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Information on EC 2.8.1.7 - cysteine desulfurase and Organism(s) Escherichia coli and UniProt Accession P77444
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2.8.1.7 cysteine desulfuraseIUBMB Comments
A pyridoxal-phosphate protein. The sulfur from free L-cysteine is first transferred to a cysteine residue in the active site, and then passed on to various other acceptors. The enzyme is involved in the biosynthesis of iron-sulfur clusters, thio-nucleosides in tRNA, thiamine, biotin, lipoate and pyranopterin (molybdopterin) . In Azotobacter vinelandii, this sulfur provides the inorganic sulfide required for nitrogenous metallocluster formation .
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Word Map
- 2.8.1.7
-
iron-sulfur
- fe-s
- iscu
- persulfide
- frataxin
- pyridoxal
- sufe
-
nifs-like
- friedreich
- moco
-
plp-dependent
- 2-thiouridine
-
desulfuration
-
sulfane
- nifu
-
35scysteine
-
molybdoenzymes
-
thionucleosides
-
cluster-containing
The taxonomic range for the selected organisms is: Escherichia coli
The enzyme appears in selected viruses and cellular organisms
The enzyme appears in selected viruses and cellular organisms
Reaction Schemes
hide(Overall reactions are displayed. Show all >>)
Synonyms
cysteine desulfurase, nfs1p, cpnifs, l-cysteine desulfurase, cysteine desulphurase, stringent starvation protein a, sufs2, lecsl, slr0077, cpsit_0959, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
CSD
-
-
-
-
CsdA
CsdB
cysteinedesulfurylase
-
-
-
-
IscS
Nfs1
-
-
-
-
NIFS
-
-
-
-
SufS
CsdB
-
-
-
-
IscS
-
-
-
-
SufS
-
-
-
-
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
L-cysteine + acceptor = L-alanine + S-sulfanyl-acceptor
mechanism
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
sulfur atom transfer
sulfur atom transfer
-
-
-
-
PATHWAY SOURCE
PATHWAYS
KEGG
-
-, -, -, -, -, -, -
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].
CAS REGISTRY NUMBER
COMMENTARY
149371-08-4
-
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 + acceptor
L-alanine + S-sulfanyl-acceptor
overall reaction
-
-
?
L-cysteine + ?
?
-
in the presence of cysteine, IscSs ability to bind iron improves significantly
-
-
?
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 + 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
-
-
-
-
?
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-selenocysteine
L-alanine + selenium
-
Cys364 residue is essential for activity toward L-cysteine but not toward L-selenocyteine
-
-
?
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
-
-
?
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 + [enzyme]-cysteine
L-alanine + [enzyme]-S-sulfanylcysteine
-
-
-
-
?
L-cysteine + [enzyme]-cysteine
L-alanine + [enzyme]-S-sulfanylcysteine
-
-
-
?
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
?
