Information on EC 2.8.1.7 - cysteine desulfurase

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The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea

EC NUMBER
COMMENTARY hide
2.8.1.7
-
RECOMMENDED NAME
GeneOntology No.
cysteine desulfurase
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
L-cysteine + acceptor = L-alanine + S-sulfanyl-acceptor
show the reaction diagram
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 TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
sulfur atom transfer
PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
L-alanine biosynthesis III
-
-
molybdenum cofactor biosynthesis
-
-
thiazole biosynthesis I (facultative anaerobic bacteria)
-
-
thiazole biosynthesis II (aerobic bacteria)
-
-
tRNA-uridine 2-thiolation (bacteria)
-
-
tRNA-uridine 2-thiolation (cytoplasmic)
-
-
tRNA-uridine 2-thiolation (mammalian mitochondria)
-
-
tRNA-uridine 2-thiolation (thermophilic bacteria)
-
-
tRNA-uridine 2-thiolation (yeast mitochondria)
-
-
[2Fe-2S] iron-sulfur cluster biosynthesis
-
-
alanine metabolism
-
-
molybdenum cofactor biosynthesis
-
-
vitamin B1 metabolism
-
-
Thiamine metabolism
-
-
Metabolic pathways
-
-
SYSTEMATIC NAME
IUBMB Comments
L-cysteine:acceptor sulfurtransferase
A pyridoxal-phosphate protein. The sulfur from free L-cysteine is first transferred to a cysteine residue in the active site, and then passed on to various other acceptors. The enzyme is involved in the biosynthesis of iron-sulfur clusters, thio-nucleosides in tRNA, thiamine, biotin, lipoate and pyranopterin (molybdopterin) [2]. In Azotobacter vinelandii, this sulfur provides the inorganic sulfide required for nitrogenous metallocluster formation [1].
CAS REGISTRY NUMBER
COMMENTARY hide
149371-08-4
-
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
-
-
Manually annotated by BRENDA team
-
SwissProt
Manually annotated by BRENDA team
strain DH5a and mutant desulfurase deficient strains csdA::Kn, csdB::Kn, ascS::Kn
-
-
Manually annotated by BRENDA team
TG1
-
-
Manually annotated by BRENDA team
-
SwissProt
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
weanling male wistar
SwissProt
Manually annotated by BRENDA team
; expression in Escherichia coli BL21(DE3)
-
-
Manually annotated by BRENDA team
YPH499as WT, GAL10-ISD11 as Isd11-depleted strain
-
-
Manually annotated by BRENDA team
PCC6714
-
-
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
malfunction
metabolism
physiological function
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
L-cysteine
L-alanine + H2S
show the reaction diagram
-
-
or formation of elemental sulfur, depending of presence of a reducing agent in the reaction mixture
-
?
L-cysteine
L-alanine + sulfur
show the reaction diagram
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
pyruvate + sulfide
show the reaction diagram
L-cysteine + ?
?
show the reaction diagram
-
in the presence of cysteine, IscS’s ability to bind iron improves significantly
-
-
?
L-cysteine + ?
L-alanine + ?
show the reaction diagram
-
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 cluster
-
-
?
L-cysteine + acceptor
L-alanine + S-sulfanyl-acceptor
show the reaction diagram
L-cysteine + acceptor
L-alanine + sulfide + ?
show the reaction diagram
L-cysteine + c-ISCS
L-alanine + c-ISCS-SSH
show the reaction diagram
-
-
-
-
?
L-cysteine + c-IscU
L-alanine + c-IscU-SSH
show the reaction diagram
-
-
-
-
?
L-cysteine + CpNifS
L-alanine + CpNifS-SSH
show the reaction diagram
-
-
-
-
?
L-cysteine + DndA
L-alanine + DndA-SSH
show the reaction diagram
-
-
-
?
L-cysteine + enzyme-cysteine
L-alanine + enzyme-S-sulfanylcysteine
show the reaction diagram
L-cysteine + IscS
L-alanine + IscS-SSH
show the reaction diagram
L-cysteine + MOC3 protein
L-alanine + S-sulfanyl-MOC3 protein
show the reaction diagram
-
-
-
-
?
L-cysteine + N,N-dimethyl-4-phenylenediamine
L-alanine + N,N-dimethyl-4-phenylenediamine sulfate
show the reaction diagram
-
-
-
-
?
