Information on EC 2.8.1.7 - cysteine desulfurase:
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EC NUMBERCOMMENTARY
2.8.1.7-

RECOMMENDED NAMEGeneOntology No.
cysteine desulfuraseGO:0031071

REACTIONREACTION DIAGRAMCOMMENTARYORGANISM UNIPROT ACCESSION NO.LITERATURE
L-cysteine + acceptor = L-alanine + S-sulfanyl-acceptor
show the reaction diagram		overall reaction---
L-cysteine + acceptor = L-alanine + S-sulfanyl-acceptor
show the reaction diagram		mechanismEscherichia coli-645615, 645628, 645630
L-cysteine + acceptor = L-alanine + S-sulfanyl-acceptor
show the reaction diagram		mechanismAzotobacter vinelandii-645615, 645631, 645636
L-cysteine + acceptor = L-alanine + S-sulfanyl-acceptor
show the reaction diagram		mechanismBacteria-645619
L-cysteine + acceptor = L-alanine + S-sulfanyl-acceptor
show the reaction diagram		mechanismErwinia chrysanthemi-645628
L-cysteine + acceptor = L-alanine + S-sulfanyl-acceptor
show the reaction diagram		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 XdhCRhodobacter capsulatus-672277
L-cysteine + [enzyme]-cysteine = L-alanine + [enzyme]-S-sulfanylcysteine
show the reaction diagram		(1a)---
[enzyme]-S-sulfanylcysteine + acceptor = [enzyme]-cysteine + S-sulfanyl-acceptor
show the reaction diagram		(1b)---

REACTION TYPEORGANISM UNIPROT ACCESSION NO.COMMENTARYLITERATURE
sulfur atom transfer----
sulfur atom transferEscherichia coli--661771
sulfur atom transferSaccharomyces cerevisiae-in mitochondria and cytoplasm662190, 662257

PATHWAYKEGG LinkMetaCyc Link
alanine biosynthesis III-PWY0-1021
molybdenum cofactor biosynthesis-PWY-6823
NIL-RXN-12588
thiazole biosynthesis I (E. coli)-PWY-6892
thiazole biosynthesis II (Bacillus)-PWY-6891

SYSTEMATIC NAMEIUBMB Comments
L-cysteine:acceptor sulfurtransferaseA 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].

SYNONYMSORGANISM UNIPROT ACCESSION NO.COMMENTARYLITERATURE
c-ISCSHomo sapiens--674541
CD0387Synechocystis sp.--702269
CpNifSArabidopsis thaliana--676898
CSD----
CsdB----
CysDTrypanosoma bruceiQ386Y7; 703682
cysteine desulfuraseMus musculus--671626
cysteine desulfuraseStreptomyces lividansQ460H9-672260
cysteine desulfuraseAcidithiobacillus ferrooxidans--672753
cysteine desulfuraseEscherichia coli--674798, 690737, 690744, 692336
cysteine desulfuraseArabidopsis thaliana--676898
cysteine desulfuraseTrypanosoma bruceiQ386Y7-703682
cysteinedesulfurylase----
DndAStreptomyces lividansQ460H9; 672260
IscS----
IscSEscherichia coli--661771, 662209, 690737, 690744, 704679, 705872
IscSAcidithiobacillus ferrooxidans--672753, 706851
L-cysteine desulfuraseRhodobacter capsulatus--672277
NfsTrypanosoma bruceiQ386Y7formerly IscS2703682
Nfs1----
Nfs1Saccharomyces cerevisiae--661595
Nfs1Mus musculus--671626
Nfs1pSaccharomyces cerevisiae--662190, 662257
NIFS----
NifS4Rhodobacter capsulatus--672277
Slr0077Synechocystis sp.--660879
Slr0077/SufSSynechocystis sp.Q55793-661090
Slr0387Synechocystis sp.--661091
SufS----
SufSEscherichia coli--674798, 692336

CAS REGISTRY NUMBERCOMMENTARY
149371-08-4-

ORGANISMCOMMENTARYLITERATURESEQUENCE CODESEQUENCE DB SOURCE
Acidithiobacillus ferrooxidans; strain ATCC 23270, expression in Escherichia coli BL21 (DE3)672753--Manually annotated by BRENDA team
Acidithiobacillus ferrooxidansstrain ATCC 23270706851--Manually annotated by BRENDA team
Arabidopsis thaliana-645618, 674773, 676898--Manually annotated by BRENDA team
Azotobacter vinelandii-645615, 645624, 645631, 645636--Manually annotated by BRENDA team
Bacteria-645619--Manually annotated by BRENDA team
Cryptosporidium parvum-645639Q8WQX4SwissProtManually annotated by BRENDA team
Erwinia chrysanthemi-645628--Manually annotated by BRENDA team
Escherichia coli-645614, 645615, 645616, 645626, 645630, 645632, 645633, 645634, 645635, 645637, 661771, 674798, 704679, 705872--Manually annotated by BRENDA team
Escherichia coli-645617P77444UniprotManually annotated by BRENDA team
Escherichia coli-645620P25745UniProtManually annotated by BRENDA team
Escherichia coli3 cysteine desulfurases: IscS, CsdB and CSD645638--Manually annotated by BRENDA team
Escherichia coliMC1061645627--Manually annotated by BRENDA team
Escherichia colirecombinat enzyme690744--Manually annotated by BRENDA team
Escherichia colistrain BL21(DE3)692336--Manually annotated by BRENDA team
Escherichia colistrain DH5a and mutant desulfurase deficient strains csdA::Kn, csdB::Kn, ascS::Kn663375--Manually annotated by BRENDA team
Escherichia colistrain MC1061662209--Manually annotated by BRENDA team
Escherichia coliTG1645628--Manually annotated by BRENDA team
Escherichia coliwild-type strain and iscS mutant strain690737--Manually annotated by BRENDA team
Escherichia coli DH5astrain DH5a and mutant desulfurase deficient strains csdA::Kn, csdB::Kn, ascS::Kn663375--Manually annotated by BRENDA team
Haemophilus influenzae-645615--Manually annotated by BRENDA team
Homo sapiens-645615, 645625, 675971--Manually annotated by BRENDA team
Homo sapienscytosolic isoform, overexpression in Pichia pastoris674541--Manually annotated by BRENDA team
Klebsiella pneumoniae-674877--Manually annotated by BRENDA team
Klebsiella pneumoniaeM5a1645614--Manually annotated by BRENDA team
Mus musculus-645615, 671626, 675971--Manually annotated by BRENDA team
Mus musculus-674628Q9Z1J3SwissProtManually annotated by BRENDA team
Pseudomonas aeruginosa-645615--Manually annotated by BRENDA team
Rattus norvegicusweanling male wistar662693Q99P39SwissProtManually annotated by BRENDA team
Rhodobacter capsulatus; expression in Escherichia coli BL21(DE3)672277--Manually annotated by BRENDA team
Ruminococcus flavefaciens-645640--Manually annotated by BRENDA team
Saccharomyces cerevisiae-645615, 645622, 675989--Manually annotated by BRENDA team
Saccharomyces cerevisiaeW303-1A, Gal-NFS1, Gal-ATM1, Gal-YAH1662257--Manually annotated by BRENDA team
Saccharomyces cerevisiaeW303-1B and YN101662190--Manually annotated by BRENDA team
Saccharomyces cerevisiaeYPH499as WT, GAL10-ISD11 as Isd11-depleted strain661595--Manually annotated by BRENDA team
Saccharomyces cerevisiae Isd11-depletedYPH499as WT, GAL10-ISD11 as Isd11-depleted strain661595--Manually annotated by BRENDA team
Salmonella entericaserovar typhimurium674271--Manually annotated by BRENDA team
Salmonella entericaserovar Typhimurium strain TR970645633--Manually annotated by BRENDA team
Streptomyces lividansexpression in Escherichia coli BL21(DE3) pLysE, expression vector pET15b672260Q460H9TrEMBLManually annotated by BRENDA team
Streptomyces lividansrecombinant protein672260--Manually annotated by BRENDA team
Synechocystis sp.PCC6714645615--Manually annotated by BRENDA team
Synechocystis sp.PCC6803645621--Manually annotated by BRENDA team
Synechocystis sp.strain PCC 6803660879, 661091, 702269--Manually annotated by BRENDA team
Synechocystis sp.strain PCC 6803661090Q55793UniprotManually annotated by BRENDA team
Trypanosoma brucei-703682--Manually annotated by BRENDA team
Trypanosoma brucei-703682Q386Y7UniProtManually annotated by BRENDA team

GENERAL INFORMATIONORGANISM UNIPROT ACCESSION NO.COMMENTARYLITERATURE
physiological functionEscherichia coli-IscS is the primary physiological sulfur-donating enzyme for the generation of the thiocarboxylate of molybdopterin synthase in molybdopterin biosynthesis704679

