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Information on EC 2.8.1.1 - thiosulfate sulfurtransferase
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2.8.1.1 thiosulfate sulfurtransferaseIUBMB Comments
A few other sulfur compounds can act as donors.
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Word Map
- 2.8.1.1
-
refolding
- thiocyanate
- chaperonins
-
sulfane
- persulfide
- groes
- thiosulphate
-
antidotal
-
sulfur-free
- h2s
-
sulfur-containing
- vinelandii
-
azotobacter
-
chaperone-like
- mercaptopyruvate
-
sulfur-substituted
- dnaj
-
chaperonin-assisted
- cystathionase
-
maltoside
-
urea-denatured
- polysulfides
- thiobacillus
-
desulfuration
- cdc25
-
trisulfide
-
unassisted
- groel-groes
- tetrathionate
-
tetradecamer
- lipoate
- medicine
- pharmacology
- analysis
The enzyme appears in viruses and cellular organisms
Synonyms
Aq-1599, Aq-477, CsoR-like sulfurtransferase repressor, CST, CysA3, GlpE, MtbCysA3, PspE, r-RhdA, RhdB2, 
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
CysA3
MtbCysA3
rhodanase
-
-
-
-
rhodanese
sulfurtransferase, thiosulfate
-
-
-
-
thiosulfate cyanide transsulfurase
-
-
-
-
thiosulfate thiotransferase
-
-
-
-
TST
rhodanese
-
-
-
-
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
thiosulfate + cyanide = sulfite + thiocyanate
double displacement mechanism
-
thiosulfate + cyanide = sulfite + thiocyanate
double displacement mechanism
-
thiosulfate + cyanide = sulfite + thiocyanate
double displacement mechanism
-
thiosulfate + cyanide = sulfite + thiocyanate
double displacement mechanism
-
thiosulfate + cyanide = sulfite + thiocyanate
double displacement mechanism
-
thiosulfate + cyanide = sulfite + thiocyanate
involving a covalent sulfur-enzyme intermediate
-
thiosulfate + cyanide = sulfite + thiocyanate
rhodanese activity is found to be a minor function of erythrocytic beta-mercaptopyruvate
-
thiosulfate + cyanide = sulfite + thiocyanate
-
-
-
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
sulfur atom transfer
-
-
-
-
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PATHWAY SOURCE
PATHWAYS
BRENDA
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SYSTEMATIC NAME
IUBMB Comments
thiosulfate:cyanide sulfurtransferase
A few other sulfur compounds can act as donors.
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CAS REGISTRY NUMBER
COMMENTARY
9026-04-4
-
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
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
-
-
-
-
?
cyanide + 3-mercaptopyruvate
?
-
-
-
?
reduced thioredoxin + methane thiosulfonate
?
-
only the less negative rhodanese isoform catalyzes the oxidation of thioredoxin
-
-
r
thiosulfate + 2-mercaptoethanol
?
-
20% of the activity with cyanide
-
-
?
thiosulfate + D,L-homocysteine
?
-
19% of the activity with cyanide
-
-
?
thiosulfate + glutathione
?
-
20% of the activity with cyanide
-
-
?
thiosulfate + L-cysteine
?
-
12% of the activity with cyanide
-
-
?
thiosulfate + N-acetyl-L-cysteine
?
-
5% of the activity with cyanide
-
-
?
thiosulfate + cyanide
sulfite + thiocyanate
-
overview: function of the enzyme in certain bacterial species
-
-
r
thiosulfate + cyanide
sulfite + thiocyanate
-
-
-
?
thiosulfate + cyanide
sulfite + thiocyanate
-
-
-
-
?