L-cysteine + RhdA
L-alanine + RhdA-SSH
show the reaction diagram
L-cysteine + Slr0077
L-alanine + Slr0077-SSH
show the reaction diagram
-
-
-
-
?
L-cysteine + SufE
L-alanine + S-sulfanyl-SufE
show the reaction diagram
-
-
-
-
?
L-cysteine + SufS
L-alanine + SufS-SSH
show the reaction diagram
L-cysteine + [enzyme]-cysteine
L-alanine + [enzyme]-S-sulfanylcysteine
show the reaction diagram
L-cysteine + [IscU]-cysteine
L-alanine + [IscU]-S-sulfanylcysteine
show the reaction diagram
-
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
show the reaction diagram
L-cysteine + [ThiI]-cysteine
L-alanine + [ThiI]-S-sulfanylcysteine
show the reaction diagram
-
-
-
-
?
L-cysteine sulfinic acid
L-alanine + sulfite
show the reaction diagram
L-cysteine sulfinic acid + ?
?
show the reaction diagram
cysteine desulfurase DndA catalyzes iron-sulfur cluster assembly by activation of apo-Fe DndC protein
-
-
?
L-cysteine sulfinic acid + DndA
?
show the reaction diagram
-
-
-
?
L-cystine
?
show the reaction diagram
-
-
-
-
?
L-cystine + Slr0077
pyruvate + Slr0077-SSH
show the reaction diagram
-
cystine lyase of Slr0077
-
-
?
L-selenocysteine
L-alanine + selenium
show the reaction diagram
L-selenocysteine + ?
?
show the reaction diagram
-
-
-
?
L-selenocysteine + DndA
L-alanine + DndA-SSeH
show the reaction diagram
-
-
-
?
L-selenocystine
?
show the reaction diagram
-
-
-
-
?
additional information
?
-
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
L-cysteine
L-alanine + sulfur
show the reaction diagram
Q460H9
DndA is able to directly activate apo-Fe DndC for its reconstitution as a fully functional [4Fe-4S] cluster protein (DndC) with unambiguously demonstrated ATP pyrophosphatase activity
-
-
?
L-cysteine + acceptor
L-alanine + S-sulfanyl-acceptor
show the reaction diagram
L-cysteine + enzyme-cysteine
L-alanine + enzyme-S-sulfanylcysteine
show the reaction diagram
-
involved in the formation of Fe-S proteins
-
-
?
L-cysteine + IscS
L-alanine + IscS-SSH
show the reaction diagram
L-cysteine + MOC3 protein
L-alanine + S-sulfanyl-MOC3 protein
show the reaction diagram
-
-
-
-
?
L-cysteine + RhdA
L-alanine + RhdA-SSH
show the reaction diagram
-
-
-
-
?
L-cysteine + Slr0077
L-alanine + Slr0077-SSH
show the reaction diagram
-
-
-
-
?
L-cysteine + SufE
L-alanine + S-sulfanyl-SufE
show the reaction diagram
-
-
-
-
?
L-cysteine + SufS
L-alanine + SufS-SSH
show the reaction diagram
L-cysteine + [enzyme]-cysteine
L-alanine + [enzyme]-S-sulfanylcysteine
show the reaction diagram
additional information
?
