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L-cysteine + [enzyme]-cysteine
L-alanine + [enzyme]-S-sulfanylcysteine
-
-
?
L-cysteine + ?
?
-
in the presence of cysteine, IscSs ability to bind iron improves significantly
-
-
?
L-cysteine + acceptor
L-alanine + S-sulfanyl-acceptor
L-cysteine + c-IscU
L-alanine + c-IscU-SSH
-
-
-
-
?
L-cysteine + IscS
L-alanine + IscS-SSH
-
-
-
-
?
L-cysteine + N,N-dimethyl-4-phenylenediamine
L-alanine + N,N-dimethyl-4-phenylenediamine sulfate
-
-
-
-
?
L-cysteine + RhdA
L-alanine + RhdA-SSH
L-cysteine + SufE
L-alanine + S-sulfanyl-SufE
-
-
-
-
?
L-cysteine + SufE
L-alanine + SufE-SSH
-
-
-
?
L-cysteine + [enzyme]-cysteine
L-alanine + [enzyme]-S-sulfanylcysteine
L-cysteine + [IscU]-cysteine
L-alanine + [IscU]-S-sulfanylcysteine
-
each enzyme subunit binds an IscU molecule and transfers sulfane sulfur generated from the conversion of cysteine to alanine to the cluster ligand cysteines of IscU. The enzyme binds preferentially to and stabilizes the D state of apo-IscU
-
-
?
L-cysteine + [ThiI]-cysteine
L-alanine + [ThiI]-S-sulfanylcysteine
-
-
-
-
?
L-cysteine sulfinic acid
L-alanine + sulfite
-
-
-
-
?
L-selenocysteine
L-alanine + selenium
additional information
?
-
L-cysteine + acceptor
L-alanine + S-sulfanyl-acceptor
-
-
-
?
L-cysteine + acceptor
L-alanine + S-sulfanyl-acceptor
overall reaction
-
-
?
L-cysteine + RhdA
L-alanine + RhdA-SSH
-
-
-
-
?
L-cysteine + RhdA
L-alanine + RhdA-SSH
-
transfer of sulfur to rhodanese with formation of a covalent complex between IscS and RhdA
-
-
?
L-cysteine + [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
-
-
-
-
?
L-selenocysteine
L-alanine + selenium
-
-
-
?
L-selenocysteine
L-alanine + selenium
-
-
-
?
L-selenocysteine
L-alanine + selenium
-
Cys364 residue is essential for activity toward L-cysteine but not toward L-selenocyteine
-
-
?
additional information
?
-
involved in biosynthesis of 2-thiouridine
-
-
?
additional information
?
-
-
involved in biosynthesis of 2-thiouridine
-
-
?
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 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
-
-
?
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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
brenda
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
brenda
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
brenda
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)
brenda
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
brenda
Lauhon, C.T.
Requirement for IscS in biosynthesis of all thionucleosides in Escherichia coli
J. Bacteriol.
184
6820-6829
2002
Escherichia coli
brenda
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
brenda
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
brenda
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
brenda
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
brenda
Nilsson, K.; Lundgren, H.K.; Hagervall, T.G.; Bjork, G.R.
The cysteine desulfurase IscS is required for synthesis of all five thiolated nucleosides present in tRNA from Salmonella enterica serovar typhimurium
J. Bacteriol.
184
6830-6835
2002
Escherichia coli, Salmonella enterica
brenda
Outten, F.W.; Wood, M.J.; Munoz, F.M.; Storz, G.
The SufE protein and the SufBCD complex enhance SufS cysteine desulfurase activity as part of a sulfur transfer pathway for Fe-S cluster assembly in Escherichia coli
J. Biol. Chem.
278
45713-45719
2003
Escherichia coli
brenda
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
brenda
Schwartz, C.J.; Djaman, O.; Imlay, J.A.; Kiley, P.J.
The cysteine desulfurase, IscS, has a major role in in vivo Fe-S cluster formation in Escherichia coli
Proc. Natl. Acad. Sci. USA
97
9009-9014
2000
Escherichia coli
brenda
Kurihara, T.; Mihara, H.; Kato, S.; Yoshimura, T.; Esaki, N.