SUBSTRATEPRODUCT                      REACTION DIAGRAMORGANISM UNIPROT ACCESSION NO. COMMENTARY/
Substrate		 LITERATURE/
Substrate		 COMMENTARY/
Product		 LITERATURE/
Product		 Reversibility
r=reversible
ir=irreversible
?=not specified
L-cysteinepyruvate + sulfide
show the reaction diagram		Synechocystis sp.-unlike other cysteine desulfurases the L-cysteine C-S-lyase from Synechocystis does not have a conserved cysteine residue at the active site645615-645615?
L-cysteineL-alanine + H2S
show the reaction diagram		Acidithiobacillus ferrooxidans--672753or formation of elemental sulfur, depending of presence of a reducing agent in the reaction mixture-?
L-cysteineL-alanine + sulfur
show the reaction diagram		Streptomyces lividansQ460H9DndA 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 activity672260--?
L-cysteine + ??
show the reaction diagram		Escherichia coli-in the presence of cysteine, IscS’s ability to bind iron improves significantly690744--?
L-cysteine + ?L-alanine + ?
show the reaction diagram		Acidithiobacillus ferrooxidans-catalyzes the elimination of S from L-cysteine to yield L-alanine and elemental sulfur or H2S, depending on whether or not a reducing agent is added to the reaction mixture, provides sulfur for the assembly of iron–sulfur cluster672753--?
L-cysteine + c-ISCSL-alanine + c-ISCS-SSH
show the reaction diagram		Homo sapiens--674541--?
L-cysteine + c-IscUL-alanine + c-IscU-SSH
show the reaction diagram		Escherichia coli--705872--?
L-cysteine + CpNifSL-alanine + CpNifS-SSH
show the reaction diagram		Arabidopsis thaliana--674773--?
L-cysteine + DndAL-alanine + DndA-SSH
show the reaction diagram		Streptomyces lividansQ460H9-672260--?
L-cysteine + enzyme-cysteineL-alanine + enzyme-S-sulfanylcysteine
show the reaction diagram		Saccharomyces cerevisiae-involved in the formation of Fe-S proteins662257--?
L-cysteine + IscSL-alanine + IscS-SSH
show the reaction diagram		Escherichia coli--662209--?
L-cysteine + RhdAL-alanine + RhdA-SSH
show the reaction diagram		Escherichia coli-transfer of sulfur to rhodanese with formation of a covalent complex between IscS and RhdA661771--?
L-cysteine + Slr0077L-alanine + Slr0077-SSH
show the reaction diagram		Synechocystis sp.--660879--?
L-cysteine + SufSL-alanine + SufS-SSH
show the reaction diagram		Synechocystis sp.Q55793-661090--?
L-cysteine + SufSL-alanine + SufS-SSH
show the reaction diagram		Synechocystis sp.--661091--?
L-cysteine + [enzyme]-cysteineL-alanine + [enzyme]-S-sulfanylcysteine
show the reaction diagram		Bacteria--645619--?
L-cysteine + [enzyme]-cysteineL-alanine + [enzyme]-S-sulfanylcysteine
show the reaction diagram		Escherichia coli--645638---
L-cysteine + [enzyme]-cysteineL-alanine + [enzyme]-S-sulfanylcysteine
show the reaction diagram		Escherichia coli--645615, 645616--?
L-cysteine + [enzyme]-cysteineL-alanine + [enzyme]-S-sulfanylcysteine
show the reaction diagram		Escherichia coliP25745-645620-645620?
L-cysteine + [enzyme]-cysteineL-alanine + [enzyme]-S-sulfanylcysteine
show the reaction diagram		Escherichia coli--645627-645627?
L-cysteine + [enzyme]-cysteineL-alanine + [enzyme]-S-sulfanylcysteine
show the reaction diagram		Escherichia coli--645628, 645630, 645632--?
L-cysteine + [enzyme]-cysteineL-alanine + [enzyme]-S-sulfanylcysteine
show the reaction diagram		Escherichia coli--645632-645632?
L-cysteine + [enzyme]-cysteineL-alanine + [enzyme]-S-sulfanylcysteine
show the reaction diagram		Escherichia coli--645633, 645634, 645635, 645638--?
L-cysteine + [enzyme]-cysteineL-alanine + [enzyme]-S-sulfanylcysteine
show the reaction diagram		Azotobacter vinelandii--645615, 645624--?
L-cysteine + [enzyme]-cysteineL-alanine + [enzyme]-S-sulfanylcysteine
show the reaction diagram		Azotobacter vinelandii--645624-645624?
L-cysteine + [enzyme]-cysteineL-alanine + [enzyme]-S-sulfanylcysteine
show the reaction diagram		Azotobacter vinelandii--645631-645631?
L-cysteine + [enzyme]-cysteineL-alanine + [enzyme]-S-sulfanylcysteine
show the reaction diagram		Azotobacter vinelandii--645636--?
L-cysteine + [enzyme]-cysteineL-alanine + [enzyme]-S-sulfanylcysteine
show the reaction diagram		Erwinia chrysanthemi--645628--?
L-cysteine + [enzyme]-cysteineL-alanine + [enzyme]-S-sulfanylcysteine
show the reaction diagram		Salmonella enterica--645633--?
L-cysteine + [enzyme]-cysteineL-alanine + [enzyme]-S-sulfanylcysteine
show the reaction diagram		Synechocystis sp.--645615, 645621, 702269--?
L-cysteine + [enzyme]-cysteineL-alanine + [enzyme]-S-sulfanylcysteine
show the reaction diagram		Ruminococcus flavefaciens--645640--?
L-cysteine + [enzyme]-cysteineL-alanine + [enzyme]-S-sulfanylcysteine
show the reaction diagram		Trypanosoma bruceiQ386Y7-703682--?
L-cysteine + [enzyme]-cysteineL-alanine + [enzyme]-S-sulfanylcysteine
show the reaction diagram		Synechocystis sp.-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 not645621--?
L-cysteine + [enzyme]-cysteineL-alanine + [enzyme]-S-sulfanylcysteine
show the reaction diagram		Azotobacter vinelandii-catalyzes the conversion of cysteine to alanine and sulfane sulfur via the formation of a protein-bound cysteine persulfide intermediate on a conserved cysteine residue645615--?
L-cysteine + [enzyme]-cysteineL-alanine + [enzyme]-S-sulfanylcysteine
show the reaction diagram		Escherichia coli-iscS has cysteine desulfurase activity and mobilizes sulfur from cysteine for the repair of the [4Fe-4S] cluster in apo-dihydroxyacid dehydratase645615--?
L-cysteine + [enzyme]-cysteineL-alanine + [enzyme]-S-sulfanylcysteine
show the reaction diagram		Azotobacter vinelandii-intermediate is an enzyme-bound cysteinyl persulfide645636--?
L-cysteine + [enzyme]-cysteineL-alanine + [enzyme]-S-sulfanylcysteine
show the reaction diagram		Escherichia coli-Cys364 residue is essential for activity toward L-cysteine but not toward L-selenocyteine645630--?
L-cysteine + [enzyme]-cysteineL-alanine + [enzyme]-S-sulfanylcysteine
show the reaction diagram		Acidithiobacillus ferrooxidans-IscS has a high affinity for L-cysteine706851--?
L-cysteine + [enzyme]-cysteineL-alanine + [enzyme]-S-sulfanylcysteine
show the reaction diagram		Escherichia coli-IscS transfers the sulfur atom from L-cysteine to the C-terminal thiocarboxylate of the MoaD subunit in vitro704679--?
L-cysteine sulfinic acidL-alanine + sulfite
show the reaction diagram		Escherichia coli--645632--?
L-cysteine sulfinic acidL-alanine + sulfite
show the reaction diagram		Synechocystis sp.-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 not645621-645621?
L-cysteine sulfinic acid + ??
show the reaction diagram		Streptomyces lividansQ460H9cysteine desulfurase DndA catalyzes iron-sulfur cluster assembly by activation of apo-Fe DndC protein672260--?
L-cysteine sulfinic acid + DndA?
show the reaction diagram		Streptomyces lividansQ460H9-672260--?
L-cystine?
show the reaction diagram		Synechocystis sp.--645621--?
L-cystine + Slr0077pyruvate + Slr0077-SSH
show the reaction diagram		Synechocystis sp.-cystine lyase of Slr0077660879--?
L-selenocysteineL-alanine + selenium
show the reaction diagram		Escherichia coli--645615--?
L-selenocysteineL-alanine + selenium
show the reaction diagram		Escherichia coliP77444-645617--?
L-selenocysteineL-alanine + selenium
show the reaction diagram		Escherichia coli--645628--?
L-selenocysteineL-alanine + selenium
show the reaction diagram		Escherichia coli--645632-645632?
L-selenocysteineL-alanine + selenium
show the reaction diagram		Arabidopsis thaliana--674773--?
L-selenocysteineL-alanine + selenium
show the reaction diagram		Azotobacter vinelandii--645615--?
L-selenocysteineL-alanine + selenium
show the reaction diagram		Azotobacter vinelandii--645624-645624?
L-selenocysteineL-alanine + selenium
show the reaction diagram		Erwinia chrysanthemi--645628--?
L-selenocysteineL-alanine + selenium
show the reaction diagram		Synechocystis sp.--645615--?
L-selenocysteineL-alanine + selenium
show the reaction diagram		Synechocystis sp.-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 not645621--?
L-selenocysteineL-alanine + selenium
show the reaction diagram		Escherichia coli-Cys364 residue is essential for activity toward L-cysteine but not toward L-selenocyteine645630--?
L-selenocysteine + ??
show the reaction diagram		Streptomyces lividansQ460H9-672260--?
L-selenocysteine + DndAL-alanine + DndA-SSeH
show the reaction diagram		Streptomyces lividansQ460H9-672260--?
L-selenocystine?
show the reaction diagram		Synechocystis sp.--645621--?
additional information?-Saccharomyces cerevisiae--645615---
additional information?-Azotobacter vinelandii-enzyme catalyzes the formation of Fe-S clusters in a component protein of nitrogenase in the presence of cysteine and ferrous iron in vitro645615---
additional information?-Escherichia coli-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 dehydrogenase645637---
additional information?-Haemophilus influenzae, Escherichia coli, Pseudomonas aeruginosa-isc genes are involved in the formation of Fe-S clusters in various Fe-S proteins645615---
additional information?-Escherichia coli, Azotobacter vinelandii-enzyme is involved in selenoprotein biosynthesis645615---
additional information?-Azotobacter vinelandii-enzyme serves as a selenide delivery protein for the in vitro biosynthesis of selenophosphate645624---
additional information?-Ruminococcus flavefaciens-involved in the production of sulfur for the mormation of iron-sulfur clusters645640---
additional information?-Escherichia coli-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 thionucleosides645627---
additional information?-Azotobacter vinelandii-involved in the mobilization of iron or sulfur required for metallocluster formation645631---
additional information?-Escherichia coli-acts as sulfurtransferase in biosynthesis of 4-thiouridine in tRNA645627---
additional information?-Escherichia coli-enzyme contributes to the biotin synthase reaction, probably by supplying sulfur to the BioB protein645614---
additional information?-Saccharomyces cerevisiae-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 biogenesis645622---
additional information?-Escherichia coli-facilitates the formation of the iron-sulfur cluster of ferredoxin in vitro645638---
additional information?-Escherichia coliP25745involved in biosynthesis of 2-thiouridine645620---
additional information?-Klebsiella pneumoniae-enzyme participates in biotin synthase reaction, probably by supplying sulfur to the iron-sulfur cluster of biotin synthase645614---
additional information?-Escherichia coli-involved in biosynthesis of thionucleosides645626, 645633---
additional information?-Salmonella enterica-involved in biosynthesis of thionucleosides645633---
additional information?-Azotobacter vinelandii-enzyme participates in the biosynthesis of the nitrogenase metalloclusters by providing the inorganic sulfur required for Fe-S core formation645636---
additional information?-Cryptosporidium parvumQ8WQX4functions as scaffold for the assembly of [Fe-S] prior to their incorporation into apoproteins645639---
additional information?-Escherichia coli-involved in thiamine biosynthesis, molybdopterin biosynthesis and tRNA modification645615---
additional information?-Escherichia coli-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 proteins645635---
additional information?-Saccharomyces cerevisiae-cysteine desulfurase is required for the proper post-translational modification of the lipoamide-containing mitochondrial subproteome in yeast675989---
additional information?-Klebsiella pneumoniae-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 nitrogenase674877---
additional information?-Acidithiobacillus ferrooxidans-enzyme is involved in the iron-sulfur cluster assembly672753---
additional information?-Rhodobacter capsulatus-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 XdhC672277---
additional information?-Salmonella enterica-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 IscS674271---
additional information?-Streptomyces lividansQ460H9cysteine desulfurase DndA catalyzes iron-sulfur cluster assembly by activation of apo-Fe DndC protein, no substrate: L-cystine, L-selenocystine672260---
additional information?-Streptomyces lividans-no substrate: L-cystine, L-selenocystine672260---
additional information?-Rhodobacter capsulatus-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 XdhC672277---
additional information?-Streptomyces lividansQ460H9substrate specificity similar to that of Escherichia coli IscS672260---
additional information?-Escherichia coli-SufA is able to bind sulfur atoms provided by the SufS-SufE complex692336---
additional information?-Escherichia coli-SufS and SufE proteins interact with the SufBCD protein complex to facilitate sulfur liberation from cysteine and donation for Fe-S cluster assembly674798---
additional information?-Escherichia coli-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 regulation690737---
additional information?-Streptomyces lividansQ460H9no substrates are L-cystine, L-selenocystine672260---
additional information?-Escherichia coli-IscS is involved in the sulfuration of MoaD subunit704679---