-
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
pyridoxal 5'-phosphate
pyridoxamine 5'-phosphate
the enzyme contains pyridoxamine 5'-phosphate which is catalytically inactive in the cysteine desulfurase reaction, leading to a lack of cysteine desulfurase activity
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
KCl
0-0.5 M KCl gives optimal activities at around 55-60°C. When the KCl concentration is increased to 2.5-3 M, this optimum temperature shifts to between 70-75°C
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
4-chloromercuribenzoate
-
preincubation dramatically inhibits enzyme activity
dithiothreitol
activity is strongly dependent on the presence of dithiothreitol, with activity increasing up to 46% when the reductant is present in the reaction mixture. Concentrations higher than 5 mM cause an inhibitory effect
Fe2+
-
the low desulfurase activity is caused by the modification of IscS rather than by the formation of FeS in the solution
interferon-gamma
-
downregulation of cysteine desulfurase and its protein partner IscU at both mRNA and protein level by stimulation of macrophages with interferon-gamma; the cysteine desulfurase Nfs1 and its scaffold protein partner IscU are down-regulated at both mRNA and protein levels when murine macrophages are physiologically stimulated with interferon-gamma
-
iodoacetamide
-
preincubation dramatically inhibits enzyme activity
K2TeO3
-
mutant strains csdA::Kn, csdB::Kn, ascS::Kn
-
L-Allylglycine
-
irreversible inactivation
L-cysteine
above 0.5 mM
L-selenocysteine
-
inhibits desulfuration of L-cysteine
lipopolysaccharide
-
downregulation of enzyme at both mRNA and protein level by stimulation of macrophages with lipopolysaccharide. Lipopolysaccharide triggers a delayed decline of cysteine desulfurase protein and its protein partner IscU; LPS triggers a delayed decline of Nfs1, rather involving transcriptional events or mRNA instability, also the expression of IscU is down-regulated in LPS-stimulated macrophages
N-ethylmaleimide
-
preincubation dramatically inhibits enzyme activity
N-iodoacetyl-N'-(5-sulfo-1-naphthyl)ethylenediamine
-
up to 90% inhibition at 5 mM
Vinylglycine
-
irreversible inactivation
additional information
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
dithiothreitol
frataxin
-
IcsU
-
forms disulfide bonds with IcsS and stimulates its activity 6fold
-
Isd11p
-
Isd11p is required for the cysteine desulfurase activity of Nfs1p
-
protein Isd11
-
forms a stable complex with Nfs1, prone to aggregation in the absence of Isd11
-
pyridoxal-5'-phosphate
-
-
pyruvate
Suf protein family
-
SufE protein can stimulate up to 8fold, addition of the SufBCD complex further stimulates up to 32fold
-
SufE
-
SufE protein
-
the enzyme requires the SufE partner protein to transfer the persulfide to the Fe-S cluster scaffold
-
additional information
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.043 - 5.1
L-cysteine
0.28 - 190
L-cysteine sulfinic acid
0.13 - 4.17
L-selenocysteine
0.003
[SufU]-cysteine
-
in 50 mM MOPS (pH 7.4), temperature not specified in the publication
-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.1 - 1.01
L-cysteine
3.2 - 3.4
L-cysteine sulfinic acid
0.04 - 15
L-selenocysteine
0.87
[SufU]-cysteine
-
in 50 mM MOPS (pH 7.4), temperature not specified in the publication
-
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.586 - 10.1
L-cysteine
290
[SufU]-cysteine
-
in 50 mM MOPS (pH 7.4), temperature not specified in the publication
-
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
20
allylglycine
-
-
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.0022
-
mutant S326A for s4U synthesis
0.0034
-
mutant S328A for s4U synthesis
0.0036
-
wild type for s4U synthesis
0.0038
-
mutant S336A for s4U synthesis
0.0043
-
mutant L333A for s4U synthesis
0.008
-
recombinant enzyme with L-cysteine as substrate
0.0127
-
cysteine to DTT
0.0224
-
crude extract, at 25°C
0.05
-
H123 mutant with L-selenocysteine as substrate
0.055
-
with L-selenocysteine as substrate
0.082
-
pH 8.0, 50°C, rate of production of thiocyanate
0.1
knockdown of Nfs-like proteins, activity measured in mitochondrial fractions
0.142
-
with L-cysteine as substrate
0.148
-
enzyme after purification, at 25°C
0.2
knockdown of selenocysteine lyase, activity measured in mitochondrial fractions
0.5
knockdown of selenocysteine lyase, activity measured in cytosolic fractions
0.9
activity measured in mitochondrial fractions
1
knockdown of Nfs-like proteins, activity measured in cytosolic fractions
1.3
-
