteine
-
in 50 mM MOPS (pH 7.4), temperature not specified in the publication
0.11
L-cysteine
-
in 50 mM Tris-HCl (pH 8.0), 10 mM MgCl2, 5 mM dithiothreitol, at 25°C
4.17
L-selenocysteine
-
25°C, pH 7.4, presence of chloroplast protein CpSufE
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.87
[SufU]-cysteine
-
in 50 mM MOPS (pH 7.4), temperature not specified in the publication
-
0.87
L-cysteine
-
in 50 mM MOPS (pH 7.4), temperature not specified in the publication
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kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
290
[SufU]-cysteine
-
in 50 mM MOPS (pH 7.4), temperature not specified in the publication
-
10.1
L-cysteine
-
in 50 mM MOPS (pH 7.4), temperature not specified in the publication
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Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
0.1
knockdown of Nfs-like proteins, activity measured in mitochondrial fractions
0.2
knockdown of selenocysteine lyase, activity measured in mitochondrial fractions
0.5
knockdown of selenocysteine lyase, activity measured in cytosolic fractions
1
knockdown of Nfs-like proteins, activity measured in cytosolic fractions
1.3
-
mutant enzyme C241A, pH and temperature not specified in the publication
3.6
substrate L-cysteine sulfinic acid, pH 8.0, 37°C; substrate L-cysteine sulfinic acid, pH 8.0, 37°C
38.6
substrate L-cysteine, pH 8.0, 37°C; substrate L-selenocysteine, pH 8.0, 37°C
45.7
-
wild type enzyme, pH and temperature not specified in the publication
56.5
substrate L-cysteine, pH 8.0, 37°C; substrate L-selenocysteine, pH 8.0, 37°C
additional information
additional information
no detectable activity for L-selenocystine and L-cystine
additional information
-
no detectable activity for L-selenocystine and L-cystine
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
7
-
isoenzyme SsCsd1 with L-selenocysteine and isoenzyme SsCsd2 with L-selenocysteine and L-cysteine sulfinic acid as substrates
7.5
maximal activity is obtained in 50 mM phosphate buffer, pH7.5, 2 M KCl at 65°C
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
6.5 - 10
pH 6.5: about 45% of maximal activity, pH 10.0: about 45% of maximal activity
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
37
55 - 60
0-0.5 M KCl gives optimal activities at around 55-60°C.When the KCl concentration is increased to 2.5-3 M, this optimum temperature shifts to between 70-75°C
70 - 75
0-0.5 M KCl gives optimal activities at around 55-60°C.When the KCl concentration is increased to 2.5-3 M, this optimum temperature shifts to between 70-75°C
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pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
strain DH5a and mutant desulfurase deficient strains csdA::Kn, csdB::Kn, ascS::Kn
-
-
brenda
YPH499as WT, GAL10-ISD11 as Isd11-depleted strain
-
-
brenda
; strain ATCC 23270, expression in Escherichia coli BL21 (DE3)
-
-
brenda
-
645614, 645615, 645616, 645626, 645630, 645632, 645633, 645634, 645635, 645637, 661771, 662209, 674798, 692336, 704679, 705872, 724057, 725215, 726388, 737712, 738600
-
-
brenda
strain DH5a and mutant desulfurase deficient strains csdA::Kn, csdB::Kn, ascS::Kn
-
-
brenda
-
-
-
brenda
expression in Escherichia coli BL21(DE3) pLysE, expression vector pET15b
TrEMBL
brenda
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
Q8WQX4
enzyme has an N-terminal targeting signal that directs the enzyme to mitochondria when expressed in Saccharomyces cerevisiae
brenda
-
mitochondrial Nfs1p is required for the biogenesis of both mitochondrial and extramitochondrial Fe/S proteins
brenda
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
malfunction
metabolism
physiological function
malfunction
-
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
-
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
-
deleting the enzyme renders the cells microaerophilic and hypersensitive to oxidative stress. Moreover, the deletion mutant shows impaired Fe-S cluster-dependent enzyme activity
-
metabolism
-
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
-
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
-
the enzyme plays an important role in environmental adaptation of the hyperthermophilic archaeon
physiological function
