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Information on EC 2.8.1.7 - cysteine desulfurase and Organism(s) Arabidopsis thaliana and UniProt Accession O49543
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2.8.1.7 cysteine desulfuraseIUBMB Comments
A pyridoxal-phosphate protein. The sulfur from free L-cysteine is first transferred to a cysteine residue in the active site, and then passed on to various other acceptors. The enzyme is involved in the biosynthesis of iron-sulfur clusters, thio-nucleosides in tRNA, thiamine, biotin, lipoate and pyranopterin (molybdopterin) . In Azotobacter vinelandii, this sulfur provides the inorganic sulfide required for nitrogenous metallocluster formation .
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Word Map
- 2.8.1.7
-
iron-sulfur
- fe-s
- iscu
- persulfide
- frataxin
- pyridoxal
- sufe
-
nifs-like
- friedreich
- moco
-
plp-dependent
- 2-thiouridine
-
desulfuration
-
sulfane
- nifu
-
35scysteine
-
molybdoenzymes
-
thionucleosides
-
cluster-containing
The taxonomic range for the selected organisms is: Arabidopsis thaliana
The enzyme appears in selected viruses and cellular organisms
The enzyme appears in selected viruses and cellular organisms
Reaction Schemes
hide(Overall reactions are displayed. Show all >>)
Synonyms
cysteine desulfurase, nfs1p, cpnifs, l-cysteine desulfurase, cysteine desulphurase, stringent starvation protein a, sufs2, lecsl, slr0077, cpsit_0959, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
CSD
-
-
-
-
CsdB
-
-
-
-
cysteinedesulfurylase
-
-
-
-
IscS
-
-
-
-
Nfs1
-
-
-
-
Nfs2
NIFS
-
-
-
-
SufS
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
sulfur atom transfer
-
-
-
-
PATHWAY SOURCE
PATHWAYS
KEGG
-
-, -, -, -, -, -, -
SYSTEMATIC NAME
IUBMB Comments
L-cysteine:acceptor sulfurtransferase
A pyridoxal-phosphate protein. The sulfur from free L-cysteine is first transferred to a cysteine residue in the active site, and then passed on to various other acceptors. The enzyme is involved in the biosynthesis of iron-sulfur clusters, thio-nucleosides in tRNA, thiamine, biotin, lipoate and pyranopterin (molybdopterin) [2]. In Azotobacter vinelandii, this sulfur provides the inorganic sulfide required for nitrogenous metallocluster formation [1].
CAS REGISTRY NUMBER
COMMENTARY
149371-08-4
-
SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
L-cysteine + [enzyme]-cysteine
L-alanine + [enzyme]-S-sulfanylcysteine
-
-
-
?
L-cysteine + [enzyme]-cysteine
L-alanine + [enzyme]-S-sulfanylcysteine
-
-
-
?
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
frataxin
frataxin modulates isoform Nfs1m kinetics, increasing Vmax and decreasing the S0.5 value for L-cysteine
-
additional information
-
in presence of purified recombinant 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 CpNifS
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additional information
the enzyme requires the presence of sulfurtransferases such as SufE proteins for optimal activity
-
additional information
-
the enzyme requires the presence of sulfurtransferases such as SufE proteins for optimal activity
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
4.17
L-selenocysteine
-
25°C, pH 7.4, presence of chloroplast protein CpSufE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). MNIF1_ARATH
453
0
50296
Swiss-Prot
Mitochondrion (Reliability: 2)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
-
enzyme CpNifS forms dynamic complexes with chloroplast protein CpSufE
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
microbatch-under-oil method, using 20% (w/v) PEG 3000, 0.2 M sodium chloride, 0.1 M HEPES pH 7.5
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
additional information
-
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 affected
additional information
-
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
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
HiTrap chelating column chromatography, and gel filtration
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Leon, S.; Touraine, B.; Briat, J.F.; Lobreaux, S.
The AtNFS2 gene from Arabidopsis thaliana encodes a NifS-like plastidial cysteine desulphurase
Biochem. J.
366
557-564
2002
Arabidopsis thaliana
Ye, 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 formation
J. Biol. Chem.
281
8958-8969
2006
Arabidopsis thaliana
Van 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 CpNifS
Proc. Natl. Acad. Sci. USA
104
5686-5691
2007
Arabidopsis thaliana
Turowski, V.R.; Busi, M.V.; Gomez-Casati, D.F.
Structural and functional studies of the mitochondrial cysteine desulfurase from Arabidopsis thaliana
Mol. Plant
5
1001-1010
2012
Arabidopsis thaliana (O49543), Arabidopsis thaliana (Q93WX6), Arabidopsis thaliana
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