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thiosulfate + cyanide
sulfite + thiocyanate
-
-
-
?
4-(dimethylamino)-4'-azobenzene sulfinate + thiosulfate
4-(dimethylamino)-4'-azobenzene thiosulfonate + SO32-
-
-
-
-
?
4-(dimethylamino)-4'-azobenzene thiosulfonate + cyanide
4-(dimethylamino)-4'-azobenzene sulfinate + SCN-
-
-
-
-
?
4-(dimethylamino)-4'-azobenzene thiosulfonate + glutathione
4-(dimethylamino)-4'-azobenzene sulfinate + reduced glutathione
-
-
-
-
?
5-dimethylamino-1-naphthalene sulfinate + thiosulfate
5-dimethylamino-1-naphthalene thiosulfonate + SO32-
-
-
-
-
?
5-dimethylamino-1-naphthalene thiosulfonate + cyanide
5-dimethylamino-1-naphthalene sulfinate + SCN-
-
-
-
-
?
5-dimethylamino-1-naphthalene thiosulfonate + glutathione
5-dimethylamino-1-naphthalene sulfinate + reduced glutathione
-
-
-
-
?
alkyl sulfinate + cyanide
?
-
-
-
-
r
aryl sulfinate + cyanide
?
-
-
-
-
?
cyanide + 2-aminoethanethiosulfate
?
-
K249A
-
-
?
cyanide + ethanethiosulfate
?
-
K249A
-
-
?
cyanide + p-toluenethiosulfonate
?
-
K249A
-
-
?
H2S + cyanide
?
-
very poor substrate
-
-
?
H2S + cyanide
thiocyanate
-
-
-
-
?
persulfide + cyanide
?
-
-
-
-
?
reduced thioredoxin + methane thiosulfonate
?
-
only the less negative rhodanese isoform catalyzes the oxidation of thioredoxin
-
-
r
thiosulfate + borohydride
?
-
-
-
-
?
thiosulfate + cyanide
sulfite + thiocyanate
thiosulfate + dihydrolipoate
?
-
-
-
-
?
thiosulfate + dithionite
?
-
-
-
-
?
thiosulfate + monothiol
?
-
-
-
-
?
thiosulfate + sulfite
sulfite + thiosulfate
thiosulfate + thiosulfinate
?
-
-
-
-
?
thiosulfonate + cyanide
?
-
-
-
-
?
additional information
?
-
thiosulfate + cyanide
sulfite + thiocyanate
-
-
645501, 645503, 645504, 645505, 645506, 645507, 645508, 645510, 645514, 645519, 645522, 645524, 645525, 645526, 645527, 645528, 645529, 645531, 645535, 645543, 645545, 673274, 675044 -
-
?
thiosulfate + cyanide
sulfite + thiocyanate
-
-
-
-
r
thiosulfate + cyanide
sulfite + thiocyanate
-
cyanide-detoxifying function
-
-
r
thiosulfate + cyanide
sulfite + thiocyanate
-
overview: function of the enzyme in certain bacterial species
-
-
r
thiosulfate + sulfite
sulfite + thiosulfate
-
-
-
-
?
thiosulfate + sulfite
sulfite + thiosulfate
-
-
-
-
r
additional information
?
-
-
no substrates: dithiols which oxidize to cyclic disulfides having more than 5 ring members, i.e. larger than the dithiolane ring of oxidized lipoate
-
-
?
additional information
?
-
-
enzyme does not metabolize sulfide. The rate limiting step in sulfide detoxification is oxidation by a sulfide oxidase to thiosulfate
-
-
?
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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
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
DELTA1-7
-
measureably destablized but no significantly alteration in contacts at the atomic level of the crystallized protein
DELTA1-7
-
significant destabilization versus wild-type
K249A
-
complete inactivation of rhodanese with thiosulfate
K249A
-
reduced stability, comparable secondary structure, more easily exposed hydrophobic surfaces and a core structure that denatured similarly to the wild-type enzyme, inactive using thiosulfate, but active with thiosulfonates
additional information
-
-
additional information
-
mutation of all nonessential cysteine residues results in a form C3S that is fully active, but less stable than wild-type
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Cannella, C.; Pecci, L.; Federici, G.
Crystalline rhodanese from beef kidney
Ital. J. Biochem.
21
1-7
1972
Bos taurus
brenda
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
brenda
Westley, J.
Thiosulfate: cyanide sulfurtransferase (rhodanese)
Methods Enzymol.
77
285-291
1981
Bos taurus
brenda
Drenth, J.; Smit, J.D.G.
Crystallographic data for rhodanese from bovine liver
Biochem. Biophys. Res. Commun.
45
1320-1322
1971
Bos taurus
brenda
Burrous, M.R.; Lane, J.; Westley, A.; Westley, J.
Chromogenic and fluorigenic substrates for sulfurtransferases
Methods Enzymol.
143
235-239
1987
Bos taurus
brenda
Oi, S.
Inhibition of bovine liver rhodanese by alpha-ketoglutarate
J. Biochem.
76
455-458
1974
Bos taurus
brenda
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
brenda
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
brenda
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
brenda
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
brenda
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
brenda
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
brenda
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
brenda
Nandi, D.L.; Horowitz, P.M.; Westley, J.
Rhodanese as a thioredoxin oxidase
Int. J. Biochem. Cell Biol.
32
465-473
2000
Bos taurus
brenda
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
brenda
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
brenda
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
brenda
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
brenda
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
brenda
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
brenda
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
brenda
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
brenda
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
brenda
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
brenda
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
-
brenda
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
brenda
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
brenda