-
IscS is the primary physiological sulfur-donating enzyme for the generation of the thiocarboxylate of molybdopterin synthase in molybdopterin biosynthesis
physiological function
-
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
the enzyme is involved in Fe-S cluster assembly in haloarchaea
physiological function
-
the csd gene is necessary for iron-sulfur cluster biosynthesis in the absence of sulfur
physiological function
-
the enzyme is involved in iron-sulfur cluster biogenesis and oxidative stress defence
physiological function
-
the enzyme is required for the repressor function of rhizobial iron regulator RirA and oxidative resistance in Agrobacterium tumefaciens
physiological function
-
the enzyme is a potential virulence factor of Mycoplasma pneumoniae being responsible for haemolysis
physiological function
-
the enzyme is involved in Fe-S cluster assembly in haloarchaea
-
physiological function
-
the enzyme is involved in iron-sulfur cluster biogenesis and oxidative stress defence
-
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PDB
SCOP
CATH
UNIPROT
ORGANISM
Archaeoglobus fulgidus (strain ATCC 49558 / VC-16 / DSM 4304 / JCM 9628 / NBRC 100126)
Bacillus subtilis (strain 168)
Escherichia coli (strain K12)
Helicobacter pylori (strain ATCC 700392 / 26695)
Legionella pneumophila subsp. pneumophila (strain Philadelphia 1 / ATCC 33152 / DSM 7513)
Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Synechocystis sp. (strain PCC 6803 / Kazusa)
Thermococcus onnurineus (strain NA1)
Archaeoglobus fulgidus (strain ATCC 49558 / VC-16 / DSM 4304 / JCM 9628 / NBRC 100126)
Archaeoglobus fulgidus (strain ATCC 49558 / VC-16 / DSM 4304 / JCM 9628 / NBRC 100126)
Archaeoglobus fulgidus (strain ATCC 49558 / VC-16 / DSM 4304 / JCM 9628 / NBRC 100126)
Archaeoglobus fulgidus (strain ATCC 49558 / VC-16 / DSM 4304 / JCM 9628 / NBRC 100126)
Helicobacter pylori (strain ATCC 700392 / 26695)
Helicobacter pylori (strain ATCC 700392 / 26695)
Helicobacter pylori (strain ATCC 700392 / 26695)
Helicobacter pylori (strain ATCC 700392 / 26695)
Helicobacter pylori (strain ATCC 700392 / 26695)
Helicobacter pylori (strain ATCC 700392 / 26695)
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
42000
45000
46000
47000
88000
45000
-
x * 45000, SDS-PAGE, high-molecular-weight complex of Nfs1 and Isd11, gel filtration
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
dimer
homodimer
monomer
-
1 * 46000, SDS-PAGE and modeling of structure; 46000
polymer
tetramer
additional information
dimer
subunit 45000, homodimer 91000, purified soluble DndA protein, gel filtration with a Superose 12 10/30 column
dimer
a large domain that binds pyridoxal-5'-phosphate and a smaller domain with the active site cysteine
polymer
-
x * 45000, SDS-PAGE, high-molecular-weight complex of Nfs1 and Isd11, gel filtration
polymer
-
x * 45000, SDS-PAGE, high-molecular-weight complex of Nfs1 and Isd11, gel filtration
-
additional information
-
enzyme CpNifS forms dynamic complexes with chloroplast protein CpSufE
additional information
-
cysteine desulfurase SufS interacts with protein SufE which transfers sulfur to the SufBCD complex to facilitate sulfur liberation from cysteine and donation for Fe-cluster assembly
additional information
-
enzyme forms a complex in vitro with overexpressed cytosolic scaffold protein ISCU
additional information
-
cysteine desulfurase NifS4 interacts with XdhC, but not with xanthine dehydrogenase
additional information
-
N-terminal beta-strand of residues 99-104 is essential for the function of Nfs1p
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POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
proteolytic modification
proteolytic modification
-
after lysis of mitochondria with detergents
proteolytic modification
-
after lysis of mitochondria with detergents
-
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CRYSTALLIZATION/commentary
ORGANISM
UNIPROT
LITERATURE
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
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
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)
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
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
C361A
C328A
-
