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L-cysteine
L-alanine + H2S
L-cysteine
L-alanine + sulfide
L-cysteine
L-alanine + sulfur
DndA is able to directly activate apo-Fe DndC for its reconstitution as a fully functional [4Fe-4S] cluster protein (DndC) with unambiguously demonstrated ATP pyrophosphatase activity
-
-
?
L-cysteine + ?
?
-
in the presence of cysteine, IscSs ability to bind iron improves significantly
-
-
?
L-cysteine + ?
L-alanine + ?
-
catalyzes the elimination of S from L-cysteine to yield L-alanine and elemental sulfur or H2S, depending on whether or not a reducing agent is added to the reaction mixture, provides sulfur for the assembly of ironsulfur cluster
-
-
?
L-cysteine + acceptor
L-alanine + S-sulfanyl-acceptor
L-cysteine + acceptor
L-alanine + sulfide + ?
L-cysteine + c-ISCS
L-alanine + c-ISCS-SSH
-
-
-
-
?
L-cysteine + c-IscU
L-alanine + c-IscU-SSH
-
-
-
-
?
L-cysteine + CpNifS
L-alanine + CpNifS-SSH
-
-
-
-
?
L-cysteine + DndA
L-alanine + DndA-SSH
-
-
-
?
L-cysteine + enzyme-cysteine
L-alanine + enzyme-S-sulfanylcysteine
L-cysteine + IscS
L-alanine + IscS-SSH
L-cysteine + MOC3 protein
L-alanine + S-sulfanyl-MOC3 protein
-
-
-
-
?
L-cysteine + N,N-dimethyl-4-phenylenediamine
L-alanine + N,N-dimethyl-4-phenylenediamine sulfate
-
-
-
-
?
L-cysteine + RhdA
L-alanine + RhdA-SSH
L-cysteine + Slr0077
L-alanine + Slr0077-SSH
-
-
-
-
?
L-cysteine + SufE
L-alanine + S-sulfanyl-SufE
-
-
-
-
?
L-cysteine + SufE
L-alanine + SufE-SSH
-
-
-
?
L-cysteine + SufS
L-alanine + SufS-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 + [SufU]-cysteine
L-alanine + [SufU]-S-sulfanylcysteine
L-cysteine + [ThiI]-cysteine
L-alanine + [ThiI]-S-sulfanylcysteine
-
-
-
-
?
L-cysteine sulfinic acid
L-alanine + sulfite
L-cysteine sulfinic acid + ?
?
cysteine desulfurase DndA catalyzes iron-sulfur cluster assembly by activation of apo-Fe DndC protein
-
-
?
L-cysteine sulfinic acid + DndA
?
-
-
-
?
L-cystine + Slr0077
pyruvate + Slr0077-SSH
-
cystine lyase of Slr0077
-
-
?
L-selenocysteine
L-alanine + selenium
L-selenocysteine + ?
?
-
-
-
?
L-selenocysteine + DndA
L-alanine + DndA-SSeH
-
-
-
?
L-selenocystine
?
-
-
-
-
?
additional information
?
-
L-cysteine
L-alanine + H2S
-
-
or formation of elemental sulfur, depending of presence of a reducing agent in the reaction mixture
-
?
L-cysteine
L-alanine + H2S
-
-
-
?
L-cysteine
L-alanine + sulfide
-
unlike other cysteine desulfurases the L-cysteine C-S-lyase from Synechocystis does not have a conserved cysteine residue at the active site
-
?
L-cysteine
L-alanine + sulfide
-
unlike other cysteine desulfurases the L-cysteine C-S-lyase from Synechocystis does not have a conserved cysteine residue at the active site
-
?
L-cysteine + acceptor
L-alanine + S-sulfanyl-acceptor
-
-
-
-
?
L-cysteine + acceptor
L-alanine + S-sulfanyl-acceptor
-
-
-
?
L-cysteine + acceptor
L-alanine + S-sulfanyl-acceptor
-
-
-
?
L-cysteine + acceptor
L-alanine + S-sulfanyl-acceptor
-
overall reaction
-
-
?
L-cysteine + acceptor
L-alanine + S-sulfanyl-acceptor
-
-
-
?
L-cysteine + acceptor
L-alanine + S-sulfanyl-acceptor
overall reaction
-
-
?
L-cysteine + acceptor
L-alanine + S-sulfanyl-acceptor
-
-
-
-
?