NATURAL SUBSTRATESNATURAL PRODUCTSREACTION DIAGRAMORGANISM UNIPROT ACCESSION NO.COMMENTARY SUBSTRATELITERATURE
(Substrate)		COMMENTARY PRODUCTLITERATURE
(Product)
L-cysteineL-alanine + sulfur
show the reaction diagram		Streptomyces lividansQ460H9DndA 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 activity672260--
L-cysteine + enzyme-cysteineL-alanine + enzyme-S-sulfanylcysteine
show the reaction diagram		Saccharomyces cerevisiae-involved in the formation of Fe-S proteins662257--
L-cysteine + IscSL-alanine + IscS-SSH
show the reaction diagram		Escherichia coli--662209--
L-cysteine + RhdAL-alanine + RhdA-SSH
show the reaction diagram		Escherichia coli--661771--
L-cysteine + Slr0077L-alanine + Slr0077-SSH
show the reaction diagram		Synechocystis sp.--660879--
L-cysteine + SufSL-alanine + SufS-SSH
show the reaction diagram		Synechocystis sp.Q55793-661090--
L-cysteine + SufSL-alanine + SufS-SSH
show the reaction diagram		Synechocystis sp.--661091--
L-cysteine + [enzyme]-cysteineL-alanine + [enzyme]-S-sulfanylcysteine
show the reaction diagram		Bacteria--645619--
L-cysteine + [enzyme]-cysteineL-alanine + [enzyme]-S-sulfanylcysteine
show the reaction diagram		Escherichia coli--645638, 645615, 645616--
L-cysteine + [enzyme]-cysteineL-alanine + [enzyme]-S-sulfanylcysteine
show the reaction diagram		Escherichia coliP25745-645620--
L-cysteine + [enzyme]-cysteineL-alanine + [enzyme]-S-sulfanylcysteine
show the reaction diagram		Escherichia coli--645627, 645628, 645630, 645632, 645633, 645634, 645635--
L-cysteine + [enzyme]-cysteineL-alanine + [enzyme]-S-sulfanylcysteine
show the reaction diagram		Azotobacter vinelandii--645615, 645624, 645631, 645636--
L-cysteine + [enzyme]-cysteineL-alanine + [enzyme]-S-sulfanylcysteine
show the reaction diagram		Erwinia chrysanthemi--645628--
L-cysteine + [enzyme]-cysteineL-alanine + [enzyme]-S-sulfanylcysteine
show the reaction diagram		Salmonella enterica--645633--
L-cysteine + [enzyme]-cysteineL-alanine + [enzyme]-S-sulfanylcysteine
show the reaction diagram		Synechocystis sp.--645615, 645621--
L-cysteine + [enzyme]-cysteineL-alanine + [enzyme]-S-sulfanylcysteine
show the reaction diagram		Ruminococcus flavefaciens--645640--
additional information?-Saccharomyces cerevisiae--645615--
additional information?-Azotobacter vinelandii-enzyme catalyzes the formation of Fe-S clusters in a component protein of nitrogenase in the presence of cysteine and ferrous iron in vitro645615--
additional information?-Escherichia coli-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 dehydrogenase645637--
additional information?-Haemophilus influenzae, Escherichia coli, Pseudomonas aeruginosa-isc genes are involved in the formation of Fe-S clusters in various Fe-S proteins645615--
additional information?-Escherichia coli, Azotobacter vinelandii-enzyme is involved in selenoprotein biosynthesis645615--
additional information?-Azotobacter vinelandii-enzyme serves as a selenide delivery protein for the in vitro biosynthesis of selenophosphate645624--
additional information?-Ruminococcus flavefaciens-involved in the production of sulfur for the mormation of iron-sulfur clusters645640--
additional information?-Escherichia coli-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 thionucleosides645627--
additional information?-Azotobacter vinelandii-involved in the mobilization of iron or sulfur required for metallocluster formation645631--
additional information?-Escherichia coli-acts as sulfurtransferase in biosynthesis of 4-thiouridine in tRNA645627--
additional information?-Escherichia coli-enzyme contributes to the biotin synthase reaction, probably by supplying sulfur to the BioB protein645614--
additional information?-Saccharomyces cerevisiae-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 biogenesis645622--
additional information?-Escherichia coli-facilitates the formation of the iron-sulfur cluster of ferredoxin in vitro645638--
additional information?-Escherichia coliP25745involved in biosynthesis of 2-thiouridine645620--
additional information?-Klebsiella pneumoniae-enzyme participates in biotin synthase reaction, probably by supplying sulfur to the iron-sulfur cluster of biotin synthase645614--
additional information?-Escherichia coli-involved in biosynthesis of thionucleosides645626, 645633--
additional information?-Salmonella enterica-involved in biosynthesis of thionucleosides645633--
additional information?-Azotobacter vinelandii-enzyme participates in the biosynthesis of the nitrogenase metalloclusters by providing the inorganic sulfur required for Fe-S core formation645636--
additional information?-Cryptosporidium parvumQ8WQX4functions as scaffold for the assembly of [Fe-S] prior to their incorporation into apoproteins645639--
additional information?-Escherichia coli-involved in thiamine biosynthesis, molybdopterin biosynthesis and tRNA modification645615--
additional information?-Escherichia coli-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 proteins645635--
additional information?-Saccharomyces cerevisiae-cysteine desulfurase is required for the proper post-translational modification of the lipoamide-containing mitochondrial subproteome in yeast675989--
additional information?-Klebsiella pneumoniae-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 nitrogenase674877--
additional information?-Acidithiobacillus ferrooxidans-enzyme is involved in the iron-sulfur cluster assembly672753--
additional information?-Rhodobacter capsulatus-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 XdhC672277--
additional information?-Salmonella enterica-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 IscS674271--
additional information?-Rhodobacter capsulatus-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 XdhC672277--
additional information?-Streptomyces lividansQ460H9substrate specificity similar to that of Escherichia coli IscS672260--
additional information?-Escherichia coli-SufA is able to bind sulfur atoms provided by the SufS-SufE complex692336--
additional information?-Escherichia coli-SufS and SufE proteins interact with the SufBCD protein complex to facilitate sulfur liberation from cysteine and donation for Fe-S cluster assembly674798--
additional information?-Escherichia coli-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 regulation690737--