IscS mutant, activity towards L-cysteine is almost completely abolished, activity toward L-selenocysteine is much less affected
C358A
-
CSD mutant, activity towards L-cysteine is almost completely abolished, activity toward L-selenocysteine is much less affected
C364A
-
CsdB mutant, activity towards L-cysteine is almost completely abolished, activity toward L-selenocysteine is much less affected
L333A
-
mutant defective in Fe-S biosynthesis in vivo but functional in persulfide formation and transfer in vitro
S326A
-
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
-
S326A
-
mutant defective in Fe-S biosynthesis in vivo but functional in persulfide formation and transfer in vitro
-
C421A
-
the mutant has a background desulfurase activity level compared to the wild type enzyme
C327S
C326A
-
inactive,the mutant enzyme is incapable of nucleophilic attack on the sulfur of the substrate L-cysteine
additional information
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
-
C327S
no residual cysteine desulfurase activity, mutant is not able to reactivate apo-Fe DndC protein; sited-directed mutagenesis, no cysteine desulfurase activity, no ability to reactivate the apo-Fe DndC
additional information
-
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; 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
-
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
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
additional information
-
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
-
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
additional information
-
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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pH STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
5 - 10
-
about 45% residual activity at pH 7.5 and 9.5, almost no activity at pH 5.0 and 10.0
706851
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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
40 - 55
-
the enzyme is relatively stable at 40°C with 67% loss of activity, and unstable at temperatures above 55°C
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
4°C, purified protein can be stored one month without loss of activity
-
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PURIFICATION/commentary
ORGANISM
UNIPROT
LITERATURE
ammonium sulfate precipitation, column chromatography, and Superose 12 gel filtration
DEAE-Toyopearl column chromatography and phenyl-Toyopearl column chromatography
-
HiTrap chelating column chromatography, and gel filtration
Ni2+-NTA affinity column chromatography, Source 30Q anion exchange chromatography, and Superdex 200 gel filtration
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CLONED/commentary
ORGANISM
UNIPROT
LITERATURE
; expression in Escherichia coli BL21(DE3) pLysE, expression vector pET15b
expressed in Escherichia coli BL21(DE3) cells
expression in Escherichia coli
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EXPRESSION
ORGANISM
UNIPROT
LITERATURE
the IscS activity is stimulated up to 1.6fold in the presence of 10fold molar excess of MoeB subunit, the addition of MoaD subunit to a mixture of IscS and MoeB subunit detectably enhances the desulfurase activity to levels much higher than those observed for the addition of MoeB subunit alone to IscS
-
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
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YEAR
ORGANISM (UNIPROT)
PUBMED ID
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Azotobacter vinelandii
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brenda
Nilsson, K.; Lundgren, H.K.; Hagervall, T.G.; Bjork, G.R.
The cysteine desulfurase IscS is required for synthesis of all five thiolated nucleosides present in tRNA from Salmonella enterica serovar typhimurium
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184
6830-6835
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Escherichia coli, Salmonella enterica
brenda
Outten, F.W.; Wood, M.J.; Munoz, F.M.; Storz, G.
The SufE protein and the SufBCD complex enhance SufS cysteine desulfurase activity as part of a sulfur transfer pathway for Fe-S cluster assembly in Escherichia coli
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Escherichia coli
brenda
Yang, W.; Rogers, P.A.; Ding, H.