-
-
[2Fe-2S]-ferredoxin interacts directly with the enzyme
-
-
?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
pyridoxal 5'-phosphate
-
-
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
Fe2+
-
the low desulfurase activity is caused by the modification of IscS rather than by the formation of FeS in the solution
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
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
pyruvate
-
increases activity of CSD towards L-selenocysteine, but not towards L-cysteine
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
-
additional information
-
SufE participates in allosteric regulation of the enzyme activity
-
SufE
-
binding of SufE, a member of the SUF protein system, to SufS stimulates the cysteine desulfurase activity of SufS by 50fold
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.05
L-cysteine
wild-type, pH 8.0, temperature not specified in the publication
0.075
L-cysteine
mutant H55A, pH 8.0, temperature not specified in the publication
0.081
L-cysteine
mutant E250A, pH 8.0, temperature not specified in the publication
0.095
L-cysteine
mutant E96A, pH 8.0, temperature not specified in the publication
0.095
L-cysteine
mutant R92A, pH 8.0, temperature not specified in the publication
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.123
L-cysteine
mutant R92A, pH 8.0, temperature not specified in the publication
0.167
L-cysteine
mutant E250A, pH 8.0, temperature not specified in the publication
0.202
L-cysteine
wild-type, pH 8.0, temperature not specified in the publication
0.23
L-cysteine
mutant E96A, pH 8.0, temperature not specified in the publication
0.65
L-cysteine
mutant H55A, pH 8.0, temperature not specified in the publication
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
physiological function
physiological function
-
IscS is the primary physiological sulfur-donating enzyme for the generation of the thiocarboxylate of molybdopterin synthase in molybdopterin biosynthesis
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
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
homodimer
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
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
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
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
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)
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
C364A
mutation abolishes the ability of SufS to generate persulfide from L-cysteine. Cys364 is essential for positioning the Cys-aldimine for Calpha deprotonation
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
mutation abolishes the ability of SufS to generate persulfide from L-cysteine. His123 acts to protonate the Ala-enamine intermediate
R92A
about 3fold decrease in kcat/Km value, dimer geometry is identical to that of wild-type
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
additional information
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
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
DEAE-Toyopearl column chromatography and phenyl-Toyopearl column chromatography
-
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli BL21(DE3) cells
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
-
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Kiyasu, T.; Asakura, A.; Nagahashi, Y.; Hoshino, T.
Contribution of cysteine desulfurase (NifS protein) to the biotin synthase reaction of Escherichia coli
J. Bacteriol.
182
2879-2885
2000
Escherichia coli, Klebsiella pneumoniae, Klebsiella pneumoniae M5a1
Mihara, H.; Esaki, N.
Bacterial cysteine desulfurases: their function and mechanisms
Appl. Microbiol. Biotechnol.
60
12-23
2002
Azotobacter vinelandii, Synechocystis sp., Saccharomyces cerevisiae, Escherichia coli, Haemophilus influenzae, Homo sapiens, Mus musculus, Pseudomonas aeruginosa, Synechocystis sp. PCC6714
Cupp-Vickery, J.R.; Urbina, H.; Vickery, L.E.
Crystal structure of IscS, a cysteine desulfurase from Escherichia coli
J. Mol. Biol.
330
1049-1059
2003
Escherichia coli
Lima, C.D.
Analysis of the E. coli NifS CsdB protein at 2.0 A reveals the structural basis for perselenide and persulfide intermediate formation
J. Mol. Biol.
315
1199-1208
2002
Escherichia coli (P77444)
Kambampati, R.; Lauhon, C.T.
MnmA and IscS are required for in vitro 2-thiouridine biosynthesis in Escherichia coli
Biochemistry
42
1109-1117
2003
Escherichia coli (P25745), Escherichia coli
Lauhon, C.T.
Requirement for IscS in biosynthesis of all thionucleosides in Escherichia coli
J. Bacteriol.
184
6820-6829
2002
Escherichia coli
Lauhon, C.T.; Kambampati, R.
The iscS gene in Escherichia coli is required for the biosynthesis of 4-thiouridine, thiamin, and NAD
J. Biol. Chem.
275
20096-20103
2000
Escherichia coli, Escherichia coli MC1061
Loiseau, L.; Ollagnier-de-Choudens, S.; Nachin, L.; Fontecave, M.; Barras, F.
Biogenesis of Fe-S cluster by the bacterial Suf system: SufS and SufE form a new type of cysteine desulfurase
J. Biol. Chem.
278
38352-38359
2003
Escherichia coli, Dickeya chrysanthemi, Escherichia coli TG1
Mihara, H.; Fujii, T.; Kato, S.; Kurihara, T.; Hata, Y.; Esaki, N.
Structure of external aldimine of Escherichia coli CsdB, an IscS/NifS homolog: implications for its specificity toward selenocysteine
J. Biochem.
131
679-685
2002
Escherichia coli
Mihara, H.; Kurihara, T.; Yoshimura, T.; Esaki, N.
