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Information on EC 2.8.1.1 - thiosulfate sulfurtransferase and Organism(s) Bos taurus and UniProt Accession P00586

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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:
Bos taurus
UNIPROT: P00586
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Word Map
The taxonomic range for the selected organisms is: Bos taurus
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
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
-
-
-
?
4-(dimethylamino)-4'-azobenzene sulfinate + thiosulfate
4-(dimethylamino)-4'-azobenzene thiosulfonate + SO32-
show the reaction diagram
-
-
-
-
?
4-(dimethylamino)-4'-azobenzene thiosulfonate + cyanide
4-(dimethylamino)-4'-azobenzene sulfinate + SCN-
show the reaction diagram
-
-
-
-
?
4-(dimethylamino)-4'-azobenzene thiosulfonate + glutathione
4-(dimethylamino)-4'-azobenzene sulfinate + reduced glutathione
show the reaction diagram
-
-
-
-
?
5-dimethylamino-1-naphthalene sulfinate + thiosulfate
5-dimethylamino-1-naphthalene thiosulfonate + SO32-
show the reaction diagram
-
-
-
-
?
5-dimethylamino-1-naphthalene thiosulfonate + cyanide
5-dimethylamino-1-naphthalene sulfinate + SCN-
show the reaction diagram
-
-
-
-
?
5-dimethylamino-1-naphthalene thiosulfonate + glutathione
5-dimethylamino-1-naphthalene sulfinate + reduced glutathione
show the reaction diagram
-
-
-
-
?
alkyl sulfinate + cyanide
?
show the reaction diagram
-
-
-
-
r
aryl sulfinate + cyanide
?
show the reaction diagram
-
-
-
-
?
cyanide + 2-aminoethanethiosulfate
?
show the reaction diagram
-
K249A
-
-
?
cyanide + ethanethiosulfate
?
show the reaction diagram
-
K249A
-
-
?
cyanide + p-toluenethiosulfonate
?
show the reaction diagram
-
K249A
-
-
?
H2S + cyanide
?
show the reaction diagram
-
very poor substrate
-
-
?
H2S + cyanide
thiocyanate
show the reaction diagram
-
-
-
-
?
persulfide + cyanide
?
show the reaction diagram
-
-
-
-
?
reduced thioredoxin + methane thiosulfonate
?
show the reaction diagram
-
only the less negative rhodanese isoform catalyzes the oxidation of thioredoxin
-
-
r
thiosulfate + borohydride
?
show the reaction diagram
-
-
-
-
?
thiosulfate + cyanide
sulfite + thiocyanate
show the reaction diagram
thiosulfate + dihydrolipoate
?
show the reaction diagram
-
-
-
-
?
thiosulfate + dithionite
?
show the reaction diagram
-
-
-
-
?
thiosulfate + monothiol
?
show the reaction diagram
-
-
-
-
?
thiosulfate + sulfite
sulfite + thiosulfate
show the reaction diagram
thiosulfate + thiosulfinate
?
show the reaction diagram
-
-
-
-
?
thiosulfonate + cyanide
?
show the reaction diagram
-
-
-
-
?
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
thiosulfate + cyanide
sulfite + thiocyanate
show the reaction diagram
-
-
-
?
thiosulfate + cyanide
sulfite + thiocyanate
show the reaction diagram
additional information
?
-
-
enzyme does not metabolize sulfide. The rate limiting step in sulfide detoxification is oxidation by a sulfide oxidase to thiosulfate
-
-
?