Repair of nitric oxide-modified ferredoxin [2Fe-2S] cluster by cysteine desulfurase (IscS)
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277
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Escherichia coli
brenda
Zheng, L.; White, R.H.; Cash, V.L.; Dean, D.R.
Mechanism for the desulfurization of L-cysteine catalyzed by the nifS gene product
Biochemistry
33
4714-4720
1994
Azotobacter vinelandii
brenda
Schwartz, C.J.; Djaman, O.; Imlay, J.A.; Kiley, P.J.
The cysteine desulfurase, IscS, has a major role in in vivo Fe-S cluster formation in Escherichia coli
Proc. Natl. Acad. Sci. USA
97
9009-9014
2000
Escherichia coli
brenda
Kurihara, T.; Mihara, H.; Kato, S.; Yoshimura, T.; Esaki, N.
Assembly of iron-sulfur clusters mediated by cysteine desulfurases, IscS, CsdB and CSD, from Escherichia coli
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1647
303-309
2003
Escherichia coli
brenda
LaGier, M.J.; Tachezy, J.; Stejskal, F.; Kutisova, K.; Keithly, J.S.
Mitochondrial-type iron-sulfur cluster biosynthesis genes (IscS and IscU) in the apicomplexan Cryptosporidium parvum
Microbiology
149
3519-3530
2003
Cryptosporidium parvum, Cryptosporidium parvum (Q8WQX4)
brenda
Kirby, J.; Wright, F.; Flint, H.J.
A cysteine desulphurase gene from the cellulolytic rumen anaerobe Ruminococcus flavefaciens
Biochim. Biophys. Acta
1368
233-237
1998
Ruminococcus flavefaciens
-
brenda
Kessler, D.
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320
571-577
2004
Synechocystis sp.
brenda
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43
12210-12219
2004
Synechocystis sp. (Q55793), Synechocystis sp.
brenda
Behshad, E.; Parkin, S.E.; Bollinger, J.M.jr.
Mechanism of cysteine desulfurase Slr0387 from Synechocystis sp. PCC 6803: Kinetic analysis of cleavage of the persulfide intermediate by chemical reductants
Biochemistry
43
12220-12226
2004
Synechocystis sp.
brenda
Adam, A.C.; Bornhövd, C.; Prokisch, H.; Neupert, W.; Hell, K.
the Nfs1 interacting protein Isd11 has an essential role in Fe/S cluster biogenesis in mitochondria
EMBO J.
25
174-183
2006
Saccharomyces cerevisiae, Saccharomyces cerevisiae Isd11-depleted
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The cysteine-desulfurase IscS promotes the production of the rhodanese RhdA in the persulfurated form
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579
6786-6790
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Escherichia coli
brenda
Nakai, Y.; Umeda, N.; Suzuki, T.; Nakai, M.; Hayashi, H.; Watanabe, K.; Kagamiyama, H.
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279
12363-12368
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Saccharomyces cerevisiae
brenda
Lauhon, C.T.; Skovran, E.; Urbina, H.D.; Downs, D.M.; Vickery, L.E.
Substitutions in an active site loop of Escherichia coli IscS result in specific defects in Fe-S cluster and thionucleoside biosynthesis in vivo
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279
19551-19558
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Escherichia coli, Escherichia coli MC1061
brenda
Muhlenhoff, U.; Balk, J.; Richhardt, N.; Kaiser, J.T.; Sipos, K.; Kispal, G.; Lill, R.
Functional characterization of the eukaryotic cysteine desulfurase Nfs1p from Saccharomyces cerevisiae
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279
36906-36915
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Saccharomyces cerevisiae
brenda
Liew, Y.F.; Shaw, N.S.
Mitochondrial cysteine desulfurase iron-sulfur cluster S and aconitase are post-transcriptionally regulated by dietary iron in skeletal muscle of rats
J. Nutr.
135
2151-2158
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Rattus norvegicus (Q99P39), Rattus norvegicus
brenda
Rojas, D.M.; Vasquez, C.C.