L-cysteine + acceptor
L-alanine + S-sulfanyl-acceptor
-
-
-
-
?
L-cysteine + acceptor
L-alanine + S-sulfanyl-acceptor
-
-
-
-
?
L-cysteine + acceptor
L-alanine + S-sulfanyl-acceptor
-
-
-
-
?
L-cysteine + acceptor
L-alanine + S-sulfanyl-acceptor
-
-
-
-
?
L-cysteine + acceptor
L-alanine + S-sulfanyl-acceptor
-
-
-
-
?
L-cysteine + acceptor
L-alanine + S-sulfanyl-acceptor
-
-
-
-
?
L-cysteine + acceptor
L-alanine + S-sulfanyl-acceptor
-
-
-
-
?
L-cysteine + acceptor
L-alanine + sulfide + ?
overall reaction, the enzyme shows a selenocysteine lyase activity approximately 280fold higher than its cysteine desulfurase activity. The desulfuration mechanism proposed for this enzyme seems to involve three different stages. At the beginning of the reaction, L-cysteine is quickly bound by the cofactor pyridoxal 5'-phosphate, shifting the UV-VIS spectrum of the enzyme. In this aldimine state, the L-cysteine sulfur atom is attacked by Cys384, resulting in persulfide formation. To regenerate the enzyme, this persulfide state must be resolved by transferring the sulphide to inorganic or organic acceptor molecules (accessory proteins, DTT or to other L-cysteine molecules)
-
-
?
L-cysteine + acceptor
L-alanine + sulfide + ?
overall reaction, the enzyme shows a selenocysteine lyase activity approximately 280fold higher than its cysteine desulfurase activity. The desulfuration mechanism proposed for this enzyme seems to involve three different stages. At the beginning of the reaction, L-cysteine is quickly bound by the cofactor pyridoxal 5'-phosphate, shifting the UV-VIS spectrum of the enzyme. In this aldimine state, the L-cysteine sulfur atom is attacked by Cys384, resulting in persulfide formation. To regenerate the enzyme, this persulfide state must be resolved by transferring the sulphide to inorganic or organic acceptor molecules (accessory proteins, DTT or to other L-cysteine molecules)
-
-
?
L-cysteine + enzyme-cysteine
L-alanine + enzyme-S-sulfanylcysteine
-
-
-
-
?
L-cysteine + enzyme-cysteine
L-alanine + enzyme-S-sulfanylcysteine
-
involved in the formation of Fe-S proteins
-
-
?
L-cysteine + IscS
L-alanine + IscS-SSH
-
-
-
-
?
L-cysteine + IscS
L-alanine + IscS-SSH
-
-
-
-
?
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 + SufS
L-alanine + SufS-SSH
-
-
-
-
?
L-cysteine + SufS
L-alanine + SufS-SSH
-
-
-
?
L-cysteine + [enzyme]-cysteine
L-alanine + [enzyme]-S-sulfanylcysteine
-
IscS has a high affinity for L-cysteine
-
-
?
L-cysteine + [enzyme]-cysteine
L-alanine + [enzyme]-S-sulfanylcysteine
-
-
-
?
L-cysteine + [enzyme]-cysteine
L-alanine + [enzyme]-S-sulfanylcysteine
-
-
-
-
?
L-cysteine + [enzyme]-cysteine
L-alanine + [enzyme]-S-sulfanylcysteine
-
-
-
?
L-cysteine + [enzyme]-cysteine
L-alanine + [enzyme]-S-sulfanylcysteine
-
-
-
?
L-cysteine + [enzyme]-cysteine
L-alanine + [enzyme]-S-sulfanylcysteine
-
-
-
-
?
L-cysteine + [enzyme]-cysteine
L-alanine + [enzyme]-S-sulfanylcysteine
-
catalyzes the conversion of cysteine to alanine and sulfane sulfur via the formation of a protein-bound cysteine persulfide intermediate on a conserved cysteine residue
-
-
?
L-cysteine + [enzyme]-cysteine
L-alanine + [enzyme]-S-sulfanylcysteine
-
intermediate is an enzyme-bound cysteinyl persulfide
-
-
?
L-cysteine + [enzyme]-cysteine
L-alanine + [enzyme]-S-sulfanylcysteine
-
-
-
-
?
L-cysteine + [enzyme]-cysteine
L-alanine + [enzyme]-S-sulfanylcysteine
-
-
-
-
?