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
-
overview: function of the enzyme in certain bacterial species
-
-
r
thiosulfate + cyanide
sulfite + thiocyanate
-
overview: function of the enzyme in certain bacterial species
-
-
r
thiosulfate + cyanide
sulfite + thiocyanate
-
overview: function of the enzyme in certain bacterial species
-
-
r
thiosulfate + cyanide
sulfite + thiocyanate
-
overview: function of the enzyme in certain bacterial species
-
-
r
thiosulfate + cyanide
sulfite + thiocyanate
-
cyanide-detoxifying function
-
-
r
thiosulfate + cyanide
sulfite + thiocyanate
-
overview: function of the enzyme in certain bacterial species
-
-
r
thiosulfate + cyanide
sulfite + thiocyanate
-
overview: function of the enzyme in certain bacterial species
-
-
r
thiosulfate + cyanide
sulfite + thiocyanate
-
role in aerobic energy metabolism
-
-
?
thiosulfate + cyanide
sulfite + thiocyanate
-
overview: function of the enzyme in certain bacterial species
-
-
r
thiosulfate + cyanide
sulfite + thiocyanate
-
overview: function of the enzyme in certain bacterial species
-
-
r
thiosulfate + cyanide
sulfite + thiocyanate
-
cyanide-detoxifying function
-
-
r
thiosulfate + cyanide
sulfite + thiocyanate
-
overview: function of the enzyme in certain bacterial species
-
-
r
thiosulfate + cyanide
sulfite + thiocyanate
-
overview: function of the enzyme in certain bacterial species
-
-
r
thiosulfate + cyanide
sulfite + thiocyanate
-
-
-
-
?
thiosulfate + cyanide
sulfite + thiocyanate
-
enzyme is involved in cyanide detoxification
-
-
?
thiosulfate + cyanide
sulfite + thiocyanate
-
thiocyanate is less toxic than cyanide
-
-
?
thiosulfate + cyanide
sulfite + thiocyanate
-
thiocyanate is less toxic than cyanide
-
-
?
thiosulfate + cyanide
sulfite + thiocyanate
-
cyanide-detoxifying function
-
-
r
thiosulfate + cyanide
sulfite + thiocyanate
-
overview: function of the enzyme in certain bacterial species
-
-
r
thiosulfate + cyanide
sulfite + thiocyanate
-
overview: function of the enzyme in certain bacterial species
-
-
r
thiosulfate + cyanide
sulfite + thiocyanate
-
overview: function of the enzyme in certain bacterial species
-
-
r
thiosulfate + cyanide
sulfite + thiocyanate
-
cyanide detoxification by engineered Escherichia coli is feasible under laboratory conditions and suggests that microbial rhodaneses may contribute to cyanide transformation in natural environments
-
-
?
thiosulfate + cyanide
sulfite + thiocyanate
-
overview: function of the enzyme in certain bacterial species
-
-
r
thiosulfate + cyanide
sulfite + thiocyanate
-
overview: function of the enzyme in certain bacterial species
-
-
r
thiosulfate + cyanide
sulfite + thiocyanate
-
overview: function of the enzyme in certain bacterial species
-
-
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
?
-
-
no activity with mercaptopyruvate as sulfur donor
-
-
?
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
-
-
?
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
?
-
-
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
?
-
-
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
?
-
-
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
?
-
-
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
?
-
-
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
?
-
-
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
?
-
-
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
?
-
-
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
?
-
-
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
?
-
-
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
?
-
-
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
?
-
-
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
?
-
-
the N-terminal domain of CstA exhibits thiosulfate sulfurtransferase activity
-
-
?
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
?
-
-
no substrates: dithiols which oxidize to cyclic disulfides having more than 5 ring members, i.e. larger than the dithiolane ring of oxidized lipoate
-
-
?
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
additional information
?
-
-
enzyme does not metabolize sulfide. The rate limiting step in sulfide detoxification is oxidation by a sulfide oxidase to thiosulfate
-
-
?
thiosulfate + cyanide
sulfite + thiocyanate
-
overview: function of the enzyme in certain bacterial species
-
-
r
thiosulfate + cyanide
sulfite + thiocyanate
-
-
-
?
thiosulfate + cyanide
sulfite + thiocyanate
-
-
-
-
?