Assembly of iron-sulfur clusters mediated by cysteine desulfurases, IscS, CsdB and CSD, from Escherichia coli
Biochim. Biophys. Acta
1647
303-309
2003
Escherichia coli
brenda
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
brenda
Lauhon, C.T.; Skovran, E.; Urbina, H.D.; Downs, D.M.; Vickery, L.E.
Substitutions in an active site loop of Escherichia coli IscS result in specific defects in Fe-S cluster and thionucleoside biosynthesis in vivo
J. Biol. Chem.
279
19551-19558
2004
Escherichia coli, Escherichia coli MC1061
brenda
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
brenda
Layer, G.; Gaddam, S.A.; Ayala-Castro, C.N.; Ollagnier-de Choudens, S.; Lascoux, D.; Fontecave, M.; Outten, F.W.
SufE transfers sulfur from SufS to SufB for iron-sulfur cluster assembly
J. Biol. Chem.
282
13342-13350
2007
Escherichia coli
brenda
Mihara, H.; Hidese, R.; Yamane, M.; Kurihara, T.; Esaki, N.
The iscS gene deficiency affects the expression of pyrimidine metabolism genes
Biochem. Biophys. Res. Commun.
372
407-411
2008
Escherichia coli
brenda
Wu, G.; Li, P.; Wu, X.
Regulation of Escherichia coli IscS desulfurase activity by ferrous iron and cysteine
Biochem. Biophys. Res. Commun.
374
399-404
2008
Escherichia coli
brenda
Sendra, M.; Ollagnier de Choudens, S.; Lascoux, D.; Sanakis, Y.; Fontecave, M.
The SUF iron-sulfur cluster biosynthetic machinery: sulfur transfer from the SUFS-SUFE complex to SUFA
FEBS Lett.
581
1362-1368
2007
Escherichia coli
brenda
Zhang, W.; Urban, A.; Mihara, H.; Leimkuehler, S.; Kurihara, T.; Esaki, N.
IscS functions as a primary sulfur-donating enzyme by interacting specifically with MoeB and MoaD in the biosynthesis of molybdopterin in Escherichia coli
J. Biol. Chem.
285
2302-2308
2010
Escherichia coli
brenda
Adinolfi, S.; Iannuzzi, C.; Prischi, F.; Pastore, C.; Iametti, S.; Martin, S.R.; Bonomi, F.; Pastore, A.
Bacterial frataxin CyaY is the gatekeeper of iron-sulfur cluster formation catalyzed by IscS
Nat. Struct. Mol. Biol.
16
390-396
2009
Escherichia coli
brenda
Hidese, R.; Mihara, H.; Esaki, N.
Bacterial cysteine desulfurases: versatile key players in biosynthetic pathways of sulfur-containing biofactors
Appl. Microbiol. Biotechnol.
91
47-61
2011
Azotobacter vinelandii, Bacillus subtilis, Saccharomyces cerevisiae, Escherichia coli, Helicobacter pylori
brenda
Kim, J.H.; Frederick, R.O.; Reinen, N.M.; Troupis, A.T.; Markley, J.L.
[2Fe-2S]-Ferredoxin binds directly to cysteine desulfurase and supplies an electron for iron-sulfur cluster assembly but is displaced by the scaffold protein or bacterial frataxin
J. Am. Chem. Soc.
135
8117-8120
2013
Escherichia coli
brenda
Kim, J.H.; Tonelli, M.; Markley, J.L.
Disordered form of the scaffold protein IscU is the substrate for iron-sulfur cluster assembly on cysteine desulfurase
Proc. Natl. Acad. Sci. USA
109
454-459
2012
Escherichia coli
brenda
Dai, Y.; Kim, D.; Dong, G.; Busenlehner, L.S.; Frantom, P.A.; Outten, F.W.
SufE D74R substitution alters active site loop dynamics to further enhance SufE interaction with the SufS cysteine desulfurase
Biochemistry
54
4824-4833
2015
Escherichia coli
brenda
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
brenda
Singh, H.; Dai, Y.; Outten, F.W.; Busenlehner, L.S.
Escherichia coli SufE sulfur transfer protein modulates the SufS cysteine desulfurase through allosteric conformational dynamics
J. Biol. Chem.
288
36189-36200
2013
Escherichia coli
brenda
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
brenda
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
brenda
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
brenda
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
brenda