L-cysteine + [enzyme]-cysteine
L-alanine + [enzyme]-S-sulfanylcysteine
-
-
-
-
?
L-cysteine + [enzyme]-cysteine
L-alanine + [enzyme]-S-sulfanylcysteine
-
-
-
-
?
L-cysteine + [enzyme]-cysteine
L-alanine + [enzyme]-S-sulfanylcysteine
-
-
-
?
L-cysteine + [enzyme]-cysteine
L-alanine + [enzyme]-S-sulfanylcysteine
-
-
-
-
?
L-cysteine + [enzyme]-cysteine
L-alanine + [enzyme]-S-sulfanylcysteine
-
-
-
?
L-cysteine + [enzyme]-cysteine
L-alanine + [enzyme]-S-sulfanylcysteine
-
-
-
-
?
L-cysteine + [enzyme]-cysteine
L-alanine + [enzyme]-S-sulfanylcysteine
-
-
?
L-cysteine + [enzyme]-cysteine
L-alanine + [enzyme]-S-sulfanylcysteine
-
iscS has cysteine desulfurase activity and mobilizes sulfur from cysteine for the repair of the [4Fe-4S] cluster in apo-dihydroxyacid dehydratase
-
-
?
L-cysteine + [enzyme]-cysteine
L-alanine + [enzyme]-S-sulfanylcysteine
-
Cys364 residue is essential for activity toward L-cysteine but not toward L-selenocyteine
-
-
?
L-cysteine + [enzyme]-cysteine
L-alanine + [enzyme]-S-sulfanylcysteine
-
IscS transfers the sulfur atom from L-cysteine to the C-terminal thiocarboxylate of the MoaD subunit in vitro
-
-
?
L-cysteine + [enzyme]-cysteine
L-alanine + [enzyme]-S-sulfanylcysteine
-
-
-
?
L-cysteine + [enzyme]-cysteine
L-alanine + [enzyme]-S-sulfanylcysteine
-
-
-
-
?
L-cysteine + [enzyme]-cysteine
L-alanine + [enzyme]-S-sulfanylcysteine
-
-
-
-
?
L-cysteine + [enzyme]-cysteine
L-alanine + [enzyme]-S-sulfanylcysteine
-
-
-
-
?
L-cysteine + [enzyme]-cysteine
L-alanine + [enzyme]-S-sulfanylcysteine
-
-
-
-
?
L-cysteine + [enzyme]-cysteine
L-alanine + [enzyme]-S-sulfanylcysteine
-
-
-
-
?
L-cysteine + [enzyme]-cysteine
L-alanine + [enzyme]-S-sulfanylcysteine
-
-
-
-
?
L-cysteine + [enzyme]-cysteine
L-alanine + [enzyme]-S-sulfanylcysteine
-
-
-
?
L-cysteine + [enzyme]-cysteine
L-alanine + [enzyme]-S-sulfanylcysteine
-
-
-
-
?
L-cysteine + [enzyme]-cysteine
L-alanine + [enzyme]-S-sulfanylcysteine
-
L-cysteine desulfuration requires a cysteine residue at the active site of the enzyme, but decomposition of L-selenocysteine and L-cysteine sufinic acid do not
-
-
?
L-cysteine + [enzyme]-cysteine
L-alanine + [enzyme]-S-sulfanylcysteine
-
-
-
-
?
L-cysteine + [enzyme]-cysteine
L-alanine + [enzyme]-S-sulfanylcysteine
-
-
-
?
L-cysteine + [SufU]-cysteine
L-alanine + [SufU]-S-sulfanylcysteine
-
-
-
-
?
L-cysteine + [SufU]-cysteine
L-alanine + [SufU]-S-sulfanylcysteine
-
the enzyme is able to reconstitute an Fe/S cluster on SufU
-
-
?
L-cysteine + [SufU]-cysteine
L-alanine + [SufU]-S-sulfanylcysteine
-
-
-
-
?
L-cysteine sulfinic acid
L-alanine + sulfite
-
-
-
-
?
L-cysteine sulfinic acid
L-alanine + sulfite
-
L-cysteine desulfuration requires a cysteine residue at the active site of the enzyme, but decomposition of L-selenocysteine and L-cysteine sufinic acid do not
-
?
L-selenocysteine
L-alanine + selenium
-
-
-
-
?
L-selenocysteine
L-alanine + selenium
-
-
-
-
?