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
-
-
?
thiosulfate + cyanide
sulfite + thiocyanate
-
overview: function of the enzyme in certain bacterial species
-
-
r
thiosulfate + cyanide
sulfite + thiocyanate
-
overview: function of the enzyme in certain bacterial species
-
-
r
thiosulfate + cyanide
sulfite + thiocyanate
-
overview: function of the enzyme in certain bacterial species
-
-
r
thiosulfate + cyanide
sulfite + thiocyanate
-
overview: function of the enzyme in certain bacterial species
-
-
r
thiosulfate + cyanide
sulfite + thiocyanate
-
cyanide-detoxifying function
-
-
r
thiosulfate + cyanide
sulfite + thiocyanate
-
overview: function of the enzyme in certain bacterial species
-
-
r
thiosulfate + cyanide
sulfite + thiocyanate
-
overview: function of the enzyme in certain bacterial species
-
-
r
thiosulfate + cyanide
sulfite + thiocyanate
-
role in aerobic energy metabolism
-
-
?
thiosulfate + cyanide
sulfite + thiocyanate
-
overview: function of the enzyme in certain bacterial species
-
-
r
thiosulfate + cyanide
sulfite + thiocyanate
-
overview: function of the enzyme in certain bacterial species
-
-
r
thiosulfate + cyanide
sulfite + thiocyanate
-
cyanide-detoxifying function
-
-
r
thiosulfate + cyanide
sulfite + thiocyanate
-
overview: function of the enzyme in certain bacterial species
-
-
r
thiosulfate + cyanide
sulfite + thiocyanate
-
overview: function of the enzyme in certain bacterial species
-
-
r
thiosulfate + cyanide
sulfite + thiocyanate
-
-
-
-
?
thiosulfate + cyanide
sulfite + thiocyanate
-
enzyme is involved in cyanide detoxification
-
-
?
thiosulfate + cyanide
sulfite + thiocyanate
-
thiocyanate is less toxic than cyanide
-
-
?
thiosulfate + cyanide
sulfite + thiocyanate
-
thiocyanate is less toxic than cyanide
-
-
?
thiosulfate + cyanide
sulfite + thiocyanate
-
cyanide-detoxifying function
-
-
r
thiosulfate + cyanide
sulfite + thiocyanate
-
overview: function of the enzyme in certain bacterial species
-
-
r
thiosulfate + cyanide
sulfite + thiocyanate
-
overview: function of the enzyme in certain bacterial species
-
-
r
thiosulfate + cyanide
sulfite + thiocyanate
-
overview: function of the enzyme in certain bacterial species
-
-
r
thiosulfate + cyanide
sulfite + thiocyanate
-
cyanide detoxification by engineered Escherichia coli is feasible under laboratory conditions and suggests that microbial rhodaneses may contribute to cyanide transformation in natural environments
-
-
?
thiosulfate + cyanide
sulfite + thiocyanate
-
overview: function of the enzyme in certain bacterial species
-
-
r
thiosulfate + cyanide
sulfite + thiocyanate
-
overview: function of the enzyme in certain bacterial species
-
-
r
thiosulfate + cyanide
sulfite + thiocyanate
-
overview: function of the enzyme in certain bacterial species
-
-
r
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
E-4-ethyl-2-[E-hydroxyimino]-5-nitro-3-hexenamide
-
dithithreitol prevents enzyme inhibition and fully restores enzyme activity
glutathione
-
activation of the enzyme with a maximum at 0.005-0.02 mM, inhibition above
menadione
-
1 h incubation at 0.02 mM leads to loss of the activity of thiosulfate sulfurtransferase by 33%. In addition, 3-mercaptosulfurtransferase and the level of sulfane sulfur and glutathione are decreased
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
SO42-
-
incubation of mitochondria with sulfate causes a significant decrease in activity
Sulfide
-
activating at 0.1 mM, inhibitory above 0.3 mM, in human colon cancer cell line HT-29
2-oxoglutarate
-
incubation of mitochondria with 2-oxoglutarate causes a significant decrease in activity
anions
-
inhibited by most anions at rather high concentration, the most active inhibitors are aromatic anions, incubation of mitochondria with sulfate and 2-oxoglutarate causes a significant decrease in activity
-
DL-dihydrolipoate
-
inactivation of rhodanese, no inactivation of sulfur-free form of the enzyme
DL-dihydrolipoate
-
activation of the enzyme at 0.001 mM, inhibition above 0.0025 mM
L-cysteine
-
0.01 mM enhances activity maximally, 0.2 mM: 29% inhibition
lipoate
-
no inactivation of rhodanese, inactivation of sulfur-free form of the enzyme
sulfite
-
competitive inhibition against thiosulfate in untreated mice, activating effect activity at high thiosulfate concentrations in p-dimethylaminoazobenzene-treated mice
Zn2+
-
not inhibitory to the enzyme, but forms complexes with the substrate cyanide and decreases thus the substrate concentration
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
Butyrate
-
significantly increase of enzyme activity and expression in human colon cancer cell line HT-29
Sulfide
-
activating at 0.1 mM, inhibitory above 0.3 mM, in human colon cancer cell line HT-29
sulfite
-
activating effect at high thiosulfate concentrations in p-dimethylaminoazobenzene-treated mice
2-mercaptoethanol
-
activates in direction of SCN-formation at low CN- concentrations
L-cysteine
-
activates in direction of SCN-formation at low CN- concentrations
L-cysteine
-
0.01 mM enhances activity maximally, 0.2 mM: 29% inhibition
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DISEASE
TITLE OF PUBLICATION
LINK TO PUBMED
Adenocarcinoma
Inactivation of rhodanese from human gastric mucosa and stomach adenocarcinoma by 2,4, 6-trinitrobenzenesulphonate and by 4,4'-diisothiocyanatostilbene-2,2'-disulphonate.