COFACTORORGANISM UNIPROT ACCESSION NO.COMMENTARYLITERATUREIMAGE
pyridoxal 5'-phosphateEscherichia coli--645615, 645616, 645630, 704679, 705872 2D-image
pyridoxal 5'-phosphateAzotobacter vinelandii--645615 2D-image
pyridoxal 5'-phosphateArabidopsis thaliana--645618 2D-image
pyridoxal 5'-phosphateBacteria--645619 2D-image
pyridoxal 5'-phosphateAzotobacter vinelandii-0.8 mol per monomer645631 2D-image
pyridoxal 5'-phosphateSynechocystis sp.--661090, 661091, 702269 2D-image
pyridoxal 5'-phosphateStreptomyces lividansQ460H9; 672260 2D-image
pyridoxal 5'-phosphateRhodobacter capsulatus--672277 2D-image
pyridoxal 5'-phosphateAcidithiobacillus ferrooxidans--672753, 706851 2D-image
pyridoxal 5'-phosphateTrypanosoma bruceiQ386Y7-703682 2D-image

METALS and IONS ORGANISM UNIPROT ACCESSION NO.COMMENTARY LITERATURE
IronKlebsiella pneumoniae-[Fe-S] cluster645614
IronBacteria-[Fe-S] cluster645619
IronSynechocystis sp.-[Fe2-S2]ferredoxin645621
IronStreptomyces lividansQ460H9a single [4Fe-4S] cluster per DndC monomer672260
IronAcidithiobacillus ferrooxidans-Fe-S cluster672753
IronArabidopsis thaliana-Fe-S cluster676898
IronEscherichia coli-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 effectively690744

INHIBITORSORGANISM UNIPROT ACCESSION NO. COMMENTARY LITERATURE IMAGE
4-chloromercuribenzoateAzotobacter vinelandii-preincubation dramatically inhibits enzyme activity645631 2D-image
Fe2+Escherichia coli-the low desulfurase activity is caused by the modification of IscS rather than by the formation of FeS in the solution690744 2D-image
interferon-gammaMus musculus-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-gamma671626-
iodoacetamideAzotobacter vinelandii-preincubation dramatically inhibits enzyme activity645631 2D-image
K2TeO3Escherichia coli-mutant strains csdA::Kn, csdB::Kn, ascS::Kn663375-
L-AllylglycineAzotobacter vinelandii-irreversible inactivation645636 2D-image
L-selenocysteineAzotobacter vinelandii-inhibits desulfuration of L-cysteine645624 2D-image
N-ethylmaleimideAzotobacter vinelandii-preincubation dramatically inhibits enzyme activity645631 2D-image
N-iodoacetyl-N'-(5-sulfo-1-naphthyl)ethylenediamineAcidithiobacillus ferrooxidans-up to 90% inhibition at 5 mM706851 2D-image
VinylglycineAzotobacter vinelandii-irreversible inactivation645636 2D-image
lipopolysaccharideMus musculus-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 macrophages671626 2D-image
additional informationMus musculus-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 expression671626-
additional informationEscherichia coli-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 complex690744-
additional informationEscherichia coli-CyaYdoes not inhibit the desulfurase activity of Isc705872-

ACTIVATING COMPOUNDORGANISM UNIPROT ACCESSION NO. COMMENTARY LITERATURE IMAGE
dithiothreitolSynechocystis sp.-increase of enzyme activity at 50 mM645621 2D-image
protein Isd11Saccharomyces cerevisiae-forms a stable complex with Nfs1, prone to aggregation in the absence of Isd11661595-
pyridoxal-5'-phosphateEscherichia coli--661771 2D-image
pyruvateSynechocystis sp.-increase of enzyme activity at 5 mM645621 2D-image
pyruvateEscherichia coli-increases activity of CSD towards L-selenocysteine, but not towards L-cysteine645632 2D-image
Suf protein familyEscherichia coli-SufE protein can stimulate up to 8fold, addition of the SufBCD complex further stimulates up to 32fold645634-
SufEErwinia chrysanthemi, Escherichia coli-binding of SufE, a member of the SUF protein system, to SufS stimulates the cysteine desulfurase activity of SufS by 50fold645628-
SufEEscherichia coli-SufE protein can stimulate up to 8fold645634-
IcsUEscherichia coli-forms disulfide bonds with IcsS and stimulates its activity 6fold645638-
additional informationArabidopsis thaliana-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 CpNifS674773-

KM VALUE [mM]KM VALUE [mM] MaximumSUBSTRATEORGANISM UNIPROT ACCESSION NO. COMMENTARY LITERATURE IMAGE
0.043-L-cysteineArabidopsis thaliana-25°C, pH 7.4, presence of chloroplast protein CpSufE674773 2D-image
0.075-L-cysteineAzotobacter vinelandii--645636 2D-image
0.1-L-cysteineArabidopsis thaliana-25°C, pH 7.4674773 2D-image
0.11-L-cysteineAcidithiobacillus ferrooxidans-in 50 mM Tris-HCl (pH 8.0), 10 mM MgCl2, 5 mM dithiothreitol, at 25°C706851 2D-image
5.1-L-cysteineStreptomyces lividansQ460H9pH 8.0, 37°C; pH 8.0, 37°C672260 2D-image
0.28-L-cysteine sulfinic acidSynechocystis sp.-pH 7.5, 37°C, isoenzyme SsCsd2645621 2D-image
3.5-L-cysteine sulfinic acidEscherichia coli-pH 8, CSD in the presence of pyruvate645632 2D-image
17-L-cysteine sulfinic acidSynechocystis sp.-pH 7.5, 37°C, isoenzyme SsCsd1645621 2D-image
26-L-cysteine sulfinic acidEscherichia coli-pH 8, IcsS in the absence of pyruvate645632 2D-image
30-L-cysteine sulfinic acidEscherichia coli-pH 8, CsdB in the presence of pyruvate645632 2D-image
39-L-cysteine sulfinic acidEscherichia coli-pH 8, CsdB in the absence of pyruvate645632 2D-image
190-L-cysteine sulfinic acidEscherichia coli-pH 8, IcsS in the presence of pyruvate645632 2D-image
0.13-L-selenocysteineAzotobacter vinelandii-37°C645624 2D-image
0.36-L-selenocysteineStreptomyces lividansQ460H9pH 8.0, 37°C; pH 8.0, 37°C672260 2D-image
0.43-L-selenocysteineSynechocystis sp.-pH 7.5, 37°C, isoenzyme SsCsd1645621 2D-image
0.59-L-selenocysteineSynechocystis sp.-pH 7.5, 37°C, isoenzyme SsCsd2645621 2D-image
1.1-L-selenocysteineEscherichia coli-pH 8, IcsS in the presence of pyruvate645632 2D-image
1.4-L-selenocysteineEscherichia coli-pH 8, CSD in the presence of pyruvate645632 2D-image
2-L-selenocysteineErwinia chrysanthemi-pH 8, 37°C645628 2D-image
2.6-L-selenocysteineEscherichia coli-pH 8, CsdB in the presence of pyruvate645632 2D-image
2.9-L-selenocysteineArabidopsis thaliana-25°C, pH 7.4674773 2D-image
4.17-L-selenocysteineArabidopsis thaliana-25°C, pH 7.4, presence of chloroplast protein CpSufE674773 2D-image