L-selenocysteine
L-alanine + selenium
-
-
-
?
L-selenocysteine
L-alanine + selenium
-
-
-
-
?
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
-
-
?
L-selenocysteine
L-alanine + selenium
-
-
-
-
?
L-selenocysteine
L-alanine + selenium
-
-
-
-
?
L-selenocysteine
L-alanine + selenium
-
L-cysteine desulfuration requires a cysteine residue at the active site of the enzyme, but decomposition of L-selenocysteine and L-cysteine sufinic acid do not
-
-
?
L-selenocysteine
L-alanine + selenium
-
-
-
-
?
additional information
?
-
-
enzyme is involved in the iron-sulfur cluster assembly
-
-
?
additional information
?
-
-
enzyme catalyzes the formation of Fe-S clusters in a component protein of nitrogenase in the presence of cysteine and ferrous iron in vitro
-
-
?
additional information
?
-
-
enzyme is involved in selenoprotein biosynthesis
-
-
?
additional information
?
-
-
enzyme serves as a selenide delivery protein for the in vitro biosynthesis of selenophosphate
-
-
?
additional information
?
-
-
involved in the mobilization of iron or sulfur required for metallocluster formation
-
-
?
additional information
?
-
-
enzyme participates in the biosynthesis of the nitrogenase metalloclusters by providing the inorganic sulfur required for Fe-S core formation
-
-
?
additional information
?
-
-
NifS specifically mobilizes sulfur for the iron-sulfur (Fe-S) cluster maturation of nitrogenase
-
-
?
additional information
?
-
functions as scaffold for the assembly of [Fe-S] prior to their incorporation into apoproteins
-
-
?
additional information
?
-
-
functions as scaffold for the assembly of [Fe-S] prior to their incorporation into apoproteins
-
-
?
additional information
?
-
-
provides sulfur for [Fe-S] cluster synthesis via its cysteine desulfurase activity for the following enzymes: NADH dehydrogenase, succinate dehydrogenase, glutamate synthase, aconitase B, 6-phophogluconate dehydratase, fumarase A, isocitrate dehydrogenase
-
-
?
additional information
?
-
-
isc genes are involved in the formation of Fe-S clusters in various Fe-S proteins
-
-
?
additional information
?
-
-
enzyme is involved in selenoprotein biosynthesis
-
-
?
additional information
?
-
-
IscS plays a significant and specific role at the top of a potentially broad sulfur transfer cascade that is required for the biosynthesis of thiamine, NAD, [Fe-S] clusters and thionucleosides
-
-
?
additional information
?
-
-
acts as sulfurtransferase in biosynthesis of 4-thiouridine in tRNA
-
-
?
additional information
?
-
-
enzyme contributes to the biotin synthase reaction, probably by supplying sulfur to the BioB protein
-
-
?
additional information
?
-
-
facilitates the formation of the iron-sulfur cluster of ferredoxin in vitro
-
-
?
additional information
?
-
involved in biosynthesis of 2-thiouridine
-
-
?
additional information
?
-
-
involved in biosynthesis of 2-thiouridine
-
-
?
additional information
?
-
-
involved in biosynthesis of thionucleosides
-
-
?
additional information
?
-
-
involved in biosynthesis of thionucleosides
-
-
?
additional information
?
-
-
involved in thiamine biosynthesis, molybdopterin biosynthesis and tRNA modification
-
-
?
additional information
?
-
-
cysteine desulfurase together with L-cysteine can efficiently repair the nitric oxide-modified ferredoxin [2Fe-2S] cluster and the iron center in the dinitroxyl iron complex may be recycled for the reassembly of iron-sulfur clusters in proteins
-
-
?
additional information
?
-
-
SufA is able to bind sulfur atoms provided by the SufS-SufE complex
-
-
?
additional information
?
-
-
SufS and SufE proteins interact with the SufBCD protein complex to facilitate sulfur liberation from cysteine and donation for Fe-S cluster assembly
-
-
?
additional information
?
-
-
uridine phosphorylase (UPase) and cytidine deaminase (CDA) are significantly down-regulated in the iscS mutant, the expression level of the protein complex YeiT-YeiA is decreased in the iscS mutant, iscS plays an essential role in the expression of pyrimidine metabolism genes and provides a clue to the potential relationship between iscS and global gene regulation
-
-
?
additional information
?