Amyotrophic Lateral Sclerosis
Regional and subcellular distribution of cyanide metabolizing enzymes in the central nervous system.
Anemia, Hemolytic
[Rhodanese activity in the erythrocytes in the course of an experimental hemolytic anemia.]
Bacterial Infections
MdRDH1, a HSP67B2-like rhodanese homologue plays a positive role in maintaining redox balance in Musca domestica.
Carcinogenesis
Heme biosynthesis pathway regulation in a model of hepatocarcinogenesis pre-initiation.
Carcinogenesis
Isolation and partial purification of mitochondrial and cytosolic rhodanese from liver of normal and p-dimethylaminoazobenzene treated mice.
Carcinogenesis
Mitochondrial and cytosolic rhodanese from liver of DAB treated mice. II. Some properties and spectral studies.
Carcinogenesis
Mitochondrial and cytosolic rhodanese from liver of DAB-treated mice. III. Inhibition kinetic studies.
Carcinoma, Ehrlich Tumor
Transamination and transsulphuration of L-cysteine in Ehrlich ascites tumor cells and mouse liver. The nonenzymatic reaction of L-cysteine with pyruvate.
Colitis
Rhodanese, but not cystathionine-gamma-lyase, is associated with dextran sulfate sodium-evoked colitis in mice: a sign of impaired colonic sulfide detoxification?
Hepatitis
[Mitochondrial alterations in experimental hepatitis due to MHV 3 virus: activation and release of fumarase and rhodanese]
Hepatitis
[Recent research on the enzymatic activity of the liver and blood in experimental MHV-3 virus hepatitis: adenylpyrophosphatase, succinic dehydrogenase, rhodanese and phosphoglucomutase.]
Infections
Crystallization and preliminary crystallographic characterization of LmACR2, an arsenate/antimonate reductase from Leishmania major.
Infections
Mycobacterium tuberculosis CysA2 is a dual sulfurtransferase with activity against thiosulfate and 3-mercaptopyruvate and interacts with mammalian cells.
Infections
Proteomic comparison of Mycobacterium avium subspecies paratuberculosis grown in vitro and isolated from clinical cases of ovine paratuberculosis.
Infections
[Metabolic aspects of hepatic tissue in infection of the mouse from EDP virus. III. Adenypyrophosphatase, succinic dehydrogenase and rhodanese activity.]
Inflammatory Bowel Diseases
Polymorphic Variants of Human Rhodanese Exhibit Differences in Thermal Stability and Sulfur Transfer Kinetics.
Leishmaniasis
Crystallization and preliminary crystallographic characterization of LmACR2, an arsenate/antimonate reductase from Leishmania major.
Manganese Poisoning
[Behavior of the rhodanese activity of tissues in experimental manganese poisoning.]
Metabolic Diseases
Unraveling the role of thiosulfate sulfurtransferase in metabolic diseases.
Mucopolysaccharidosis III
Murine cellular model of mucopolysaccharidosis, type IIIB (MPS IIIB) - A preliminary study with particular emphasis on the non-oxidative l-cysteine metabolism.
