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Information on EC 2.8.1.7 - cysteine desulfurase and Organism(s) Haloferax volcanii and UniProt Accession D4GYV5

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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 .
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Haloferax volcanii
UNIPROT: D4GYV5
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Word Map
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The taxonomic range for the selected organisms is: Haloferax volcanii
The enzyme appears in selected viruses and cellular organisms
Reaction Schemes
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L-cysteine
+
acceptor
=
L-alanine
+
S-sulfanyl-acceptor
+
=
+
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
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
-
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 + acceptor
L-alanine + sulfide + ?
show the reaction diagram
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)
-
-
?
additional information
?
-
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
additional information
?
-
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
pyridoxal 5'-phosphate
-
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
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
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
L-cysteine
above 0.5 mM
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
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
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7.5
maximal activity is obtained in 50 mM phosphate buffer, pH7.5, 2 M KCl at 65°C
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
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
SwissProt
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
physiological function
the enzyme is involved in Fe-S cluster assembly in haloarchaea
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
110000
gel filtration
46800
2 * 46800, calculated from sequence
60200
2 * 60200, SDS-PAGE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
dimer
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Zafrilla, B.; Martinez-Espinosa, R.M.; Esclapez, J.; Perez-Pomares, F.; Bonete, M.J.
SufS protein from Haloferax volcanii involved in Fe-S cluster assembly in haloarchaea
Biochim. Biophys. Acta
1804
1476-1482
2010
Haloferax volcanii (D4GYV5), Haloferax volcanii, Haloferax volcanii DSM 3757 (D4GYV5)
Manually annotated by BRENDA team