Kinetic and mutational studies of three NifS homologs from Escherichia coli: mechanistic difference between L-cysteine desulfurase and L-selenocysteine lyase reactions
J. Biochem.
127
559-567
2000
Escherichia coli
Nilsson, K.; Lundgren, H.K.; Hagervall, T.G.; Bjork, G.R.
The cysteine desulfurase IscS is required for synthesis of all five thiolated nucleosides present in tRNA from Salmonella enterica serovar typhimurium
J. Bacteriol.
184
6830-6835
2002
Escherichia coli, Salmonella enterica
Outten, F.W.; Wood, M.J.; Munoz, F.M.; Storz, G.
The SufE protein and the SufBCD complex enhance SufS cysteine desulfurase activity as part of a sulfur transfer pathway for Fe-S cluster assembly in Escherichia coli
J. Biol. Chem.
278
45713-45719
2003
Escherichia coli
Yang, W.; Rogers, P.A.; Ding, H.
Repair of nitric oxide-modified ferredoxin [2Fe-2S] cluster by cysteine desulfurase (IscS)
J. Biol. Chem.
277
12868-12873
2002
Escherichia coli
Schwartz, C.J.; Djaman, O.; Imlay, J.A.; Kiley, P.J.
The cysteine desulfurase, IscS, has a major role in in vivo Fe-S cluster formation in Escherichia coli
Proc. Natl. Acad. Sci. USA
97
9009-9014
2000
Escherichia coli
Kurihara, T.; Mihara, H.; Kato, S.; Yoshimura, T.; Esaki, N.
Assembly of iron-sulfur clusters mediated by cysteine desulfurases, IscS, CsdB and CSD, from Escherichia coli
Biochim. Biophys. Acta
1647
303-309
2003
Escherichia coli
Forlani, F.; Cereda, A.; Freuer, A.; Nimtz, M.; Leimkhler, S.; Pagani, S.
The cysteine-desulfurase IscS promotes the production of the rhodanese RhdA in the persulfurated form
FEBS Lett.
579
6786-6790
2005
Escherichia coli
Lauhon, C.T.; Skovran, E.; Urbina, H.D.; Downs, D.M.; Vickery, L.E.
Substitutions in an active site loop of Escherichia coli IscS result in specific defects in Fe-S cluster and thionucleoside biosynthesis in vivo
J. Biol. Chem.
279
19551-19558
2004
Escherichia coli, Escherichia coli MC1061
Rojas, D.M.; Vasquez, C.C.
Sensitivity to potassium tellurite of Escherichia coli cells deficient in CSD, CsdB and IscS cysteine desulfurases
Res. Microbiol.
156
465-471
2005
Escherichia coli, Escherichia coli DH5-alpha
Layer, G.; Gaddam, S.A.; Ayala-Castro, C.N.; Ollagnier-de Choudens, S.; Lascoux, D.; Fontecave, M.; Outten, F.W.
SufE transfers sulfur from SufS to SufB for iron-sulfur cluster assembly
J. Biol. Chem.
282
13342-13350
2007
Escherichia coli
Mihara, H.; Hidese, R.; Yamane, M.; Kurihara, T.; Esaki, N.
The iscS gene deficiency affects the expression of pyrimidine metabolism genes
Biochem. Biophys. Res. Commun.
372
407-411
2008
Escherichia coli
Wu, G.; Li, P.; Wu, X.
Regulation of Escherichia coli IscS desulfurase activity by ferrous iron and cysteine
Biochem. Biophys. Res. Commun.
374
399-404
2008
Escherichia coli
Sendra, M.; Ollagnier de Choudens, S.; Lascoux, D.; Sanakis, Y.; Fontecave, M.
The SUF iron-sulfur cluster biosynthetic machinery: sulfur transfer from the SUFS-SUFE complex to SUFA
FEBS Lett.
581
1362-1368
2007
Escherichia coli
Zhang, W.; Urban, A.; Mihara, H.; Leimkuehler, S.; Kurihara, T.; Esaki, N.