Neoplasms
Bis(3,5-diiodo-2,4,6-trihydroxyphenyl)squaraine: A novel candidate in photodynamic therapy for skin cancer models in vivo.
Neoplasms
CYSTEINE DESULFHYDRASE AND RHODANASE ACTIVITY IN CELLS OF TISSUE CULTURES AND IN TRANSPLANTABLE TUMORS.
Neoplasms
Evaluation of acetone cyanohydrin effect in 'in vitro' inativation of the Ehrlich ascites tumor cells.
Neoplasms
Identification of novel immunohistochemical tumor markers for primary hepatocellular carcinoma; clathrin heavy chain and formiminotransferase cyclodeaminase.
Neoplasms
Isolation and partial purification of mitochondrial and cytosolic rhodanese from liver of normal and p-dimethylaminoazobenzene treated mice.
Neoplasms
Nephroprotective effect of cystathionine is due to its diverse action on the kidney and Ehrlich ascites tumor cells.
Neoplasms
Rhodanese and ALA-S in mammary tumor and liver from normal and tumor-bearing mice.
Neoplasms
Transamination and transsulphuration of L-cysteine in Ehrlich ascites tumor cells and mouse liver. The nonenzymatic reaction of L-cysteine with pyruvate.
Optic Atrophy
Leber's hereditary optic atrophy: further evidence for a defect of cyanide metabolism?
Optic Atrophy, Hereditary, Leber
Cyanide in human disease: a review of clinical and laboratory evidence.
Optic Atrophy, Hereditary, Leber
Normal rhodanese activity in leukocytes from Leber patients: enzyme characterization and activity levels.
Optic Atrophy, Hereditary, Leber
Rhodanese isozymes in three subjects with Leber's optic neuropathy.
Porphyria, Acute Intermittent
STZ-induced diabetes in mice and heme pathway enzymes. Effect of allylisopropylacetamide and alpha-tocopherol.
Tuberculosis
Expression, purification, crystallization and preliminary X-ray analysis of Rv3117, a probable thiosulfate sulfurtransferase (CysA3) from Mycobacterium tuberculosis.
Tuberculosis
Mycobacterium tuberculosis CysA2 is a dual sulfurtransferase with activity against thiosulfate and 3-mercaptopyruvate and interacts with mammalian cells.
Virus Diseases
[Biochemical study of experimental West Nile virus infections; behavior of succinodehydrogenase, asparticketoglutaric transaminase, adenylpyrophosphatase, rhodanese and hexokinase activity in the brain and liver.]
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.61
CN-
-
37°C, pH 6.5, mitochondrial enzyme of p-dimethylaminoazobenzene-treated mice
1.11
CN-
-
37°C, pH 6.5, cytosolic enzyme of p-dimethylaminoazobenzene-treated mice
1.7
cyanide
-
apparent value, in 100 mM Tris-HCl, pH 9.0, 10 mM KCN, at 85°C
1
thiosulfate
-
apparent value, in 100 mM Tris-HCl, pH 9.0, 10 mM KCN, at 85°C
4.58
thiosulfate
-
37°C, pH 6.5, cytosolic enzyme of p-dimethylaminoazobenzene-treated mice
31.75
thiosulfate
-
37°C, pH 6.5, mitochondrial enzyme of p-dimethylaminoazobenzene-treated mice
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
0.01
0.02
0.027
0.04
0.046
0.05
0.06
0.069
-
rhodanese activity in the Ehrlich ascites tumor cells of tumor-bearing mouse on the fourth day after intraperitoneal administration of methionine
0.07
0.071
0.077
-
rhodanese activity in the Ehrlich ascites tumor cells of tumor-bearing mouse on the fourth day after intraperitoneal administration of cysteine
0.078
-
rhodanese activity in the Ehrlich ascites tumor cells of tumor-bearing mouse on the fourth day after intraperitoneal administration of thiocystine
0.08
0.085
-
rhodanese activity in the Ehrlich ascites tumor cells of tumor-bearing mouse on the fourth day after intraperitoneal administration of 2-methyl-thiazolidine-4-carboxylic acid
0.09
0.113
-
rhodanese activity in the Ehrlich ascites tumor cells of tumor-bearing mouse on the fourth day after intraperitoneal administration of 2-methyl-thiazolidine-2,4-dicarboxylic acid
0.12
0.13
0.15
0.18
0.23
-
rhodanese activity in the liver of tumor-bearing mouse on the fourth day after intraperitoneal administration of cysteine
0.24
0.25
0.26
0.28
