HOME
login
history
all enzymes
BRENDA home
History
Enzyme Nomenclature
Information on EC 2.8.1.7 - cysteine desulfurase
for references in articles please use BRENDA:EC2.8.1.7
Word Map on EC 2.8.1.7
- 2.8.1.7
-
iron-sulfur
- persulfide
-
frataxin
- pyridoxal
-
nifs-like
- friedreich
-
plp-dependent
-
desulfuration
-
thionucleosides
-
sulfane
- 2-thiouridine
- moco
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
Specify your search results
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
topPlease wait a moment until the data is sorted. This message will disappear when the data is sorted.
EC NUMBER 
COMMENTARY 
2.8.1.7
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
RECOMMENDED NAME
GeneOntology No.
cysteine desulfurase
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
sulfur atom transfer
sulfur atom transfer
-
-
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
SYSTEMATIC NAME
IUBMB Comments
L-cysteine:acceptor sulfurtransferase
A pyridoxal-phosphate protein. The sulfur from free L-cysteine is first transferred to a cysteine residue in the active site, and then passed on to various other acceptors. The enzyme is involved in the biosynthesis of iron-sulfur clusters, thio-nucleosides in tRNA, thiamine, biotin, lipoate and pyranopterin (molybdopterin) [2]. In Azotobacter vinelandii, this sulfur provides the inorganic sulfide required for nitrogenous metallocluster formation [1].
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
CAS REGISTRY NUMBER
COMMENTARY
149371-08-4
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
strain DH5a and mutant desulfurase deficient strains csdA::Kn, csdB::Kn, ascS::Kn
-
-
YPH499as WT, GAL10-ISD11 as Isd11-depleted strain
-
-
; strain ATCC 23270, expression in Escherichia coli BL21 (DE3)
-
-
-
645614, 645615, 645616, 645626, 645630, 645632, 645633, 645634, 645635, 645637, 661771, 662209, 674798, 692336, 704679, 705872, 724057, 725215, 726388, 737712, 738600
-
-
strain DH5a and mutant desulfurase deficient strains csdA::Kn, csdB::Kn, ascS::Kn
-
-
expression in Escherichia coli BL21(DE3) pLysE, expression vector pET15b
TrEMBL
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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, IscSs 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 ironsulfur 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
Q386Y7
-
-
-
?
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 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 SUBSTRATES
NATURAL PRODUCTS
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
-
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
INHIBITORS
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
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
0.1
Q386Y7
knockdown of Nfs-like proteins, activity measured in mitochondrial fractions
0.2
Q386Y7
knockdown of selenocysteine lyase, activity measured in mitochondrial fractions
0.5
Q386Y7
knockdown of selenocysteine lyase, activity measured in cytosolic fractions
1
Q386Y7
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
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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
-
mitochondrial Nfs1p is required for the biogenesis of both mitochondrial and extramitochondrial Fe/S proteins
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
PDB
SCOP
CATH
ORGANISM
UNIPROT
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)
Legionella pneumophila subsp. pneumophila (strain Philadelphia 1 / ATCC 33152 / DSM 7513)
Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Synechocystis sp. (strain PCC 6803 / Kazusa)
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
SUBUNITS
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
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
proteolytic modification
proteolytic modification
-
after lysis of mitochondria with detergents
proteolytic modification
-
after lysis of mitochondria with detergents
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
4°C, purified protein can be stored one month without loss of activity
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
ENGINEERING
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
Show AA Sequence (30534 entries)
Longer loading times are possible. Please use the Sequence Search for a specific query.
Longer loading times are possible. Please use the Sequence Search for a specific query.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
LINKS TO OTHER DATABASES (specific for EC-Number 2.8.1.7)
html completed
Use of this online version of BRENDA is free but requires a license. See terms of use.
Information
