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Information on EC 2.8.1.1 - thiosulfate sulfurtransferase and Organism(s) Azotobacter vinelandii and UniProt Accession P52197

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EC Tree
     2 Transferases
         2.8 Transferring sulfur-containing groups
             2.8.1 Sulfurtransferases
                2.8.1.1 thiosulfate sulfurtransferase
IUBMB Comments
A few other sulfur compounds can act as donors.
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This record set is specific for:
Azotobacter vinelandii
UNIPROT: P52197
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Word Map
The taxonomic range for the selected organisms is: Azotobacter vinelandii
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
Synonyms
rhodanese, thiosulfate sulfurtransferase, thiosulfate:cyanide sulfurtransferase, rhodanase, glutaredoxin-like protein, cysa2, tstd1, r-rhda, thiosulfate cyanide sulfurtransferase, aq-477, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
rhodanase
-
-
-
-
rhodanese
-
-
-
-
sulfurtransferase, thiosulfate
-
-
-
-
thiosulfate cyanide transsulfurase
-
-
-
-
thiosulfate thiotransferase
-
-
-
-
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
thiosulfate + cyanide = sulfite + thiocyanate
show the reaction diagram
double displacement mechanism
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
sulfur atom transfer
-
-
-
-
SYSTEMATIC NAME
IUBMB Comments
thiosulfate:cyanide sulfurtransferase
A few other sulfur compounds can act as donors.
CAS REGISTRY NUMBER
COMMENTARY hide
9026-04-4
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
thiosulfate + cyanide
sulfite + thiocyanate
show the reaction diagram
-
-
-
?
thiosulfate + cyanide
sulfite + thiocyanate
show the reaction diagram
-
-
-
-
?
thiosulfate + dihydrolipoate
?
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
thiosulfate + cyanide
sulfite + thiocyanate
show the reaction diagram
-
-
-
?
thiosulfate + cyanide
sulfite + thiocyanate
show the reaction diagram
-
-
-
-
?
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
E-4-ethyl-2-[E-hydroxyimino]-5-nitro-3-hexenamide
-
dithithreitol prevents enzyme inhibition and fully restores enzyme activity
S-nitroso-glutathione
-
dithiothreitol prevents enzyme inhibition and fully restores enzyme activity
S-nitroso-N-acetyl-penicillamine
-
dithithreitol prevents enzyme inhibition and fully restores enzyme activity
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
225
-
recombinant wild-type enzyme
pI VALUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
THTR_AZOVI
271
0
29629
Swiss-Prot
-
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
29000
-
calculated from the amino acid composition
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
monomer
-
1 * 29000 SDS-PAGE
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
in the sulfur-free state the catalytic Cys residue adopts two alternate conformations, catalytic mechanism relies primarily on the main-chain conformation of the 230 to 235 active-site loop and on a surrounding strong positive electrostatic field
composed of two identically folded domains with 13 and 21% identical residues
-
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
T232A
-
increase in thiosulfate-cyanide sulfurtransferase activity and no activity with 3-mercaptopyruvate as sulfur donor
T232K
-
increase in thiosulfate-cyanide sulfurtransferase activity and no activity with 3-mercaptopyruvate as sulfur donor
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
dithithreitol prevents enzyme inhibition by NO-donors and fully restores catalytic activity
-
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant N-terminal domain
-
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
cloning and overexpression of the N-terminal domain of the protein
-
overexpression in Escherichia coli BL-21
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overexpression in Escherichia coli M15
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Pagani, S.; Sessa, G.; Sessa, F.; Colnaghi, R.
Properties of Azotobacter vinelandii rhodanese
Biochem. Mol. Biol. Int.
29
595-604
1993
Azotobacter vinelandii
Manually annotated by BRENDA team
Spallarossa, A.; Forlani, F.; Pagani, S.; Salvati, L.; Visca, P.; Ascenzi, P.; Bolognesi, M.; Bordo, D.
Inhibition of Azotobacter vinelandii rhodanese by NO-donors
Biochem. Biophys. Res. Commun.
306
1002-1007
2003
Azotobacter vinelandii
Manually annotated by BRENDA team
Pagani, S.; Forlani, F.; Carpen, A.; Bordo, D.; Colnaghi, R.
Mutagenic analysis of Thr-232 in rhodanese from Azotobacter vinelandii highlighted the differences of this prokaryotic enzyme from the known sulfurtransferases
FEBS Lett.
472
307-311
2000
Azotobacter vinelandii, Bos taurus
Manually annotated by BRENDA team
Melino, S.; Cicero, D.O.; Orsale, M.; Forlani, F.; Pagani, S.; Paci, M.
Azotobacter vinelandii rhodanese: Selenium loading and ion interaction studies
Eur. J. Biochem.
270
4208-4215
2003
Azotobacter vinelandii
Manually annotated by BRENDA team
Kudlicki, W.; Coffman, A.; Kramer, G.; Hardesty, B.
Renaturation of rhodanese by translational elongation factor (EF) Tu. Protein refolding by EF-Tu flexing
J. Biol. Chem.
272
32206-32210
1997
Azotobacter vinelandii, Bos taurus
Manually annotated by BRENDA team
Bordo, D.; Deriu, D.; Colnaghi, R.; Carpen, A.; Pagani, S.; Bolognesi, M.
The crystal structure of a sulfurtransferase from Azotobacter vinelandii highlights the evolutionary relationship between the rhodanese and phosphatase enzyme families
J. Mol. Biol.
298
691-704
2000
Azotobacter vinelandii (P52197), Azotobacter vinelandii
Manually annotated by BRENDA team
Melino, S.; Cicero, D.O.; Forlani, F.; Pagani, S.; Paci, M.
The N-terminal rhodanese domain from Azotobacter vinelandii has a stable and folded structure independently of the C-terminal domain
FEBS Lett.
577
403-408
2004
Azotobacter vinelandii
Manually annotated by BRENDA team