mutant enzyme C241A, pH and temperature not specified in the publication
2.5
activity measured in cytosolic fractions
3.6
substrate L-cysteine sulfinic acid, pH 8.0, 37°C; substrate L-cysteine sulfinic acid, pH 8.0, 37°C
4.5
-
isoenzyme SsCsd1, with L-cysteine sulfinic acid as substrate
4.8
-
isoenzyme SsCsd2, with L-cysteine sulfinic acid as substrate
5.8
-
isoenzyme SsCsd2, with L-selenocysteine as substrate
21
-
isoenzyme SsCsd1, with L-selenocysteine as substrate
38.6
substrate L-cysteine, pH 8.0, 37°C; substrate L-selenocysteine, pH 8.0, 37°C
45.7
-
wild type enzyme, pH and temperature not specified in the publication
56.5
substrate L-cysteine, pH 8.0, 37°C; substrate L-selenocysteine, pH 8.0, 37°C
82500
-
pH 8.0, 50°C
additional information
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7
-
isoenzyme SsCsd1 with L-selenocysteine and isoenzyme SsCsd2 with L-selenocysteine and L-cysteine sulfinic acid as substrates
7.5
maximal activity is obtained in 50 mM phosphate buffer, pH7.5, 2 M KCl at 65°C
7.7
-
isoenzyme SsCsd1 with S-cysteine sulfinic acid as substrate
additional information
-
activity is highly sensitive to pH
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6.5 - 10
pH 6.5: about 45% of maximal activity, pH 10.0: about 45% of maximal activity
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
55 - 60
0-0.5 M KCl gives optimal activities at around 55-60°C.When the KCl concentration is increased to 2.5-3 M, this optimum temperature shifts to between 70-75°C
70 - 75
0-0.5 M KCl gives optimal activities at around 55-60°C.When the KCl concentration is increased to 2.5-3 M, this optimum temperature shifts to between 70-75°C
additional information
-
activity is highly sensitive to temperature
pI VALUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6.1
-
isoelectric focusing
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
PDB
SCOP
CATH
ORGANISM
UNIPROT
Archaeoglobus fulgidus (strain ATCC 49558 / VC-16 / DSM 4304 / JCM 9628 / NBRC 100126)
Archaeoglobus fulgidus (strain ATCC 49558 / VC-16 / DSM 4304 / JCM 9628 / NBRC 100126)
Archaeoglobus fulgidus (strain ATCC 49558 / VC-16 / DSM 4304 / JCM 9628 / NBRC 100126)
Archaeoglobus fulgidus (strain ATCC 49558 / VC-16 / DSM 4304 / JCM 9628 / NBRC 100126)
Bacillus subtilis (strain 168)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Helicobacter pylori (strain ATCC 700392 / 26695)
Helicobacter pylori (strain ATCC 700392 / 26695)
Helicobacter pylori (strain ATCC 700392 / 26695)
Helicobacter pylori (strain ATCC 700392 / 26695)
Legionella pneumophila subsp. pneumophila (strain Philadelphia 1 / ATCC 33152 / DSM 7513)
Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Synechocystis sp. (strain PCC 6803 / Kazusa)
Thermococcus onnurineus (strain NA1)
Thermococcus onnurineus (strain NA1)
Thermococcus onnurineus (strain NA1)
Thermococcus onnurineus (strain NA1)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
43200
-
calculated from nucleotide sequence
44000
-
homodimer, 2 * 44000, SDS-PAGE
46800
2 * 46800, calculated from sequence
47300
-
deduced molcular mass
49720
calculated
50000
-
x * 50000, SDS-PAGE
51000
-
x * 51000, SDS-PAGE
54000
-
x * 54000, SDS-PAGE
55000
-
x * 55000, SDS-PAGE
60200
2 * 60200, SDS-PAGE
87000
-
isoenzyme SsCsd1, gel filtration
87500
-
gel filtration
102000
-
gel filtration
110000
gel filtration
113000
-
gel filtration
140000
-
NifU/NifS complex, gel filtration
180000 - 200000
-
gel filtration
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
homodimer
monomer
-
1 * 46000, SDS-PAGE and modeling of structure; 46000
polymer
tetramer
additional information
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
proteolytic modification
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
modeling of structure
-
microbatch-under-oil method, using 20% (w/v) PEG 3000, 0.2 M sodium chloride, 0.1 M HEPES pH 7.5
hanging drop vapor diffusion method, using 0.2 M calcium acetate, 0.1 sodium cacodylate pH 6.5, 40% (v/v) PEG 300
homodimer in complex with pyrodoxal 5'-phosphate, alanine, and Cys361-persulfide, sitting drop vapor diffusion method, using 0.1 M HEPES, pH 7.5, 50% (w/v) PEG 400
CsdA and CsdACsdE complex, hanging drop vapor diffusion method, using 20-30% (w/v) PEG 8000, 0.05 M potassium di-hydrogen phosphate, and 0.1 M MES, pH 6.5 (or pH 5.5), or 20-30% (w/v) PEG 8000, 0.05 M sodium di-hydrogen phosphate, and 0.1 M MES, pH 6.5 (or 0.1 M Tris, pH 8.5)
hanging drop vapor diffusion method, complexed with L-propargylglycine
-
