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Enzyme Nomenclature
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
- frataxin
- persulfide
- pyridoxal
- sufe
- friedreich
-
nifs-like
-
plp-dependent
- moco
-
desulfuration
- nifu
- 2-thiouridine
-
thionucleosides
-
cluster-containing
-
sulfane
-
35scysteine
-
molybdoenzymes
The enzyme appears in viruses and cellular organisms
Reaction Schemes
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
CD630_12790
CSD
CsdA
CsdB
cysteine desulfurase
cysteine desulphurase
cysteine:SufU sulfurtransferase
cysteinedesulfurylase
-
-
-
-
DndA
IcsS
IscS
IscS2
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
mechanism
-
L-cysteine + acceptor = L-alanine + S-sulfanyl-acceptor
mechanism
-
L-cysteine + acceptor = L-alanine + S-sulfanyl-acceptor
overall reaction
-
-
-
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 + 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, 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 + 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
L-alanine + H2S
-
-
or formation of elemental sulfur, depending of presence of a reducing agent in the reaction mixture
-
?
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
-
overall reaction
-
-
?
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 + 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
-
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
?
-
-
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
?
-
-
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
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
-
-
-
-
?
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
?
-
functions as scaffold for the assembly of [Fe-S] prior to their incorporation into apoproteins
-
-
?
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
?
-
-
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
?
-
-
SufA is able to bind sulfur atoms provided by the SufS-SufE complex
-
-
?
additional information
?
-
-
involved in biosynthesis of thionucleosides
-
-
?
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
?
-
-
involved in thiamine biosynthesis, molybdopterin biosynthesis and tRNA modification
-
-
?
additional information
?
-
-
[2Fe-2S]-ferredoxin interacts directly with the enzyme
-
-
?
additional information
?
-
-
involved in biosynthesis of thionucleosides
-
-
?
additional information
?
-
-
involved in biosynthesis of 2-thiouridine
-
-
?
additional information
?
-
involved in biosynthesis of 2-thiouridine
-
-
?
additional information
?
-
-
facilitates the formation of the iron-sulfur cluster of ferredoxin in vitro
-
-
?
additional information
?
-
-
enzyme contributes to the biotin synthase reaction, probably by supplying sulfur to the BioB protein
-
-
?
additional information
?
-
-
acts as sulfurtransferase in biosynthesis of 4-thiouridine in tRNA
-
-
?
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
?
-
-
enzyme is involved in selenoprotein biosynthesis
-
-
?
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
?
-
-
acts as sulfurtransferase in biosynthesis of 4-thiouridine in tRNA
-
-
?
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
?
-
-
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
?
-
-
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
?
-
-
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
?
-
-
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
?
-
-
involved in the production of sulfur for the mormation of iron-sulfur clusters
-
-
?
additional information
?
-
-
cysteine desulfurase is required for the proper post-translational modification of the lipoamide-containing mitochondrial subproteome in yeast
-
-
?
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
?
-
-
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
?
-
-
involved in biosynthesis of thionucleosides
-
-
?
additional information
?
-
-
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
-
the cofactor is covalently attached to the side chain amino group of Lys201 in a deep surface pocket via the formation of an internal aldimine Schiff base
pyridoxal 5'-phosphate
adding pyridoxal 5'-phosphate to IscS produces an enzyme that displays in vitro L-cysteine desulfurase activity
pyridoxal 5'-phosphate
-
recombinant protein possesses PLP-binding activity, catalytic activity requires pyridoxal 5'-phosphate
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
D-cycloserine
-
inhibitor of PLP-dependent enzymes, inhibits CPSIT_0959 protein catalytic 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-iodoacetyl-N'-(5-sulfo-1-naphthyl)ethylenediamine
-
up to 90% inhibition at 5 mM
NaBH4
-
inhibitor of PLP-dependent enzymes, inhibits CPSIT_0959 protein catalytic activity
N-ethylmaleimide
-
preincubation dramatically inhibits enzyme activity
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
Anabaena sulfur acceptor E
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.
-
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.
Starvation
Discovery and characterization of a novel family of prokaryotic nanocompartments involved in sulfur metabolism.
Starvation
Escherichia coli SspA is a transcription activator for bacteriophage P1 late genes.
Starvation
Evidence for Sigma Factor Competition in the Regulation of Alginate Production by Pseudomonas aeruginosa.
Starvation
Identification and Characterization of a Bacterial Homolog of Chloride Intracellular Channel (CLIC) Protein.
Starvation
Investigation of antibacterial mechanism and identification of bacterial protein targets mediated by antibacterial medicinal plant extracts.
Starvation
Null mutation in sspA of Cronobacter sakazakii influences its tolerance to environmental stress.
Starvation
Regulation of nucleoside diphosphate kinase and an alternative kinase in Escherichia coli: role of the sspA and rnk genes in nucleoside triphosphate formation.
Starvation
SspA is required for acid resistance in stationary phase by downregulation of H-NS in Escherichia coli.
Starvation
SspA positively controls exopolysaccharides production and biofilm formation by up-regulating the algU expression in Pseudoalteromonas sp. R3.