Sensitivity to potassium tellurite of Escherichia coli cells deficient in CSD, CsdB and IscS cysteine desulfurases
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156
465-471
2005
Escherichia coli, Escherichia coli DH5-alpha
brenda
Canal, F.; Fosset, C.; Chauveau, M.J.; Drapier, J.C.; Bouton, C.
Regulation of the cysteine desulfurase Nfs1 and the scaffold protein IscU in macrophages stimulated with interferon-gamma and lipopolysaccharide
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465
282-292
2007
Mus musculus
brenda
You, D.; Wang, L.; Yao, F.; Zhou, X.; Deng, Z.
A novel DNA modification by sulfur: DndA is a NifS-like cysteine desulfurase capable of assembling DndC as an iron-sulfur cluster protein in Streptomyces lividans
Biochemistry
46
6126-6133
2007
Streptomyces lividans (Q460H9), Streptomyces lividans
brenda
Neumann, M.; Stoecklein, W.; Walburger, A.; Magalon, A.; Leimkuehler, S.
Identification of a Rhodobacter capsulatus L-cysteine desulfurase that sulfurates the molybdenum cofactor when bound to XdhC and before its insertion into xanthine dehydrogenase
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46
9586-9595
2007
Rhodobacter capsulatus
brenda
Zeng, J.; Zhang, Y.; Liu, Y.; Zhang, X.; Xia, L.; Liu, J.; Qiu, G.
Expression, purification and characterization of a cysteine desulfurase, IscS, from Acidithiobacillus ferrooxidans
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1983-1990
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Acidithiobacillus ferrooxidans
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Structural alterations of the cysteine desulfurase IscS of Salmonella enterica serovar Typhimurium reveal substrate specificity of IscS in tRNA thiolation
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188
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Salmonella enterica
brenda
Li, K.; Tong, W.H.; Hughes, R.M.; Rouault, T.A.
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281
12344-12351
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Homo sapiens
brenda
Fosset, C.; Chauveau, M.J.; Guillon, B.; Canal, F.; Drapier, J.C.; Bouton, C.
RNA silencing of mitochondrial m-Nfs1 reduces Fe-S enzyme activity both in mitochondria and cytosol of mammalian cells
J. Biol. Chem.
281
25398-25406
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Mus musculus (Q9Z1J3)
brenda
Ye, H.; Abdel-Ghany, S.E.; Anderson, T.D.; Pilon-Smits, E.A.; Pilon, M.
CpSufE activates the cysteine desulfurase CpNifS for chloroplastic Fe-S cluster formation
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281
8958-8969
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Arabidopsis thaliana
brenda
Layer, G.; Gaddam, S.A.; Ayala-Castro, C.N.; Ollagnier-de Choudens, S.; Lascoux, D.; Fontecave, M.; Outten, F.W.
SufE transfers sulfur from SufS to SufB for iron-sulfur cluster assembly
J. Biol. Chem.
282
13342-13350
2007
Escherichia coli
brenda
Zhao, D.; Curatti, L.; Rubio, L.M.
Evidence for nifU and nifS participation in the biosynthesis of the iron-molybdenum cofactor of nitrogenase
J. Biol. Chem.
282
37016-37025
2007
Klebsiella pneumoniae
brenda
Biederbick, A.; Stehling, O.; Roesser, R.; Niggemeyer, B.; Nakai, Y.; Elsaesser, H.P.; Lill, R.
Role of human mitochondrial Nfs1 in cytosolic iron-sulfur protein biogenesis and iron regulation
Mol. Cell. Biol.
26
5675-5687
2006
Homo sapiens, Mus musculus
brenda
Onder, O.; Yoon, H.; Naumann, B.; Hippler, M.; Dancis, A.; Daldal, F.