C327S mutant in complex with pyridoxal 5'-phosphate and in the absence of L-cysteine, hanging drop vapor diffusion method, using 20% (w/v) PEG 3350, 0.1 M sodium acetate, pH 5.5, and 0.2 M ammonium citrate
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5 - 10
-
about 45% residual activity at pH 7.5 and 9.5, almost no activity at pH 5.0 and 10.0
706851
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
40 - 55
-
the enzyme is relatively stable at 40°C with 67% loss of activity, and unstable at temperatures above 55°C
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
4°C, purified protein can be stored one month without loss of activity
-
at 4°C, 1 month, without significant change of activity
-
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
ammonium sulfate precipitation, column chromatography, and Superose 12 gel filtration
by one-step affinity chromatography to homogeneity
-
copurified with IscU
-
DEAE-Toyopearl column chromatography and phenyl-Toyopearl column chromatography
-
Hi-Trap column chromatography
-
HiTrap chelating column chromatography, and gel filtration
isoenzyme SsCsd1, isoenzyme SsCsd2 and isoenzyme SsCsd3
-
Ni affinity column chromatography and Superdex 200 gel filtration
Ni-NTA agarose column chromatography
-
Ni-NTA agarosecolumn chromatography
-
Ni-NTA bead chromatography and Superdex 200 gel filtration
Ni2+ HiTrap chelating resin column chromatography
Ni2+-NTA affinity column chromatography, Source 30Q anion exchange chromatography, and Superdex 200 gel filtration
Ni2+-NTA column chromatography
-
nickel Hi-trap column chromatography
-
purified as the N-terminal His6 fusion protein
-
Q-Sepharose column chromatography and Sephacryl S-200 gel filtration
-
Q-Sepharose column chromatography, and Superdex 75 gel filtration
-
three homologs: CSD, CsdB and IscS
-
to homogeneity with a HiTrap chelating column
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
; expression in Escherichia coli BL21 (DE3)
-
; expression in Escherichia coli BL21(DE3) pLysE, expression vector pET15b
expressed in Escherichia coli
-
expressed in Escherichia coli BL21 (DE3) Codon Plus cells
-
expressed in Escherichia coli BL21(DE3) cells
expressed in Escherichia coli BL21(DE3) RIL cells
expressed in Escherichia coli C41 cells
expressed in Escherichia coli CL100 cells
-
expressed in Escherichia coli Rosetta-Blue(DE3)pLysS cells
-
expressed in Saccharomyces cerevisiae
expressiion in Escherichia coli
-
expression in Escherichia coli
expression in Escherichia coli BL21(DE3)
-
expression in Escherichia coli DH5a
-
expression in HeLa cell
-
wild-type and null mutant
-
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
the IscS activity is stimulated up to 1.6fold in the presence of 10fold molar excess of MoeB subunit, the addition of MoaD subunit to a mixture of IscS and MoeB subunit detectably enhances the desulfurase activity to levels much higher than those observed for the addition of MoeB subunit alone to IscS
-
ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
C384S
the variant mimicks the resting state of the enzyme
C325A
-
no cysteine desulfurase activity
C369S
-
no enzyme activity
C328A
-
IscS mutant, activity towards L-cysteine is almost completely abolished, activity toward L-selenocysteine is much less affected
C328S
-
inactive
C358A
-
CSD mutant, activity towards L-cysteine is almost completely abolished, activity toward L-selenocysteine is much less affected
C364A
-
CsdB mutant, activity towards L-cysteine is almost completely abolished, activity toward L-selenocysteine is much less affected
H123A
-
decreased specific activity towards L-selenocysteine
H55A
-
normal activity towards L-selenocysteine and L-cysteine
L333A
-
mutant defective in Fe-S biosynthesis in vivo but functional in persulfide formation and transfer in vitro
R379A
-
significant loss of activity towards L-selenocysteine
S326A
-
mutant defective in Fe-S biosynthesis in vivo but functional in persulfide formation and transfer in vitro
L333A
-
mutant defective in Fe-S biosynthesis in vivo but functional in persulfide formation and transfer in vitro
-
S326A
-
mutant defective in Fe-S biosynthesis in vivo but functional in persulfide formation and transfer in vitro
-
C421A
-
the mutant has a background desulfurase activity level compared to the wild type enzyme
K263A
-
inactive
C327S/S329C
inactive
S325C/C327S
inactive
C326A
-
inactive,the mutant enzyme is incapable of nucleophilic attack on the sulfur of the substrate L-cysteine
C372A
active enzyme via a second pathway
additional information
Show AA Sequence (30069 entries)
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