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Information on EC 2.8.1.7 - cysteine desulfurase and Organism(s) Synechocystis sp. and UniProt Accession Q55793

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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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Synechocystis sp.
UNIPROT: Q55793
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Word Map
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The taxonomic range for the selected organisms is: Synechocystis sp.
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 + SufS
L-alanine + SufS-SSH
show the reaction diagram
-
-
-
?
L-cysteine
L-alanine + sulfide
show the reaction diagram
-
unlike other cysteine desulfurases the L-cysteine C-S-lyase from Synechocystis does not have a conserved cysteine residue at the active site
-
?
L-cysteine + Slr0077
L-alanine + Slr0077-SSH
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 sulfinic acid
L-alanine + sulfite
show the reaction diagram
-
L-cysteine desulfuration requires a cysteine residue at the active site of the enzyme, but decomposition of L-selenocysteine and L-cysteine sufinic acid do not
-
?
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-selenocystine
?
show the reaction diagram
-
-
-
-
?
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
L-cysteine + SufS
L-alanine + SufS-SSH
show the reaction diagram
-
-
-
?
L-cysteine + Slr0077
L-alanine + Slr0077-SSH
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
-
-
-
-
?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
pyridoxal 5'-phosphate
-
pyridoxal 5'-phosphate
-
-
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Iron
-
[Fe2-S2]ferredoxin
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
dithiothreitol
-
increase of enzyme activity at 50 mM
pyruvate
-
increase of enzyme activity at 5 mM
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.28 - 17
L-cysteine sulfinic acid
0.43 - 0.59
L-selenocysteine
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
3.2 - 3.4
L-cysteine sulfinic acid
4 - 15
L-selenocysteine
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
21
-
isoenzyme SsCsd1, with L-selenocysteine as substrate
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
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
7.7
-
isoenzyme SsCsd1 with S-cysteine sulfinic acid as substrate
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
37
-
assay at
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
strain PCC 6803
Uniprot
Manually annotated by BRENDA team
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
42000
-
2 * 42000, SDS-PAGE
87000
-
isoenzyme SsCsd1, gel filtration
88000
-
isoenzyme SsCsd2, gel filtration
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
dimer
a large domain that binds pyridoxal-5'-phosphate and a smaller domain with the active site cysteine
dimer
-
2 * 42000, SDS-PAGE
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
C372A
active enzyme via a second pathway
C326A
-
inactive,the mutant enzyme is incapable of nucleophilic attack on the sulfur of the substrate L-cysteine
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
isoenzyme SsCsd1, isoenzyme SsCsd2 and isoenzyme SsCsd3
-
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli BL21(DE3) cells
-
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
Manually annotated by BRENDA team
Kato, S.; Mihara, H.; Kurihara, T.; Yoshimura, T.; Esaki, N.
Gene cloning, purification, and characterization of two cyanobacterial NifS homologs driving iron-sulfur cluster formation
Biosci. Biotechnol. Biochem.
64
2412-2419
2000
Synechocystis sp.
Manually annotated by BRENDA team
Kessler, D.
Slr0077 of Synechocystis has cysteine desulfurase as well as cystine lyase activity
Biochem. Biophys. Res. Commun.
320
571-577
2004
Synechocystis sp.
Manually annotated by BRENDA team
Tirupati, B.; Vey, J.L.; Drennan, C.L.; Bollinger, J.M.jr.
Kinetic and structural characterization of Slr0077/SufS, the essential cysteine desulfurase from Synechocystis sp. PCC 6803
Biochemistry
43
12210-12219
2004
Synechocystis sp. (Q55793), Synechocystis sp.
Manually annotated by BRENDA team
Behshad, E.; Parkin, S.E.; Bollinger, J.M.jr.
Mechanism of cysteine desulfurase Slr0387 from Synechocystis sp. PCC 6803: Kinetic analysis of cleavage of the persulfide intermediate by chemical reductants
Biochemistry
43
12220-12226
2004
Synechocystis sp.
Manually annotated by BRENDA team
Behshad, E.; Bollinger, J.M.
Kinetic analysis of cysteine desulfurase CD0387 from Synechocystis sp. PCC 6803: formation of the persulfide intermediate
Biochemistry
48
12014-12023
2009
Synechocystis sp.
Manually annotated by BRENDA team