-
-
IscS is involved in the sulfuration of MoaD subunit
-
-
?
additional information
?
-
-
[2Fe-2S]-ferredoxin interacts directly with the enzyme
-
-
?
additional information
?
-
-
IscS is essential for Fe-S cluster assembly in vivo
-
-
?
additional information
?
-
-
the enzyme is capable of donating the persulfide sulfur atoms to a variety of biosynthetic pathways for sulfur-containing biofactors, such as iron-sulfur clusters, thiamin, transfer RNA thionucleosides, biotin, and lipoic acid
-
-
?
additional information
?
-
-
IscS plays a significant and specific role at the top of a potentially broad sulfur transfer cascade that is required for the biosynthesis of thiamine, NAD, [Fe-S] clusters and thionucleosides
-
-
?
additional information
?
-
-
acts as sulfurtransferase in biosynthesis of 4-thiouridine in tRNA
-
-
?
additional information
?
-
-
isc genes are involved in the formation of Fe-S clusters in various Fe-S proteins
-
-
?
additional information
?
-
the enzyme is involved in Fe-S cluster assembly in haloarchaea
-
-
?
additional information
?
-
-
the enzyme is involved in Fe-S cluster assembly in haloarchaea
-
-
?
additional information
?
-
the enzyme is involved in Fe-S cluster assembly in haloarchaea
-
-
?
additional information
?
-
-
NFS1 acts as the sulfur donor for the C-terminal domain of MOCS3 protein (a cytosolic protein involved in molybdenum cofactor biosynthesis and tRNA thiolation)
-
-
?
additional information
?
-
-
enzyme participates in biotin synthase reaction, probably by supplying sulfur to the iron-sulfur cluster of biotin synthase
-
-
?
additional information
?
-
-
cysteine desulfurase participates in the biosynthesis of the iron-molybdenum cofactor of nitrogenase as the major provider of Fe-S clusters, but it is not essential to synthesize active nitrogenase
-
-
?
additional information
?
-
-
enzyme participates in biotin synthase reaction, probably by supplying sulfur to the iron-sulfur cluster of biotin synthase
-
-
?
additional information
?
-
-
the enzyme Lecsl has both cysteine sulfoxide lyase and cysteine desulfurase activity
-
-
?
additional information
?
-
-
HapE is a bifunctional enzyme which has both the cysteine desulfurase activity to produce alanine and the cysteine desulfhydrase activity to produce pyruvate and hydrogen sulfide
-
-
?
additional information
?
-
-
isc genes are involved in the formation of Fe-S clusters in various Fe-S proteins
-
-
?
additional information
?
-
-
enzyme NifS4 is involved in formation of the Mo-S ligand of Moco. It mobilizes sulfur by formation of a protein-bound persulfide intermediate and transfers this sulfur further to Moco. Moco is sulfurated before the insertion into xanthine dehydrogenase, while it is bound to XdhC
-
-
?
additional information
?
-
-
NifS4 is involved in the formation of the Mo=S ligand of molybdenum cofactor. NifS4 mobilizes sulfur from L-cysteine by formation of a protein-bound persulfide intermediate and transfers this sulfur further to molybdenum cofactor. Molybdenum cofactor is sulfurated before the insertion into XDH, while it is bound to XdhC
-
-
?
additional information
?
-
-
involved in the production of sulfur for the mormation of iron-sulfur clusters
-
-
?
additional information
?
-
-
-
-
-
?
additional information
?
-
-
enzyme is required for synthesis of both mitochondrial and cytosolic Fe/S proteins, biosynthesis of Fe/S clusters is initiated in the mitochondrial matrix by the cysteine desulfurase Nfs1p, which provides elemental sulfur for biogenesis
-
-
?
additional information
?
-
-
cysteine desulfurase is required for the proper post-translational modification of the lipoamide-containing mitochondrial subproteome in yeast
-
-
?
additional information
?
-
-
Nfs1 mediates assembly of the Fe-S cluster of both mitochondrial and cytosolic Fe-S proteins in the mitochondrial Fe-S assembly system
-
-
?
additional information
?
-
-
involved in biosynthesis of thionucleosides
-
-
?
additional information
?