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Zn2+
-
one ion per monomer, but not necessary for enzyme activity
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
2-Naphthalene sulfonate
-
-
2-oxoglutarate
-
-
anions
-
-
-
CaCl2
-
0.02 M, 35% inhibition
CN-
-
-
Dinitrobenzene
-
-
dithioerythritol
-
-
dithiothreitol
-
-
DL-dihydrolipoate
-
inactivation of rhodanese, no inactivation of sulfur-free form of the enzyme
H2O2
-
the less negative isoform is more instable to H2O2
H2S
-
at concentrations above 30 mM
lipoate
-
no inactivation of rhodanese, inactivation of sulfur-free form of the enzyme
Phenylglyoxal
-
-
SO32-
-
-
sulfhydryl reagents
-
-
Zn2+
-
not inhibitory to the enzyme, but forms complexes with the substrate cyanide and decreases thus the substrate concentration
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.06
CN-
-
-
3.7 - 73.2
thiosulfate
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.02
-
enzyme from muscle, pH 9.2, 37°C
0.04
-
enzyme from stomach, pH 9.2, 37°C
0.13
-
enzyme from lung, pH 9.2, 37°C
0.26
-
substrate H2S, pH 9.2, 22°C
0.36
-
enzyme from brain, pH 9.2, 37°C
0.82
-
enzyme from kidney cortex, pH 9.2, 37°C
10.3
-
enzyme from epithelial layer of rumen, pH 9.2, 37°C
332
-
wild-type
353
-
Ser-1
389
-
Ser-2
391
-
one additional Arg residue at the 3'-end followed by a TAA stop codon
4.95
-
enzyme from liver, pH 9.2, 37°C
575.5
-
R186L
672.8
-
wild-type
720
-
-
730
-
purificated liver rhodanese
816
-
washed precipitate of recombinant rhodanese
85.3
-
substrate thiosulfate, pH 9.2, 22°C
additional information
-
detection method for cyanide based on the enzymic reaction. Method shows a linear detection range from 0.015 to 0.5 mM with a detection limit of 0.003 mM and a limit of quantitation of 0.09 mM
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
Uniprot
Manually annotated by BRENDA team
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
-
-
Manually annotated by BRENDA team
-
-
Manually annotated by BRENDA team
-
of rumen
Manually annotated by BRENDA team
-
only about 20% of the activity of normal liver
Manually annotated by BRENDA team
-
-
Manually annotated by BRENDA team
-
-
Manually annotated by BRENDA team
-
and muscular layer of rumen
Manually annotated by BRENDA team
additional information
-
in all mammalian tissues except blood and muscle
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
THTR_BOVIN
297
0
33296
Swiss-Prot
Mitochondrion (Reliability: 5)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
18500
-
alpha2, 2 * 18500, crystallographic data
19000
-
alpha2, 2 * 19000, SDS-PAGE
33000
-
x * 33000, bovine liver and recombinant Escherichia coli BL21(DE3) enzyme, SDS-PAGE
37000
-
ultracentrifugation
37500
-
sedimentation velocity-diffusion method
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
?
-
x * 33000, bovine liver and recombinant Escherichia coli BL21(DE3) enzyme, SDS-PAGE
dimer
monomer
additional information
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
at 2 mM (NH4)2SO4 soluble enzyme has low activity and crystals are stable when substrates are added, at 1.4 mM (NH4)2SO4 crystals rapidly dissolve in 1 mM CN- but are relatively stable in 1 mM S2O32-
-
composed of two identically folded domains with 13 and 21% identical residues
-
crystallization in a solution with (NH4)2SO4 at pH 7.3, space group C2 with a: 156.0 A, b: 49.0 A, c: 42.2 A and beta: 98.3°
-
crystallization in a solution with (NH4)2SO4 at pH 7.9
-
the model contains 2327 protein atoms and 407 solvent molecules, replacement of the precipitant (NH4)2SO4 with cryoprotectants in the crystal-suspending medium led to the removal of the sulfate ion from the enzyme active site
-
wild-type and DELTA1-7 in polyethyleneglycol 6000, the two-domain structure is not significantly altered by drastically different crystallization conditions or crystal packing, sitting-drop vapour-diffusion method, orthorhombic crystal
-
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Arg
-
one additional Arg residue at the 3'-end followed by a TAA stop codon, no significant changes to the wild-type enzyme
C247S
-
no activity to thiosulfate
C254S
-
more resistant than wild-type to inactivation by dithiothreitol, more readily reactivated following oxidative inactivation and increased exposure of hydrophobic surfaces following removal of the transferable sulfur
C254S/C263S
-
less stable in urea than wild type, more resistant than wild-type to inactivation by dithiothreitol, more readily reactivated following oxidative inactivation and increased exposure of hydrophobic surfaces following removal of the transferable sulfur
C263S
-
less stable in urea than wild type
C3S
-