TURNOVER NUMBER [1/s] TURNOVER NUMBER MAXIMUM[1/s] SUBSTRATEORGANISM UNIPROT ACCESSION NO. COMMENTARY LITERATURE IMAGE
0.1-L-cysteineAzotobacter vinelandii-37°C645624 2D-image
0.5-L-cysteineStreptomyces lividansQ460H9pH 8.0, 37°C; pH 8.0, 37°C672260 2D-image
3.2-L-cysteine sulfinic acidSynechocystis sp.-pH 7.5, 37°C, isoenzyme SsCsd1645621 2D-image
3.4-L-cysteine sulfinic acidSynechocystis sp.-pH 7.5, 37°C, isoenzyme SsCsd2645621 2D-image
0.04-L-selenocysteineAzotobacter vinelandii-37°C645624 2D-image
1.4-L-selenocysteineStreptomyces lividansQ460H9pH 8.0, 37°C; pH 8.0, 37°C672260 2D-image
4-L-selenocysteineSynechocystis sp.-pH 7.5, 37°C, isoenzyme SsCsd2645621 2D-image
15-L-selenocysteineSynechocystis sp.-pH 7.5, 37°C, isoenzyme SsCsd1645621 2D-image

kcat/KM VALUE [1/mMs-1]kcat/KM VALUE [1/mMs-1] MaximumSUBSTRATEORGANISM UNIPROT ACCESSION NO. COMMENTARY LITERATURE IMAGE
No entries in this field

Ki VALUE [mM]Ki VALUE [mM] MaximumINHIBITORORGANISM UNIPROT ACCESSION NO. COMMENTARY LITERATURE IMAGE
20-allylglycineAzotobacter vinelandii--645636 2D-image

IC50 VALUE [mM]IC50 VALUE [mM] MaximumINHIBITORORGANISM UNIPROT ACCESSION NO. COMMENTARY LITERATURE IMAGE
No entries in this field

SPECIFIC ACTIVITY [µmol/min/mg] SPECIFIC ACTIVITY MAXIMUM ORGANISM UNIPROT ACCESSION NO. COMMENTARY LITERATURE
0.0022-Escherichia coli-mutant S326A for s4U synthesis662209
0.0034-Escherichia coli-mutant S328A for s4U synthesis662209
0.0036-Escherichia coli-wild type for s4U synthesis662209
0.0038-Escherichia coli-mutant S336A for s4U synthesis662209
0.0043-Escherichia coli-mutant L333A for s4U synthesis662209
0.008-Escherichia coli-recombinant enzyme with L-cysteine as substrate645634
0.0127-Saccharomyces cerevisiae-cysteine to DTT662257
0.0224-Acidithiobacillus ferrooxidans-crude extract, at 25°C706851
0.05-Escherichia coli-H123 mutant with L-selenocysteine as substrate645630
0.055-Azotobacter vinelandii-with L-selenocysteine as substrate645624
0.082-Acidithiobacillus ferrooxidans-pH 8.0, 50°C, rate of production of thiocyanate672753
0.1-Trypanosoma bruceiQ386Y7knockdown of Nfs-like proteins, activity measured in mitochondrial fractions703682
0.142-Azotobacter vinelandii-with L-cysteine as substrate645624
0.148-Acidithiobacillus ferrooxidans-enzyme after purification, at 25°C706851
0.2-Trypanosoma bruceiQ386Y7knockdown of selenocysteine lyase, activity measured in mitochondrial fractions703682
0.5-Trypanosoma bruceiQ386Y7knockdown of selenocysteine lyase, activity measured in cytosolic fractions703682
0.9-Trypanosoma bruceiQ386Y7activity measured in mitochondrial fractions703682
1-Trypanosoma bruceiQ386Y7knockdown of Nfs-like proteins, activity measured in cytosolic fractions703682
2.5-Trypanosoma bruceiQ386Y7activity measured in cytosolic fractions703682
3.6-Streptomyces lividansQ460H9substrate L-cysteine sulfinic acid, pH 8.0, 37°C; substrate L-cysteine sulfinic acid, pH 8.0, 37°C672260
4.5-Synechocystis sp.-isoenzyme SsCsd1, with L-cysteine sulfinic acid as substrate645621
4.8-Synechocystis sp.-isoenzyme SsCsd2, with L-cysteine sulfinic acid as substrate645621
5.8-Synechocystis sp.-isoenzyme SsCsd2, with L-selenocysteine as substrate645621
21-Synechocystis sp.-isoenzyme SsCsd1, with L-selenocysteine as substrate645621
38.6-Streptomyces lividansQ460H9substrate L-cysteine, pH 8.0, 37°C; substrate L-selenocysteine, pH 8.0, 37°C672260
56.5-Streptomyces lividansQ460H9substrate L-cysteine, pH 8.0, 37°C; substrate L-selenocysteine, pH 8.0, 37°C672260
82500-Acidithiobacillus ferrooxidans-pH 8.0, 50°C672753
additional information-Streptomyces lividansQ460H9no detectable activity for L-selenocystine and L-cystine672260

pH OPTIMUMpH MAXIMUMORGANISM UNIPROT ACCESSION NO. COMMENTARYLITERATURE
7-Synechocystis sp.-isoenzyme SsCsd1 with L-selenocysteine and isoenzyme SsCsd2 with L-selenocysteine and L-cysteine sulfinic acid as substrates645621
7.4-Trypanosoma bruceiQ386Y7assay at703682
7.7-Synechocystis sp.-isoenzyme SsCsd1 with S-cysteine sulfinic acid as substrate645621
88.5Acidithiobacillus ferrooxidans--706851
8.38.6Ruminococcus flavefaciens--645640
8.5-Saccharomyces cerevisiae--662257
additional information-Azotobacter vinelandii-activity is highly sensitive to pH645636

pH RANGEpH RANGE MAXIMUMORGANISM UNIPROT ACCESSION NO.COMMENTARYLITERATURE
79Acidithiobacillus ferrooxidans--706851

TEMPERATURE OPTIMUMTEMPERATURE OPTIMUM MAXIMUMORGANISM UNIPROT ACCESSION NO.COMMENTARYLITERATURE
25-Trypanosoma bruceiQ386Y7assay at703682
30-Acidithiobacillus ferrooxidans--706851
37-Synechocystis sp.-assay at645621
37-Azotobacter vinelandii-assay at645624
37-Erwinia chrysanthemi-assay at645628
37-Ruminococcus flavefaciens--645640
additional information-Azotobacter vinelandii-activity is highly sensitive to temperature645636

TEMPERATURE RANGE TEMPERATURE MAXIMUM ORGANISM UNIPROT ACCESSION NO. COMMENTARY LITERATURE
No entries in this field

pI VALUEpI VALUE MAXIMUMORGANISM UNIPROT ACCESSION NO.COMMENTARYLITERATURE
No entries in this field

SOURCE TISSUE ORGANISM UNIPROT ACCESSION NO. COMMENTARY LITERATURE SOURCE
brainHomo sapiens--645625Manually annotated by BRENDA team
brainRattus norvegicusQ99P39-662693Manually annotated by BRENDA team
fibroblastMus musculusQ9Z1J3cultured fibroblast674628Manually annotated by BRENDA team
heartHomo sapiens--645625Manually annotated by BRENDA team
heartRattus norvegicusQ99P39-662693Manually annotated by BRENDA team
HeLa cellHomo sapiens--675971Manually annotated by BRENDA team
K-562 cellHomo sapiens--645625Manually annotated by BRENDA team
liverHomo sapiens--645625Manually annotated by BRENDA team
liverRattus norvegicusQ99P39-662693Manually annotated by BRENDA team
lungRattus norvegicusQ99P39-662693Manually annotated by BRENDA team
macrophageMus musculus-enzyme isoform Nfs1; mitochondrial isoform of Nfs1671626Manually annotated by BRENDA team
pancreasHomo sapiens--645625Manually annotated by BRENDA team
skeletal muscleHomo sapiens--645625Manually annotated by BRENDA team
skeletal muscleRattus norvegicusQ99P39-662693Manually annotated by BRENDA team
sporozoiteCryptosporidium parvumQ8WQX4-645639Manually annotated by BRENDA team