-
-
the synthesis of 4-thiouridine and 5-methylaminomethyl-2-thiouridine occurs by a transfer of sulfur from enzyme IscS via various proteins to the target nucleoside in the tRNA, and no iron-sulfur cluster protein participates, whereas the synthesis of 2-thiocytidine and N6-(4-hydroxyisopentenyl)-2-methylthioadenosine is dependent on iron-sulfur cluster proteins, whose formation and maintenance depend on IscS
-
-
?
additional information
?
-
-
cysteine desulfurase DndA catalyzes iron-sulfur cluster assembly by activation of apo-Fe DndC protein
-
-
?
additional information
?
-
cysteine desulfurase DndA catalyzes iron-sulfur cluster assembly by activation of apo-Fe DndC protein
-
-
?
additional information
?
-
-
no substrate: L-cystine, L-selenocystine
-
-
?
additional information
?
-
no substrate: L-cystine, L-selenocystine
-
-
?
additional information
?
-
-
substrate specificity similar to that of Escherichia coli IscS
-
-
?
additional information
?
-
substrate specificity similar to that of Escherichia coli IscS
-
-
?
additional information
?
-
-
no substrates are L-cystine, L-selenocystine
-
-
?
additional information
?
-
no substrates are L-cystine, L-selenocystine
-
-
?
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Sulfobacillus acidophilus, Sulfobacillus acidophilus TPY
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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
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291-301
2020
Escherichia coli (P77444), Escherichia coli
brenda
Ho, T.; Huynh, K.; Nguyen, D.; Park, H.; Jung, K.; Sur, B.; Ahn, Y.; Cha, S.; Kang, L.
Catalytic intermediate crystal structures of cysteine desulfurase from the archaeon Thermococcus onnurineus NA1
Archaea
2017
5395293
2017
Thermococcus onnurineus (B6YT87)
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Banerjee, M.; Chakravarty, D.; Ballal, A.
Molecular basis of function and the unusual antioxidant activity of a cyanobacterial cysteine desulfurase
Biochem. J.
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2017
Nostoc sp. PCC 7120 = FACHB-418 (Q8YU59)
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Cai, K.; Tonelli, M.; Frederick, R.O.; Markley, J.L.
Human mitochondrial ferredoxin 1 (FDX1) and ferredoxin 2 (FDX2) both bind cysteine desulfurase and donate electrons for iron-sulfur cluster biosynthesis
Biochemistry
56
487-499
2017
Homo sapiens (Q9Y697), Homo sapiens
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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
Nakamura, R.; Hikita, M.; Ogawa, S.; Takahashi, Y.; Fujishiro, T.
Snapshots of PLP-substrate and PLP-product external aldimines as intermediates in two types of cysteine desulfurase enzymes
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2020
Helicobacter pylori (O25008), Bacillus subtilis (O32164), Bacillus subtilis 168 (O32164), Helicobacter pylori ATCC 700392 (O25008)
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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.
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2357
2019
Escherichia coli
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Giordano, N.; Hastie, J.; Smith, A.; Foss, E.; Gutierrez-Munoz, D.; Carlson, P.J.
Cysteine desulfurase IscS2 plays a role in oxygen resistance in Clostridium difficile
Infect. Immun.
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2018
Clostridioides difficile (Q18BE4), Clostridioides difficile, Clostridioides difficile 630 (Q18BE4)
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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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Wen, Y.; Chen, Y.; Li, L.; Xu, M.; Tan, Y.; Li, Y.; Wang, C.; Chen, Q.; Kuang, X.; Wu, Y.
Localization and characterization of a putative cysteine desulfurase in Chlamydia psittaci
J. Cell. Biochem.
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4409-4422
2019
Chlamydia psittaci
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Liu, L.; Jiang, S.; Xing, M.; Chen, C.; Lai, C.; Li, N.; Liu, G.; Wu, D.; Gao, H.; Hong, L.; Tan, P.; Chen, S.; Deng, Z.; Wu, G.; Wang, L.
Structural analysis of an L-cysteine desulfurase from an Ssp DNA phosphorothioation system
mBio
11
e00488
2020
Vibrio cyclitrophicus
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Cory, S.A.; Van Vranken, J.G.; Brignole, E.J.; Patra, S.; Winge, D.R.; Drennan, C.L.; Rutter, J.; Barondeau, D.P.
Structure of human Fe-S assembly subcomplex reveals unexpected cysteine desulfurase architecture and acyl-ACP-ISD11 interactions
Proc. Natl. Acad. Sci. USA
114
E5325-E5334
2017
Homo sapiens (Q9Y697), Homo sapiens
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