mutant enzyme is fully active but less stable than wild-type enzyme, mutant enzyme has more easily exposed apparent hydrophobic surfaces than wild-type enzyme
C63S
-
less stable in urea than wild type
C63S/C254S/C263S
-
less stable in urea than wild type, more resistant than wild-type to inactivation by dithiothreitol, more readily reactivated following oxidative inactivation and increased exposure of hydrophobic surfaces following removal of the transferable sulfur
DELTA1-3
-
no significant change in stability versus wild-type
DELTA1-7
K249A
R186L
-
increased KM for thiosulfate
Ser-1
-
one additional Ser residue at the 3'-end followed by a TAA stop codon, loss of enzymatic activity above 30°C
Ser-2
-
one additional Ser residue at the 3'-end followed by a TAG stop codon, loss of enzymatic activity above 30°C
additional information
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
at 1.4 M ammonium sulfate, crystals rapidly dissolve in 1 mM CN- but are relatively stable in 1 mM S2O32-
-
at 2 M ammonium sulfate, crystals of the enzyme are stable when substrates are added
-
mutant enzyme C3S is inactivated by bis(1,8-anilinonaphthalenesulfonate) in the light, bis(1,8-anilinonaphthalenesulfonate) is photo-incorporated into the C-terminal domain of C3S and makes the mutant enzyme less stable, binding to wild-type enzyme is very slow
-
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
bovine liver and recombinant Escherichia coli BL21(DE3) enzyme
-
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
transient expression in cos-7 and 293 cells and expression in Escherichia coli XL1 B
expression in a cell free Escherichia coli system by coupled transcription/translation
-
expression in Escherichia coli
-
expression in Escherichia coli BL21(DE3)
-
RENATURED/Commentary
ORGANISM
UNIPROT
LITERATURE
refolds from 8 M urea to enzymatically active species
-
translation elongation factor EF-Tu enhances renaturation of rhodanese after treatment with 8 mM urea
-
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
analysis
-
detection method for cyanide based on in-capillary enzymic reaction. Method shows a linear detection range from 0.015 to 0.5 mM with a detection limit of 0.003 mM and a limit of quantitation of 0.09 mM. The method is rapid, simple and can easily be automated
medicine
-
thiosulfate sulfurtransferase does not metabolize sulfide. The rate limiting step in sulfide detoxification is oxidation by a sulfide oxidase to thiosulfate, therefor the use of thiosulfate sulfurtransferase activity to determine the rate that colonic mucosa detoxifies sulfide is inappropriate
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Cannella, C.; Pecci, L.; Federici, G.
Crystalline rhodanese from beef kidney
Ital. J. Biochem.
21
1-7
1972
Bos taurus
Manually annotated by BRENDA team
Westley, J.
Rhodanese
Adv. Enzymol. Relat. Areas Mol. Biol.
39
327-368
1973
Acidithiobacillus ferrooxidans, Calliphoridae, Bos taurus, Brassica sp., Canis lupus familiaris, Desulfotomaculum nigrificans, Oryctolagus cuniculus, Escherichia coli, Felis catus, Homo sapiens, Manihot esculenta, Petroselinum crispum, Pseudomonas aeruginosa, Spinacia oleracea, Starkeya novella, Thiobacillus denitrificans, Brassica rapa subsp. rapa
Manually annotated by BRENDA team
Westley, J.
Thiosulfate: cyanide sulfurtransferase (rhodanese)
Methods Enzymol.
77
285-291
1981
Bos taurus
Manually annotated by BRENDA team
Drenth, J.; Smit, J.D.G.
Crystallographic data for rhodanese from bovine liver
Biochem. Biophys. Res. Commun.
45
1320-1322
1971
Bos taurus
Manually annotated by BRENDA team
Burrous, M.R.; Lane, J.; Westley, A.; Westley, J.
Chromogenic and fluorigenic substrates for sulfurtransferases
Methods Enzymol.
143
235-239
1987
Bos taurus
Manually annotated by BRENDA team
Oi, S.
Inhibition of bovine liver rhodanese by alpha-ketoglutarate
J. Biochem.
76
455-458
1974
Bos taurus
Manually annotated by BRENDA team
Pagani, S.; Bonomi, F.; Cerletti, P.
The inhibition of rhodanese by lipoate and iron-sulfur proteins
Biochim. Biophys. Acta
742
116-121
1983
Bos taurus
Manually annotated by BRENDA team
Miller, D.M.; Kurzban, G.P.; Mendoza, J.A.; Chirgwin, J.M.; Hardies, S.C.; Horowitz, P.M.
Recombinant bovine rhodanese: purification and comparison with bovine liver rhodanese
Biochim. Biophys. Acta
1121
286-292
1992
Bos taurus
Manually annotated by BRENDA team
Miller, D.M.; Delgado, R.; Chirgwin, J.M.
Expression of cloned bovine adrenal rhodanese
J. Biol. Chem.
266
4686-4691
1991
Bos taurus (P00586), Bos taurus
Manually annotated by BRENDA team
Horowitz, P.M.; Patel, K.
Some comparisons between solution and crystal properties of thiosulfate sulfurtransferase
Biochem. Biophys. Res. Commun.
94
419-423
1980
Bos taurus
Manually annotated by BRENDA team
Pallini, R.; Guazzi, G.C.; Cannella, C.; Cacace, M.G.