Modifications of the lipoamide-containing mitochondrial subproteome in a yeast mutant defective in cysteine desulfurase
Mol. Cell. Proteomics
5
1426-1436
2006
Saccharomyces cerevisiae
brenda
Van Hoewyk, D.; Abdel-Ghany, S.E.; Cohu, C.M.; Herbert, S.K.; Kugrens, P.; Pilon, M.; Pilon-Smits, E.A.
Chloroplast iron-sulfur cluster protein maturation requires the essential cysteine desulfurase CpNifS
Proc. Natl. Acad. Sci. USA
104
5686-5691
2007
Arabidopsis thaliana
brenda
Mihara, H.; Hidese, R.; Yamane, M.; Kurihara, T.; Esaki, N.
The iscS gene deficiency affects the expression of pyrimidine metabolism genes
Biochem. Biophys. Res. Commun.
372
407-411
2008
Escherichia coli
brenda
Wu, G.; Li, P.; Wu, X.
Regulation of Escherichia coli IscS desulfurase activity by ferrous iron and cysteine
Biochem. Biophys. Res. Commun.
374
399-404
2008
Escherichia coli
brenda
Sendra, M.; Ollagnier de Choudens, S.; Lascoux, D.; Sanakis, Y.; Fontecave, M.
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581
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2007
Escherichia coli
brenda
Behshad, E.; Bollinger, J.M.
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Biochemistry
48
12014-12023
2009
Synechocystis sp.
brenda
Poliak, P.; Van Hoewyk, D.; Obornik, M.; Zikova, A.; Stuart, K.D.; Tachezy, J.; Pilon, M.; Lukes, J.
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277
383-393
2010
Trypanosoma brucei (Q386Y7), Trypanosoma brucei
brenda
Zhang, W.; Urban, A.; Mihara, H.; Leimkuehler, S.; Kurihara, T.; Esaki, N.
IscS functions as a primary sulfur-donating enzyme by interacting specifically with MoeB and MoaD in the biosynthesis of molybdopterin in Escherichia coli
J. Biol. Chem.
285
2302-2308
2010
Escherichia coli
brenda
Adinolfi, S.; Iannuzzi, C.; Prischi, F.; Pastore, C.; Iametti, S.; Martin, S.R.; Bonomi, F.; Pastore, A.
Bacterial frataxin CyaY is the gatekeeper of iron-sulfur cluster formation catalyzed by IscS
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16
390-396
2009
Escherichia coli
brenda
WU, A.; ZHANG, Y.; ZHENG, C.; DAI, Y.; LIU, Y.; ZENG, J.; GU, G.; LIU, J.
Purification and enzymatic characteristics of cysteine desulfurase, IscS, in Acidithiobacillus ferrooxidans ATCC 23270
Trans. Nonferrous Met. Soc. China
18
1450-1457
2008
Acidithiobacillus ferrooxidans
-
brenda
Hidese, R.; Mihara, H.; Esaki, N.
Bacterial cysteine desulfurases: versatile key players in biosynthetic pathways of sulfur-containing biofactors
Appl. Microbiol. Biotechnol.
91
47-61
2011
Azotobacter vinelandii, Bacillus subtilis, Escherichia coli, Helicobacter pylori, Saccharomyces cerevisiae
brenda
Pandey, A.; Golla, R.; Yoon, H.; Dancis, A.; Pain, D.
Persulfide formation on mitochondrial cysteine desulfurase: enzyme activation by a eukaryote-specific interacting protein and Fe-S cluster synthesis
Biochem. J.
448
171-187
2012
Saccharomyces cerevisiae
brenda
Selbach, B.; Earles, E.; Dos Santos, P.C.
Kinetic analysis of the bisubstrate cysteine desulfurase SufS from Bacillus subtilis
Biochemistry
49
8794-8802
2010
Bacillus subtilis, Bacillus subtilis PS832
brenda
Yamanaka, Y.; Zeppieri, L.; Nicolet, Y.; Marinoni, E.N.; de Oliveira, J.S.; Odaka, M.; Dean, D.R.; Fontecilla-Camps, J.C.