LOCALIZATION ORGANISM UNIPROT ACCESSION NO. COMMENTARY GeneOntology No. LITERATURE SOURCE
chloroplastArabidopsis thaliana--9507645618, 676898Manually annotated by BRENDA team
cytoplasmErwinia chrysanthemi, Escherichia coli--5737645628Manually annotated by BRENDA team
cytoplasmTrypanosoma bruceiQ386Y7-5737703682Manually annotated by BRENDA team
cytosolHomo sapiens--5829645625, 674541Manually annotated by BRENDA team
cytosolSaccharomyces cerevisiae-low activity5829662257Manually annotated by BRENDA team
cytosolHomo sapiens-small amounts of isoform Nfs15829675971Manually annotated by BRENDA team
cytosolTrypanosoma bruceiQ386Y7-5829703682Manually annotated by BRENDA team
mitochondrial matrixSaccharomyces cerevisiae--5759645615, 645622, 661595Manually annotated by BRENDA team
mitochondrial matrixHomo sapiens, Mus musculus--5759645615Manually annotated by BRENDA team
mitochondrionHomo sapiens--5739645625Manually annotated by BRENDA team
mitochondrionCryptosporidium parvumQ8WQX4enzyme has an N-terminal targeting signal that directs the enzyme to mitochondria when expressed in Saccharomyces cerevisiae5739645639Manually annotated by BRENDA team
mitochondrionSaccharomyces cerevisiae--5739662190Manually annotated by BRENDA team
mitochondrionSaccharomyces cerevisiae-mitochondrial Nfs1p is required for the biogenesis of both mitochondrial and extramitochondrial Fe/S proteins5739662257Manually annotated by BRENDA team
mitochondrionRattus norvegicusQ99P39-5739662693Manually annotated by BRENDA team
mitochondrionHomo sapiens-predominat localization of isoform Nfs15739675971Manually annotated by BRENDA team
mitochondrionMus musculus--5739675971Manually annotated by BRENDA team
mitochondrionTrypanosoma bruceiQ386Y7-5739703682Manually annotated by BRENDA team
nucleusHomo sapiens--5634645625Manually annotated by BRENDA team
nucleusSaccharomyces cerevisiae--5634662190Manually annotated by BRENDA team
nucleusSaccharomyces cerevisiae-low activity5634662257Manually annotated by BRENDA team
nucleusTrypanosoma bruceiQ386Y7-5634703682Manually annotated by BRENDA team

PDBSCOPCATHORGANISM
4eb5, downloadSCOP (4eb5)CATH (4eb5)Archaeoglobus fulgidus (strain ATCC 49558 / VC-16 / DSM 4304 / JCM 9628 / NBRC 100126)
4eb7, downloadSCOP (4eb7)CATH (4eb7)Archaeoglobus fulgidus (strain ATCC 49558 / VC-16 / DSM 4304 / JCM 9628 / NBRC 100126)
4hvk, downloadSCOP (4hvk)CATH (4hvk)Archaeoglobus fulgidus (strain ATCC 49558 / VC-16 / DSM 4304 / JCM 9628 / NBRC 100126)
3lvj, downloadSCOP (3lvj)CATH (3lvj)Escherichia coli O157:H7
3lvk, downloadSCOP (3lvk)CATH (3lvk)Escherichia coli O157:H7
3lvl, downloadSCOP (3lvl)CATH (3lvl)Escherichia coli O157:H7
3lvm, downloadSCOP (3lvm)CATH (3lvm)Escherichia coli O157:H7
1t3i, downloadSCOP (1t3i)CATH (1t3i)Synechocystis sp. (strain PCC 6803 / Kazusa)

MOLECULAR WEIGHT MOLECULAR WEIGHT MAXIMUM ORGANISM UNIPROT ACCESSION NO. COMMENTARY LITERATURE
42000-Ruminococcus flavefaciens-SDS-PAGE645640
43200-Ruminococcus flavefaciens-calculated from nucleotide sequence645640
45000-Streptomyces lividansQ460H9subunit, SDS-PAGE672260
46000-Acidithiobacillus ferrooxidans-recombinant IscS by SDS-PAGE672753
46000-Acidithiobacillus ferrooxidans-SDS-PAGE706851
47000-Homo sapiens-SDS-PAGE, pulse chase electrophosesis645625
47000-Synechocystis sp.Q55793-661090
47000-Rattus norvegicusQ99P39immunologically from mitochondrial fraction662693
47300-Saccharomyces cerevisiae-deduced molcular mass662257
49720-Rattus norvegicusQ99P39calculated662693
87000-Synechocystis sp.-isoenzyme SsCsd1, gel filtration645621
87500-Azotobacter vinelandii-gel filtration645631
88000-Synechocystis sp.-isoenzyme SsCsd2, gel filtration645621
102000-Saccharomyces cerevisiae-gel filtration662257
140000-Klebsiella pneumoniae-NifU/NifS complex, gel filtration645614
180000200000Saccharomyces cerevisiae-gel filtration661595

SUBUNITS ORGANISM UNIPROT ACCESSION NO. COMMENTARY LITERATURE
dimerBacteria-homodimer645619
dimerSynechocystis sp.-2 * 42000, SDS-PAGE645621
dimerAzotobacter vinelandii-homodimer, 2 * 44000, SDS-PAGE645631
dimerSynechocystis sp.Q55793a large domain that binds pyridoxal-5'-phosphate and a smaller domain with the active site cysteine661090
dimerSaccharomyces cerevisiae-homodimer, gel filtration662257
dimerStreptomyces lividansQ460H9subunit 45000, homodimer 91000, purified soluble DndA protein, gel filtration with a Superose 12 10/30 column672260
dimerEscherichia coli--705872
polymerSaccharomyces cerevisiae-x * 45000, SDS-PAGE, high-molecular-weight complex of Nfs1 and Isd11, gel filtration661595
tetramerKlebsiella pneumoniae-heterotetramer, NifU2NifS2645614
monomerAcidithiobacillus ferrooxidans-1 * 46000, SDS-PAGE and modeling of structure; 46000672753
additional informationSaccharomyces cerevisiae-N-terminal beta-strand of residues 99-104 is essential for the function of Nfs1p662257
additional informationRhodobacter capsulatus-cysteine desulfurase NifS4 interacts with XdhC, but not with xanthine dehydrogenase672277
additional informationHomo sapiens-enzyme forms a complex in vitro with overexpressed cytosolic scaffold protein ISCU674541
additional informationArabidopsis thaliana-enzyme CpNifS forms dynamic complexes with chloroplast protein CpSufE674773
additional informationEscherichia coli-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 assembly674798

POSTTRANSLATIONAL MODIFICATION ORGANISM UNIPROT ACCESSION NO. COMMENTARY LITERATURE
proteolytic modificationSaccharomyces cerevisiae-after lysis of mitochondria with detergents661595

Crystallization/COMMENTARY ORGANISM UNIPROT ACCESSION NO. LITERATURE
modeling of structureAcidithiobacillus ferrooxidans-672753
hanging drop vapor diffusion method, complexed with L-propargylglycineEscherichia coli-645630
-Synechocystis sp.Q55793661090

pH STABILITYpH STABILITY MAXIMUM ORGANISM UNIPROT ACCESSION NO. COMMENTARY LITERATURE
510Acidithiobacillus ferrooxidans-about 45% residual activity at pH 7.5 and 9.5, almost no activity at pH 5.0 and 10.0706851

TEMPERATURE STABILITYTEMPERATURE STABILITY MAXIMUM ORGANISM UNIPROT ACCESSION NO. COMMENTARYLITERATURE
4055Acidithiobacillus ferrooxidans-the enzyme is relatively stable at 40°C with 67% loss of activity, and unstable at temperatures above 55°C706851

GENERAL STABILITYORGANISM UNIPROT ACCESSION NO.LITERATURE
No entries in this field

ORGANIC SOLVENT ORGANISM UNIPROT ACCESSION NO. COMMENTARY LITERATURE
No entries in this field

OXIDATION STABILITY ORGANISM UNIPROT ACCESSION NO. LITERATURE
No entries in this field

STORAGE STABILITY ORGANISM UNIPROT ACCESSION NO. LITERATURE
4°C, purified protein can be stored one month without loss of activityAcidithiobacillus ferrooxidans-672753
at 4°C, 1 month, without significant change of activityAcidithiobacillus ferrooxidans-672753

Purification/COMMENTARY ORGANISM UNIPROT ACCESSION NO. LITERATURE
by one-step affinity chromatography to homogeneityAcidithiobacillus ferrooxidans-672753
Hi-Trap column chromatographyAcidithiobacillus ferrooxidans-706851
-Arabidopsis thaliana-645618
-Azotobacter vinelandii-645631
-Erwinia chrysanthemi-645628
-Escherichia coli-645634, 645635, 674798
copurified with IscUEscherichia coli-645638
DEAE-Toyopearl column chromatography and phenyl-Toyopearl column chromatographyEscherichia coli-704679
purified as the N-terminal His6 fusion proteinEscherichia coli-662209
three homologs: CSD, CsdB and IscSEscherichia coli-645632
-Klebsiella pneumoniae-645614
-Rattus norvegicusQ99P39662693
-Saccharomyces cerevisiae-661595, 662257
to homogeneity with a HiTrap chelating columnStreptomyces lividansQ460H9672260
-Synechocystis sp.-660879, 661090, 661091, 702269
isoenzyme SsCsd1, isoenzyme SsCsd2 and isoenzyme SsCsd3Synechocystis sp.-645621

