Any feedback?
Please rate this page
(enzyme.php)
(0/150)

BRENDA support

BRENDA Home
show all | hide all No of entries

Information on EC 2.8.1.7 - cysteine desulfurase and Organism(s) Archaeoglobus fulgidus and UniProt Accession O29689

for references in articles please use BRENDA:EC2.8.1.7
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
EC Tree
     2 Transferases
         2.8 Transferring sulfur-containing groups
             2.8.1 Sulfurtransferases
                2.8.1.7 cysteine desulfurase
IUBMB 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 .
Specify your search results
Select one or more organisms in this record: ?
This record set is specific for:
Archaeoglobus fulgidus
UNIPROT: O29689
Show additional data
Do not include text mining results
Include (text mining) results
Include results (AMENDA + additional results, but less precise)
Word Map
The taxonomic range for the selected organisms is: Archaeoglobus fulgidus
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
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
L-cysteine desulfurase
-
CSD
-
-
-
-
CsdB
-
-
-
-
cysteinedesulfurylase
-
-
-
-
IscS
-
-
-
-
Nfs1
-
-
-
-
NIFS
-
-
-
-
SufS
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
sulfur atom transfer
-
-
-
-
PATHWAY SOURCE
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
-
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
pyridoxal 5'-phosphate
adding pyridoxal 5'-phosphate to IscS produces an enzyme that displays in vitro L-cysteine desulfurase activity
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
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
hanging drop vapor diffusion method, using 0.2 M calcium acetate, 0.1 sodium cacodylate pH 6.5, 40% (v/v) PEG 300
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
ammonium sulfate precipitation, column chromatography, and Superose 12 gel filtration
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli C41 cells
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Yamanaka, Y.; Zeppieri, L.; Nicolet, Y.; Marinoni, E.N.; de Oliveira, J.S.; Odaka, M.; Dean, D.R.; Fontecilla-Camps, J.C.
Crystal structure and functional studies of an unusual L-cysteine desulfurase from Archaeoglobus fulgidus
Dalton Trans.
42
3092-3099
2013
Archaeoglobus fulgidus (O29689), Archaeoglobus fulgidus
Manually annotated by BRENDA team