Crystal structure and functional studies of an unusual L-cysteine desulfurase from Archaeoglobus fulgidus
Dalton Trans.
42
3092-3099
2013
Archaeoglobus fulgidus, Archaeoglobus fulgidus (O29689)
brenda
Albrecht, A.G.; Peuckert, F.; Landmann, H.; Miethke, M.; Seubert, A.; Marahiel, M.A.
Mechanistic characterization of sulfur transfer from cysteine desulfurase SufS to the iron-sulfur scaffold SufU in Bacillus subtilis
FEBS Lett.
585
465-470
2011
Bacillus subtilis
brenda
Kim, J.H.; Frederick, R.O.; Reinen, N.M.; Troupis, A.T.; Markley, J.L.
[2Fe-2S]-Ferredoxin binds directly to cysteine desulfurase and supplies an electron for iron-sulfur cluster assembly but is displaced by the scaffold protein or bacterial frataxin
J. Am. Chem. Soc.
135
8117-8120
2013
Escherichia coli
brenda
Turowski, V.R.; Busi, M.V.; Gomez-Casati, D.F.
Structural and functional studies of the mitochondrial cysteine desulfurase from Arabidopsis thaliana
Mol. Plant
5
1001-1010
2012
Arabidopsis thaliana, Arabidopsis thaliana (O49543), Arabidopsis thaliana (Q93WX6)
brenda
Chen, F.; Zhang, Z.; Lin, K.; Qian, T.; Zhang, Y.; You, D.; He, X.; Wang, Z.; Liang, J.; Deng, Z.; Wu, G.
Crystal structure of the cysteine desulfurase DndA from Streptomyces lividans which is involved in DNA phosphorothioation
PLoS ONE
7
e36635
2012
Streptomyces lividans (A7TUX7), Streptomyces lividans
brenda
Marelja, Z.; Mullick Chowdhury, M.; Dosche, C.; Hille, C.; Baumann, O.; Loehmannsroeben, H.G.; Leimkuehler, S.
The L-cysteine desulfurase NFS1 is localized in the cytosol where it provides the sulfur for molybdenum cofactor biosynthesis in humans
PLoS ONE
8
e60869
2013
Homo sapiens
brenda
Song, J.Y.; Marszalek, J.; Craig, E.A.
Cysteine desulfurase Nfs1 and Pim1 protease control levels of Isu, the Fe-S cluster biogenesis scaffold
Proc. Natl. Acad. Sci. USA
109
10370-10375
2012
Saccharomyces cerevisiae
brenda
Kim, J.H.; Tonelli, M.; Markley, J.L.
Disordered form of the scaffold protein IscU is the substrate for iron-sulfur cluster assembly on cysteine desulfurase
Proc. Natl. Acad. Sci. USA
109
454-459
2012
Escherichia coli
brenda
Zafrilla, B.; Martinez-Espinosa, R.M.; Esclapez, J.; Perez-Pomares, F.; Bonete, M.J.
SufS protein from Haloferax volcanii involved in Fe-S cluster assembly in haloarchaea
Biochim. Biophys. Acta
1804
1476-1482
2010
Haloferax volcanii (D4GYV5), Haloferax volcanii, Haloferax volcanii DSM 3757 (D4GYV5)
brenda
Hidese, R.; Inoue, T.; Imanaka, T.; Fujiwara, S.
Cysteine desulphurase plays an important role in environmental adaptation of the hyperthermophilic archaeon Thermococcus kodakarensis
Mol. Microbiol.
93
331-345
2014
Thermococcus kodakarensis
brenda
Roret, T.; Pegeot, H.; Couturier, J.; Mulliert, G.; Rouhier, N.; Didierjean, C.
X-ray structures of Nfs2, the plastidial cysteine desulfurase from Arabidopsis thaliana
Acta Crystallogr. Sect. F
70
1180-1185
2014
Arabidopsis thaliana, Arabidopsis thaliana (Q93WX6)
brenda
Terali, K.; Beavil, R.L.; Pickersgill, R.W.; van der Giezen, M.