Cloned/COMMENTARY ORGANISM UNIPROT ACCESSION NO. LITERATURE
; expression in Escherichia coli BL21 (DE3)Acidithiobacillus ferrooxidans-672753
expressed in Escherichia coli BL21(DE3) cellsAcidithiobacillus ferrooxidans-706851
-Arabidopsis thaliana-645618
-Azotobacter vinelandii-645631
expressed in Saccharomyces cerevisiaeCryptosporidium parvumQ8WQX4645639
-Erwinia chrysanthemi-645628
-Escherichia coli-645614, 645634, 645635, 674798
expression in Escherichia coliEscherichia coli-662209
expression in Escherichia coli DH5aEscherichia coli-663375
wild-type and null mutantEscherichia coli-645637
-Homo sapiens-645625
-Klebsiella pneumoniae-645614
expression in HeLa cellMus musculus-675971
-Rattus norvegicusQ99P39662693
expression in Escherichia coli BL21(DE3)Rhodobacter capsulatus-672277
expressed in Escherichia coliRuminococcus flavefaciens-645640
expressiion in Escherichia coliSaccharomyces cerevisiae-662257
; expression in Escherichia coli BL21(DE3) pLysE, expression vector pET15bStreptomyces lividansQ460H9672260
-Synechocystis sp.-645621
expressed in Escherichia coli BL21(DE3) cellsSynechocystis sp.-702269

EXPRESSION ORGANISM UNIPROT ACCESSION NO. 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 IscSEscherichia coli-704679

ENGINEERINGORGANISM UNIPROT ACCESSION NO.COMMENTARYLITERATURE
C325AAzotobacter vinelandii-no cysteine desulfurase activity645636
C369SErwinia chrysanthemi-no enzyme activity645628
C328AEscherichia coli-IscS mutant, activity towards L-cysteine is almost completely abolished, activity toward L-selenocysteine is much less affected645632
C358AEscherichia coli-CSD mutant, activity towards L-cysteine is almost completely abolished, activity toward L-selenocysteine is much less affected645632
C364AEscherichia coli-CsdB mutant, activity towards L-cysteine is almost completely abolished, activity toward L-selenocysteine is much less affected645632
H123AEscherichia coli-decreased specific activity towards L-selenocysteine645630
H55AEscherichia coli-normal activity towards L-selenocysteine and L-cysteine645630
R379AEscherichia coli-significant loss of activity towards L-selenocysteine645630
C327SStreptomyces lividansQ460H9no 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 DndC672260
C326ASynechocystis sp.-inactive,the mutant enzyme is incapable of nucleophilic attack on the sulfur of the substrate L-cysteine702269
C372ASynechocystis sp.Q55793active enzyme via a second pathway661090
additional informationArabidopsis thaliana-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 affected676898
L333AEscherichia coli-mutant defective in Fe-S biosynthesis in vivo but functional in persulfide formation and transfer in vitro662209
additional informationEscherichia coli-deletion of the iscS gene, tRNA from this mutant contains less than 5% of the level of sulfur found in the parent strain645626
additional informationEscherichia coli-deletion of the iscS gene results in a mutant strain that lacks 4-thiouridine in its tRNA645627
S326AEscherichia coli-mutant defective in Fe-S biosynthesis in vivo but functional in persulfide formation and transfer in vitro662209
additional informationHomo sapiens-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 impaired675971
additional informationMus musculusQ9Z1J3depletion 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 form674628
additional informationMus musculus-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 presequence675971
additional informationSaccharomyces cerevisiae-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 complexes675989
additional informationSalmonella enterica-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-methylthioadenosine674271

Renatured/COMMENTARYORGANISM UNIPROT ACCESSION NO.LITERATURE
No entries in this field

APPLICATIONORGANISM UNIPROT ACCESSION NO.COMMENTARYLITERATURE
No entries in this field

DISEASETITLE OF PUBLICATIONLINK TO PUBMED
Anemia, HypochromicChloroplast iron-sulfur cluster protein maturation requires the essential cysteine desulfurase CpNifS. PubMed
Darier DiseaseHistochemical study of oxidative enzymes and cysteine desulfurase in familiar benign chronic pemphigus and Darier's disease. PubMed
PemphigusHistochemical study of oxidative enzymes and cysteine desulfurase in familiar benign chronic pemphigus and Darier's disease. PubMed
Pemphigus, Benign FamilialHistochemical study of oxidative enzymes and cysteine desulfurase in familiar benign chronic pemphigus and Darier's disease. PubMed

