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Information on EC 2.8.1.7 - cysteine desulfurase and Organism(s) Mus musculus and UniProt Accession Q9Z1J3
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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
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iron-sulfur
- fe-s
- iscu
- persulfide
- frataxin
- pyridoxal
- sufe
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nifs-like
- friedreich
- moco
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plp-dependent
- 2-thiouridine
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desulfuration
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sulfane
- nifu
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35scysteine
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molybdoenzymes
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thionucleosides
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cluster-containing
The taxonomic range for the selected organisms is: Mus musculus
The enzyme appears in selected viruses and cellular organisms
The enzyme appears in selected viruses and cellular organisms
Reaction Schemes
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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
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-
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CsdB
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-
-
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cysteinedesulfurylase
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-
-
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IscS
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-
-
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Nfs1
NIFS
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-
-
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SufS
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-
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Nfs1
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
sulfur atom transfer
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-
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PATHWAY SOURCE
PATHWAYS
KEGG
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-, -, -, -, -, -, -
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
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
interferon-gamma
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downregulation of cysteine desulfurase and its protein partner IscU at both mRNA and protein level by stimulation of macrophages with interferon-gamma
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interferon-gamma
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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
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lipopolysaccharide
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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
lipopolysaccharide
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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
additional information
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exposure of macrophages to exogenous sources of nitric oxide does not alter enzyme expression
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additional information
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exposure of cells to exogenous sources of NO does not alter Nfs1 expression
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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). NFS1_MOUSE
459
0
50570
Swiss-Prot
Mitochondrion (Reliability: 1)
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
additional information
depletion 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 form
additional information
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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 presequence
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Mihara, H.; Esaki, N.
Bacterial cysteine desulfurases: their function and mechanisms
Appl. Microbiol. Biotechnol.
60
12-23
2002
Azotobacter vinelandii, Synechocystis sp., Saccharomyces cerevisiae, Escherichia coli, Haemophilus influenzae, Homo sapiens, Mus musculus, Pseudomonas aeruginosa, Synechocystis sp. PCC6714
Canal, 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 lipopolysaccharide
Arch. Biochem. Biophys.
465
282-292
2007
Mus musculus
Fosset, 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 cells
J. Biol. Chem.
281
25398-25406
2006
Mus musculus (Q9Z1J3)
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