Starvation
SspA up-regulates gene expression of the LEE pathogenicity island by decreasing H-NS levels in enterohemorrhagic Escherichia coli.
Starvation
Stringent starvation protein A and LuxI/LuxR-type quorum sensing system constitute a mutual positive regulation loop in Pseudoalteromonas.
Starvation
Stringent Starvation Protein Regulates Prodiginine Biosynthesis via Affecting Siderophore Production in Pseudoalteromonas sp. Strain R3.
Starvation
Structural and Biochemical Characterization of the Francisella tularensis Pathogenicity Regulator, Macrophage Locus Protein A (MglA).
Starvation
Structural basis for the function of stringent starvation protein a as a transcription factor.
Starvation
Transposon Insertion Sequencing Elucidates Novel Gene Involvement in Susceptibility and Resistance to Phages T4 and T7 in Escherichia coli O157.
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
-
0.095
L-cysteine
-
mutant R92A, pH 8.0, temperature not specified in the publication
0.187
L-cysteine
presence of Anabaena sulfur acceptor E, pH 7.4, temperature not specified in the publication
0.152
L-cysteine
absence of Anabaena sulfur acceptor E, 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
0.095
L-cysteine
mutant R92A, pH 8.0, temperature not specified in the publication
0.095
L-cysteine
mutant E96A, pH 8.0, temperature not specified in the publication
0.086
L-cysteine
-
in 50 mM MOPS (pH 7.4), temperature not specified in the publication
0.081
L-cysteine
mutant E250A, pH 8.0, temperature not specified in the publication
0.075
L-cysteine
mutant H55A, pH 8.0, temperature not specified in the publication
0.05
L-cysteine
wild-type, pH 8.0, temperature not specified in the publication
0.043
L-cysteine
-
25°C, pH 7.4, presence of chloroplast protein CpSufE
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
-
1.427
L-cysteine
presence of Anabaena sulfur acceptor E, 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
0.65
L-cysteine
mutant H55A, pH 8.0, temperature not specified in the publication
0.23
L-cysteine
mutant E96A, pH 8.0, temperature not specified in the publication
0.202
L-cysteine
wild-type, pH 8.0, temperature not specified in the publication
0.167
L-cysteine
mutant E250A, pH 8.0, temperature not specified in the publication
0.136
L-cysteine
absence of Anabaena sulfur acceptor E, pH 7.4, temperature not specified in the publication
0.123
L-cysteine
mutant R92A, pH 8.0, 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
-
1.2
L-cysteine
mutant E250A, pH 8.0, temperature not specified in the publication
1.3
L-cysteine
mutant R92A, pH 8.0, temperature not specified in the publication
2.3
L-cysteine
mutant E96A, pH 8.0, temperature not specified in the publication
4
L-cysteine
wild-type, pH 8.0, temperature not specified in the publication
8.3
L-cysteine
mutant H55A, pH 8.0, 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
38.6
45.7
-
wild type enzyme, pH and temperature not specified in the publication
56.5
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
-
645626, 645630, 645632, 645633, 645634, 645635, 645637, 661771, 662209, 674798, 692336, 704679, 705872, 724057, 725215, 726388, 737712
-
-
brenda
strain DH5a and mutant desulfurase deficient strains csdA::Kn, csdB::Kn, ascS::Kn
-
-
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
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 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
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
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
-
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 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
-
the enzyme is a potential virulence factor of Mycoplasma pneumoniae being responsible for haemolysis
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
-
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
-
SspA can form a complex with SspD, an ATP diphosphatase
physiological function
-
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
-
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
-
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
-
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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Show AA Sequence and Transmembrane Helices (88273 entries)
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PDB
SCOP
CATH
UNIPROT
ORGANISM
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
42000
45000
46000
47000
88000
45000
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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
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
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
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
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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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
C361A
E96A
about 6fold decrease in kcat/Km value, mutant displays altered dimer geometries
S326A
-
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
-
about 6fold decrease in kcat/Km value, mutant displays altered dimer geometries
H123A
H55A
L333A
-
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
C364A
C358A
-
CSD mutant, activity towards L-cysteine is almost completely abolished, activity toward L-selenocysteine is much less affected
C328A
-
IscS mutant, activity towards L-cysteine is almost completely abolished, activity toward L-selenocysteine is much less affected
S326A
-
mutant defective in Fe-S biosynthesis in vivo but functional in persulfide formation and transfer in vitro
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L333A
-
mutant defective in Fe-S biosynthesis in vivo but functional in persulfide formation and transfer in vitro
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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
C327S
sited-directed mutagenesis, no cysteine desulfurase activity, no ability to reactivate the apo-Fe DndC
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
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H123A
mutation abolishes the ability of SufS to generate persulfide from L-cysteine. His123 acts to protonate the Ala-enamine intermediate
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
-
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
-
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
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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
-
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
additional information
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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
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
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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
expressed in Escherichia coli BL21(DE3) cells
expression in Escherichia coli
expression in Escherichia coli BL21(DE3) pLysE, expression vector pET15b