REF. AUTHORS TITLE JOURNAL VOL. PAGES YEAR ORGANISMLINK TO PUBMEDSOURCE
645614Kiyasu, T.; Asakura, A.; Nagahashi, Y.; Hoshino, T.Contribution of cysteine desulfurase (NifS protein) to the biotin synthase reaction of Escherichia coliJ. Bacteriol.1822879-28852000Escherichia coli, Klebsiella pneumoniae PubMed
645615Mihara, H.; Esaki, N.Bacterial cysteine desulfurases: their function and mechanismsAppl. Microbiol. Biotechnol.6012-232002Azotobacter vinelandii, Escherichia coli, Haemophilus influenzae, Homo sapiens, Mus musculus, Pseudomonas aeruginosa, Saccharomyces cerevisiae, Synechocystis sp. PubMed
645616Cupp-Vickery, J.R.; Urbina, H.; Vickery, L.E.Crystal structure of IscS, a cysteine desulfurase from Escherichia coliJ. Mol. Biol.3301049-10592003Escherichia coli PubMed
645617Lima, C.D.Analysis of the E. coli NifS CsdB protein at 2.0 A reveals the structural basis for perselenide and persulfide intermediate formationJ. Mol. Biol.3151199-12082002Escherichia coli PubMed
645618Leon, S.; Touraine, B.; Briat, J.F.; Lobreaux, S.The AtNFS2 gene from Arabidopsis thaliana encodes a NifS-like plastidial cysteine desulphuraseBiochem. J.366557-5642002Arabidopsis thaliana PubMed
645619Frazzon, J.; Dean, D.R.Formation of iron-sulfur clusters in bacteria: an emerging field in bioinorganic chemistryCurr. Opin. Chem. Biol.7166-1732003Bacteria PubMed
645620Kambampati, R.; Lauhon, C.T.MnmA and IscS are required for in vitro 2-thiouridine biosynthesis in Escherichia coliBiochemistry421109-11172003Escherichia coli PubMed
645621Kato, S.; Mihara, H.; Kurihara, T.; Yoshimura, T.; Esaki, N.Gene cloning, purification, and characterization of two cyanobacterial NifS homologs driving iron-sulfur cluster formationBiosci. Biotechnol. Biochem.642412-24192000Synechocystis sp. PubMed
645622Kispal, G.; Csere, P.; Prohl, C.; Lill, R.The mitochondrial proteins Atm1p and Nfs1p are essential for biogenesis of cytosolic Fe/S proteinsEMBO J.183981-39891999Saccharomyces cerevisiae PubMed
645624Lacourciere, G.M.; Stadtman, T.C.The NIFS protein can function as a selenide delivery protein in the biosynthesis of selenophosphateJ. Biol. Chem.27330921-309261998Azotobacter vinelandii PubMed
645625Land, T.; Rouault, T.A.Targeting of a human iron-sulfur cluster assembly enzyme, nifs, to different subcellular compartments is regulated through alternative AUG utilizationMol. Cell2807-8151998Homo sapiens PubMed
645626Lauhon, C.T.Requirement for IscS in biosynthesis of all thionucleosides in Escherichia coliJ. Bacteriol.1846820-68292002Escherichia coli PubMed
645627Lauhon, C.T.; Kambampati, R.The iscS gene in Escherichia coli is required for the biosynthesis of 4-thiouridine, thiamin, and NADJ. Biol. Chem.27520096-201032000Escherichia coli PubMed
645628Loiseau, 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 desulfuraseJ. Biol. Chem.27838352-383592003Erwinia chrysanthemi, Escherichia coli PubMed
645630Mihara, 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 selenocysteineJ. Biochem.131679-6852002Escherichia coli PubMed
645631Zheng, L.; White, R.H.; Cash, V.L.; Jack, R.F.; Dean, D.R.Cysteine desulfurase activity indicates a role for NIFS in metallocluster biosynthesisProc. Natl. Acad. Sci. USA902754-27581993Azotobacter vinelandii PubMed
645632Mihara, 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 reactionsJ. Biochem.127559-5672000Escherichia coli PubMed
645633Nilsson, 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 typhimuriumJ. Bacteriol.1846830-68352002Escherichia coli, Salmonella enterica PubMed
645634Outten, 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 coliJ. Biol. Chem.27845713-457192003Escherichia coli PubMed
645635Yang, W.; Rogers, P.A.; Ding, H.Repair of nitric oxide-modified ferredoxin [2Fe-2S] cluster by cysteine desulfurase (IscS)J. Biol. Chem.27712868-128732002Escherichia coli PubMed
645636Zheng, L.; White, R.H.; Cash, V.L.; Dean, D.R.Mechanism for the desulfurization of L-cysteine catalyzed by the nifS gene productBiochemistry334714-47201994Azotobacter vinelandii PubMed
645637Schwartz, 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 coliProc. Natl. Acad. Sci. USA979009-90142000Escherichia coli PubMed
645638Kurihara, T.; Mihara, H.; Kato, S.; Yoshimura, T.; Esaki, N.Assembly of iron-sulfur clusters mediated by cysteine desulfurases, IscS, CsdB and CSD, from Escherichia coliBiochim. Biophys. Acta1647303-3092003Escherichia coli PubMed
645639LaGier, M.J.; Tachezy, J.; Stejskal, F.; Kutisova, K.; Keithly, J.S.Mitochondrial-type iron-sulfur cluster biosynthesis genes (IscS and IscU) in the apicomplexan Cryptosporidium parvumMicrobiology1493519-35302003Cryptosporidium parvum PubMed
645640Kirby, J.; Wright, F.; Flint, H.J.A cysteine desulphurase gene from the cellulolytic rumen anaerobe Ruminococcus flavefaciensBiochim. Biophys. Acta1368233-2371998Ruminococcus flavefaciens-
660879Kessler, D.Slr0077 of Synechocystis has cysteine desulfurase as well as cystine lyase activityBiochem. Biophys. Res. Commun.320571-5772004Synechocystis sp. PubMed
661090Tirupati, B.; Vey, J.L.; Drennan, C.L.; Bollinger, J.M.jr.Kinetic and structural characterization of Slr0077/SufS, the essential cysteine desulfurase from Synechocystis sp. PCC 6803Biochemistry4312210-122192004Synechocystis sp. PubMed
661091Behshad, E.; Parkin, S.E.; Bollinger, J.M.jr.Mechanism of cysteine desulfurase Slr0387 from Synechocystis sp. PCC 6803: Kinetic analysis of cleavage of the persulfide intermediate by chemical reductantsBiochemistry4312220-122262004Synechocystis sp. PubMed
661595Adam, A.C.; Bornhövd, C.; Prokisch, H.; Neupert, W.; Hell, K.the Nfs1 interacting protein Isd11 has an essential role in Fe/S cluster biogenesis in mitochondriaEMBO J.25174-1832006Saccharomyces cerevisiae PubMed
661771Forlani, F.; Cereda, A.; Freuer, A.; Nimtz, M.; Leimkühler, S.; Pagani, S.The cysteine-desulfurase IscS promotes the production of the rhodanese RhdA in the persulfurated formFEBS Lett.5796786-67902005Escherichia coli PubMed
662190Nakai, Y.; Umeda, N.; Suzuki, T.; Nakai, M.; Hayashi, H.; Watanabe, K.; Kagamiyama, H.Yeast Nfs1p is involved in thio-modification of both mitochondrial and cytoplasmic tRNAsJ. Biol. Chem.27912363-123682004Saccharomyces cerevisiae PubMed
662209Lauhon, 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 vivoJ. Biol. Chem.27919551-195582004Escherichia coli PubMed
662257Muhlenhoff, U.; Balk, J.; Richhardt, N.; Kaiser, J.T.; Sipos, K.; Kispal, G.; Lill, R.Functional characterization of the eukaryotic cysteine desulfurase Nfs1p from Saccharomyces cerevisiaeJ. Biol. Chem.27936906-369152004Saccharomyces cerevisiae PubMed
662693Liew, Y.F.; Shaw, N.S.Mitochondrial cysteine desulfurase iron-sulfur cluster S and aconitase are post-transcriptionally regulated by dietary iron in skeletal muscle of ratsJ. Nutr.1352151-21582005Rattus norvegicus PubMed
663375Rojas, D.M.; Vasquez, C.C.Sensitivity to potassium tellurite of Escherichia coli cells deficient in CSD, CsdB and IscS cysteine desulfurasesRes. Microbiol.156465-4712005Escherichia coli PubMed
671626Canal, F.; Fosset, C.; Chauveau, M.J.; Drapier, J.C.; Bouton, C.Regulation of the cysteine desulfurase Nfs1 and the scaffold protein IscU in macrophages stimulated with interferon-gamma and lipopolysaccharideArch. Biochem. Biophys.465282-2922007Mus musculus PubMed
672260You, D.; Wang, L.; Yao, F.; Zhou, X.; Deng, Z.A novel DNA modification by sulfur: DndA is a NifS-like cysteine desulfurase capable of assembling DndC as an iron-sulfur cluster protein in Streptomyces lividansBiochemistry466126-61332007Streptomyces lividans PubMed
672277Neumann, M.; Stoecklein, W.; Walburger, A.; Magalon, A.; Leimkuehler, S.Identification of a Rhodobacter capsulatus L-cysteine desulfurase that sulfurates the molybdenum cofactor when bound to XdhC and before its insertion into xanthine dehydrogenaseBiochemistry469586-95952007Rhodobacter capsulatus PubMed
672753Zeng, J.; Zhang, Y.; Liu, Y.; Zhang, X.; Xia, L.; Liu, J.; Qiu, G.Expression, purification and characterization of a cysteine desulfurase, IscS, from Acidithiobacillus ferrooxidansBiotechnol. Lett.291983-19902007Acidithiobacillus ferrooxidans PubMed
674271Lundgren, H.K.; Bjoerk, G.R.Structural alterations of the cysteine desulfurase IscS of Salmonella enterica serovar Typhimurium reveal substrate specificity of IscS in tRNA thiolationJ. Bacteriol.1883052-30622006Salmonella enterica PubMed
674541Li, K.; Tong, W.H.; Hughes, R.M.; Rouault, T.A.Roles of the mammalian cytosolic cysteine desulfurase, ISCS, and scaffold protein, ISCU, in iron-sulfur cluster assemblyJ. Biol. Chem.28112344-123512006Homo sapiens PubMed
674628Fosset, C.; Chauveau, M.J.; Guillon, B.; Canal, F.; Drapier, J.C.; Bouton, C.RNA silencing of mitochondrial m-Nfs1 reduces Fe-S enzyme activity both in mitochondria and cytosol of mammalian cellsJ. Biol. Chem.28125398-254062006Mus musculus PubMed
674773Ye, H.; Abdel-Ghany, S.E.; Anderson, T.D.; Pilon-Smits, E.A.; Pilon, M.CpSufE activates the cysteine desulfurase CpNifS for chloroplastic Fe-S cluster formationJ. Biol. Chem.2818958-89692006Arabidopsis thaliana PubMed
674798Layer, 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 assemblyJ. Biol. Chem.28213342-133502007Escherichia coli PubMed
674877Zhao, D.; Curatti, L.; Rubio, L.M.Evidence for nifU and nifS participation in the biosynthesis of the iron-molybdenum cofactor of nitrogenaseJ. Biol. Chem.28237016-370252007Klebsiella pneumoniae PubMed
675971Biederbick, A.; Stehling, O.; Roesser, R.; Niggemeyer, B.; Nakai, Y.; Elsaesser, H.P.; Lill, R.Role of human mitochondrial Nfs1 in cytosolic iron-sulfur protein biogenesis and iron regulationMol. Cell. Biol.265675-56872006Homo sapiens, Mus musculus PubMed
675989Onder, O.; Yoon, H.; Naumann, B.; Hippler, M.; Dancis, A.; Daldal, F.Modifications of the lipoamide-containing mitochondrial subproteome in a yeast mutant defective in cysteine desulfuraseMol. Cell. Proteomics51426-14362006Saccharomyces cerevisiae PubMed
676898Van Hoewyk, D.; Abdel-Ghany, S.E.; Cohu, C.M.; Herbert, S.K.; Kugrens, P.; Pilon, M.; Pilon-Smits, E.A.Chloroplast iron-sulfur cluster protein maturation requires the essential cysteine desulfurase CpNifSProc. Natl. Acad. Sci. USA1045686-56912007Arabidopsis thaliana PubMed
690737Mihara, H.; Hidese, R.; Yamane, M.; Kurihara, T.; Esaki, N.The iscS gene deficiency affects the expression of pyrimidine metabolism genesBiochem. Biophys. Res. Commun.372407-4112008Escherichia coli PubMed
690744Wu, G.; Li, P.; Wu, X.Regulation of Escherichia coli IscS desulfurase activity by ferrous iron and cysteineBiochem. Biophys. Res. Commun.374399-4042008Escherichia coli PubMed
692336Sendra, 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 SUFAFEBS Lett.5811362-13682007Escherichia coli PubMed
702269Behshad, E.; Bollinger, J.M.Kinetic analysis of cysteine desulfurase CD0387 from Synechocystis sp. PCC 6803: formation of the persulfide intermediateBiochemistry4812014-120232009Synechocystis sp. PubMed
703682Poliak, P.; Van Hoewyk, D.; Obornik, M.; Zikova, A.; Stuart, K.D.; Tachezy, J.; Pilon, M.; Lukes, J.Functions and cellular localization of cysteine desulfurase and selenocysteine lyase in Trypanosoma bruceiFEBS J.277383-3932010Trypanosoma brucei PubMed
704679Zhang, 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 coliJ. Biol. Chem.2852302-23082010Escherichia coli PubMed
705872Adinolfi, 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 IscSNat. Struct. Mol. Biol.16390-3962009Escherichia coli PubMed
706851WU, A.; ZHANG, Y.; ZHENG, C.; DAI, Y.; LIU, Y.; ZENG, J.; GU, G.; LIU, J.Purification and enzymatic characteristics of cysteine desulfurase, IscS, in Acidithiobacillus ferrooxidans ATCC 23270Trans. Nonferrous Met. Soc. China181450-14572008Acidithiobacillus ferrooxidans-

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