Cloning and sequence analysis of the human liver rhodanese: comparison with the bovine and chicken enzymes
Biochem. Biophys. Res. Commun.
180
887-893
1991
Bos taurus, Gallus gallus, Homo sapiens
Manually annotated by BRENDA team
Aird, B.A.; Heinrikson, R.L.; Westley, J.
Isolation and characterization of a prokaryotic sulfurtransferase
J. Biol. Chem.
262
17327-17335
1987
Acinetobacter calcoaceticus, Bos taurus
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
Nandi, D.L.; Horowitz, P.M.; Westley, J.
Rhodanese as a thioredoxin oxidase
Int. J. Biochem. Cell Biol.
32
465-473
2000
Bos taurus
Manually annotated by BRENDA team
Ybarra, J.; Bhattacharyya, A.M.; Panda, M.; Horowitz, P.M.
Active rhodanese lacking nonessential sulfhydryl groups contains an unstable C-terminal domain and can be bound, inactivated, and reactivated by GroEL*
J. Biol. Chem.
278
1693-1699
2003
Bos taurus
Manually annotated by BRENDA team
Trevino, R.J.; Gliubich, F.; Berni, R.; Cianci, M.; Chirgwin, J.M.; Zanotti, G.; Horowitz, P.M.
NH2-terminal sequence truncation decreases the stability of bovine rhodanese, minimally perturbs its crystal structure, and enhances interaction with GroEL under native conditions
J. Biol. Chem.
274
13938-13947
1999
Bos taurus
Manually annotated by BRENDA team
Luo, G.X.; Horowitz, P.M.
The sulfurtransferase activity and structure of rhodanese are affected by site-directed replacement of Arg-186 or Lys-249
J. Biol. Chem.
269
8220-8225
1994
Bos taurus
Manually annotated by BRENDA team
Miller-Martin, D.M.; Chirgwin, J.M.; Horowitz, P.M.
Mutations of noncatalytic sulfhydryl groups influence the stability, folding, and oxidative susceptibility of rhodanese
J. Biol. Chem.
269
3423-3428
1994
Bos taurus
Manually annotated by BRENDA team
Kramer, G.; Ramachandiran, V.; Horowitz, P.; Hardesty, B.
An additional serine residue at the C terminus of rhodanese destabilizes the enzyme
Arch. Biochem. Biophys.
385
332-337
2001
Bos taurus
Manually annotated by BRENDA team
Trevino, R.J.; Hunt, J.; Horowitz, P.M.; Chirgwin, J.M.
Chinese hamster rhodanese cDNA: activity of the expressed protein is not blocked by a C-terminal extension
Protein Expr. Purif.
6
693-699
1995
Bos taurus, Oncorhynchus mykiss
Manually annotated by BRENDA team
Picton, R.; Eggo, M.C.; Merrill, G.A.; Langman, M.J.S.; Singh, S.
Mucosal protection against sulphide: Importance of the enzyme rhodanese
Gut
50
201-205
2002
Bos taurus, Homo sapiens
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
Gliubich, F.; Berni, R.; Colapietro, M.; Barba, L.; Zanotti, G.
Structure of sulfur-substituted rhodanese at 1.36 A resolution
Acta Crystallogr. Sect. D
54
481-486
1998
Bos taurus
Manually annotated by BRENDA team
Kaur, Y.; Ybarra, J.; Horowitz, P.M.
Active rhodanese lacking nonessential sulfhydryl groups has increased hydrophobic exposure not observed in wild-type enzyme
Protein J.
23
255-261
2004
Bos taurus
Manually annotated by BRENDA team
Aminlari, M.; Malekhusseini, A.; Akrami, F.; Ebrahimnejad, H.
Cyanide-metabolizing enzyme rhodanese in human tissues: comparison with domestic animals
Comp. Clin. Pathol.
16
47-51
2007
Bos taurus, Camelus dromedarius, Canis lupus familiaris, Capra hircus, Gallus gallus, Equus caballus, Ovis aries, Homo sapiens
-
Manually annotated by BRENDA team
Wilson, K.; Mudra, M.; Furne, J.; Levitt, M.
Differentiation of the roles of sulfide oxidase and rhodanese in the detoxification of sulfide by the colonic mucosa
Dig. Dis. Sci.
53
277-283
2007
Bos taurus
Manually annotated by BRENDA team
Papezova, K.; Glatz, Z.
Determination of cyanide in microliter samples by capillary electrophoresis and in-capillary enzymatic reaction with rhodanese
J. Chromatogr. A
1120
268-272
2006
Bos taurus
Manually annotated by BRENDA team