IscS functions as a primary sulfur-donating enzyme by interacting specifically with MoeB and MoaD in the biosynthesis of molybdopterin in Escherichia coli
J. Biol. Chem.
285
2302-2308
2010
Escherichia coli
Adinolfi, S.; Iannuzzi, C.; Prischi, F.; Pastore, C.; Iametti, S.; Martin, S.R.; Bonomi, F.; Pastore, A.
Bacterial frataxin CyaY is the gatekeeper of iron-sulfur cluster formation catalyzed by IscS
Nat. Struct. Mol. Biol.
16
390-396
2009
Escherichia coli
Hidese, R.; Mihara, H.; Esaki, N.
Bacterial cysteine desulfurases: versatile key players in biosynthetic pathways of sulfur-containing biofactors
Appl. Microbiol. Biotechnol.
91
47-61
2011
Azotobacter vinelandii, Bacillus subtilis, Saccharomyces cerevisiae, Escherichia coli, Helicobacter pylori
Kim, J.H.; Frederick, R.O.; Reinen, N.M.; Troupis, A.T.; Markley, J.L.
[2Fe-2S]-Ferredoxin binds directly to cysteine desulfurase and supplies an electron for iron-sulfur cluster assembly but is displaced by the scaffold protein or bacterial frataxin
J. Am. Chem. Soc.
135
8117-8120
2013
Escherichia coli
Kim, J.H.; Tonelli, M.; Markley, J.L.
Disordered form of the scaffold protein IscU is the substrate for iron-sulfur cluster assembly on cysteine desulfurase
Proc. Natl. Acad. Sci. USA
109
454-459
2012
Escherichia coli
Dai, Y.; Kim, D.; Dong, G.; Busenlehner, L.S.; Frantom, P.A.; Outten, F.W.
SufE D74R substitution alters active site loop dynamics to further enhance SufE interaction with the SufS cysteine desulfurase
Biochemistry
54
4824-4833
2015
Escherichia coli
Kim, S.; Park, S.
Structural changes during cysteine desulfurase CsdA and sulfur acceptor CsdE interactions provide insight into the trans-persulfuration
J. Biol. Chem.
288
27172-27180
2013
Escherichia coli (Q46925), Escherichia coli
Singh, H.; Dai, Y.; Outten, F.W.; Busenlehner, L.S.
Escherichia coli SufE sulfur transfer protein modulates the SufS cysteine desulfurase through allosteric conformational dynamics
J. Biol. Chem.
288
36189-36200
2013
Escherichia coli
Dunkle, J.; Bruno, M.; Frantom, P.
Structural evidence for a latch mechanism regulating access to the active site of SufS-family cysteine desulfurases
Acta Crystallogr. Sect. D
76
291-301
2020
Escherichia coli (P77444), Escherichia coli
Dunkle, J.A.; Bruno, M.R.; Outten, F.W.; Frantom, P.A.
Structural evidence for dimer-interface-driven regulation of the type II cysteine desulfurase, SufS
Biochemistry
58
687-696
2019
Escherichia coli (P77444), Escherichia coli
Wang, J.; Guo, X.; Li, H.; Qi, H.; Qian, J.; Yan, S.; Shi, J.; Niu, W.
Hydrogen sulfide from cysteine desulfurase, not 3-mercaptopyruvate sulfurtransferase, contributes to sustaining cell growth and bioenergetics in E. coli under anaerobic conditions
Front. Microbiol.
10
2357
2019
Escherichia coli
Blahut, M.; Wise, C.E.; Bruno, M.R.; Dong, G.; Makris, T.M.; Frantom, P.A.; Dunkle, J.A.; Outten, F.W.
Direct observation of intermediates in the SufS cysteine desulfurase reaction reveals functional roles of conserved active-site residues
J. Biol. Chem.
294
12444-12458
2019
Escherichia coli (P77444), Escherichia coli
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