The effect of the adaptor protein Isd11 on the quaternary structure of the eukaryotic cysteine desulphurase Nfs1
Biochem. Biophys. Res. Commun.
440
235-240
2013
Saccharomyces cerevisiae
brenda
Rybniker, J.; Pojer, F.; Marienhagen, J.; Kolly, G.S.; Chen, J.M.; van Gumpel, E.; Hartmann, P.; Cole, S.T.
The cysteine desulfurase IscS of Mycobacterium tuberculosis is involved in iron-sulfur cluster biogenesis and oxidative stress defence
Biochem. J.
459
467-478
2014
Mycobacterium tuberculosis, Mycobacterium tuberculosis Rv3025c
brenda
Dai, Y.; Kim, D.; Dong, G.; Busenlehner, L.S.; Frantom, P.A.; Outten, F.W.
SufE D74R substitution alters active site loop dynamics to further enhance SufE interaction with the SufS cysteine desulfurase
Biochemistry
54
4824-4833
2015
Escherichia coli
brenda
Kovarova, J.; Horakova, E.; Changmai, P.; Vancova, M.; Luke?, J.
Mitochondrial and nucleolar localization of cysteine desulfurase Nfs and the scaffold protein Isu in Trypanosoma brucei
Eukaryot. Cell
13
353-362
2014
Trypanosoma brucei
brenda
Kim, S.; Park, S.
Structural changes during cysteine desulfurase CsdA and sulfur acceptor CsdE interactions provide insight into the trans-persulfuration
J. Biol. Chem.
288
27172-27180
2013
Escherichia coli, Escherichia coli (Q46925)
brenda
Singh, H.; Dai, Y.; Outten, F.W.; Busenlehner, L.S.
Escherichia coli SufE sulfur transfer protein modulates the SufS cysteine desulfurase through allosteric conformational dynamics
J. Biol. Chem.
288
36189-36200
2013
Escherichia coli
brenda
Pandey, A.; Gordon, D.M.; Pain, J.; Stemmler, T.L.; Dancis, A.; Pain, D.
Frataxin directly stimulates mitochondrial cysteine desulfurase by exposing substrate-binding sites, and a mutant Fe-S cluster scaffold protein with frataxin-bypassing ability acts similarly
J. Biol. Chem.
288
36773-36786
2013
Saccharomyces cerevisiae
brenda
Bhubhanil, S.; Niamyim, P.; Sukchawalit, R.; Mongkolsuk, S.
Cysteine desulphurase-encoding gene sufS2 is required for the repressor function of RirA and oxidative resistance in Agrobacterium tumefaciens
Microbiology
160
79-90
2014
Agrobacterium tumefaciens
brenda
Grosshennig, S.; Ischebeck, T.; Gibhardt, J.; Busse, J.; Feussner, I.; Stuelke, J.
Hydrogen sulfide is a novel potential virulence factor of Mycoplasma pneumoniae: characterization of the unusual cysteine desulfurase/desulfhydrase HapE
Mol. Microbiol.
100
42-54
2016
Mycoplasma pneumoniae
brenda
Blauenburg, B.; Mielcarek, A.; Altegoer, F.; Fage, C.D.; Linne, U.; Bange, G.; Marahiel, M.A.
Crystal structure of Bacillus subtilis cysteine desulfurase SufS and its dynamic interaction with frataxin and scaffold protein SufU
PLoS ONE
11
e0158749
2016
Bacillus subtilis, Bacillus subtilis (O32164)
brenda
Liu, Y.; Lei, X.Y.; Chen, L.F.; Bian, Y.B.; Yang, H.; Ibrahim, S.A.; Huang, W.
A novel cysteine desulfurase influencing organosulfur compounds in Lentinula edodes
Sci. Rep.
5
10047
2015
Lentinula edodes
brenda
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