0.31
0.32
0.35
0.36
0.362
-
rhodanese activity in the liver of tumor-bearing mouse on the fourth day after intraperitoneal administration of 2-methyl-thiazolidine-2,4-dicarboxylic acid
0.37
0.374
-
rhodanese activity in the liver of tumor-bearing mouse on the fourth day after intraperitoneal administration of 2-methyl-thiazolidine-4-carboxylic acid
0.376
-
rhodanese activity in the liver of tumor-bearing mouse on the fourth day after intraperitoneal administration of methionine
0.4
-
rhodanese activity in the liver of tumor-bearing mouse on the fourth day after intraperitoneal administration of thiocystine
0.47
0.476
-
rhodanese activity in the liver of tumor-bearing mouse on the fourth day after intraperitoneal administration of thiazolidine-4-carboxylic acid
0.56
0.94
1.7
2.93
3.31
3.76
816
additional information
0.071
-
rhodanese activity in the Ehrlich ascites tumor cells of tumor-bearing mouse on the fourth day after intraperitoneal administration of 0.9% NaCl as control
0.071
-
rhodanese activity in the Ehrlich ascites tumor cells of tumor-bearing mouse on the fourth day after intraperitoneal administration of thiosulfate
0.09
-
rhodanese activity in the Ehrlich ascites tumor cells of tumor-bearing mouse on the fourth day after intraperitoneal administration of thiazolidine-4-carboxylic acid
0.24
-
microsomal rhodanese 12 h, 14, 28 and 24 days after apparent operation
0.36
-
rhodanese activity in the liver of tumor-bearing mouse on the fourth day after intraperitoneal administration of thiosulfate
0.37
-
rhodanese activity in the liver of tumor-bearing mouse on the fourth day after intraperitoneal administration of 0.9% NaCl as control
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
additional information
-
up to the 42nd day after a common bile duct ligation rhodanese of cytosol, mitochondria and microsom show a significant decrease in activity, activity of rhodanese in the serum increases markedly with a peak after one day and than decreases gradually to the control level
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
7.5
additional information
-
cytoplasmic enzyme exhibits a more acidic pH-optimum than the mitochondrial enzyme
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
5.5 - 10.5
-
pH 5.5: about 45% of maximal activity, pH 10.5: about 95% of maximal activity, pH 11.0: about 15% of maximal activity
6 - 11
-
pH 6.0: about 75% of activity maximum, pH 11.0: about 70% of activity maximum
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
20
20 - 32
30
35
30
-
mitochondrial and cytosolic enzyme of p-dimethylaminoazobenzene-treated mice
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TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
6.6
-
isoelectric focusing in Phast Gel isoelectric focusing gel with pH range: 3 - 9
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
comparison of enzyme activity with several tissues of sheep, cattle, goat, camel, dog, chicken and human
-
-
brenda
-
645510, 645514, 645519, 645522, 645524, 645525, 645526, 645527, 645528, 645529, 645531, 645535, 645543, 645545, 663321, 673274, 675044
-
-
brenda
comparison of enzyme activity with several tissues of sheep, goat, camel, horse, dog, chicken and human
-
-
brenda
comparison of enzyme activity with several tissues of sheep, cattle, goat, horse, dog, chicken and human
-
-
brenda
comparison of enzyme activity with several tissues of sheep, cattle, goat, camel, horse, dog, chicken and human
-
-
brenda
comparison of enzyme activity with several tissues of sheep, cattle, camel, horse, dog, chicken and human
-
-
brenda
comparison of enzyme activity with several tissues of sheep, cattle, goat, camel, horse, dog, chicken and human
-
-
brenda
comparison of enzyme activity with several tissues of sheep, cattle, goat, camel, horse, dog, chicken
-
-
brenda
higher enzymic activity in females than in males. Circadian rhythm of enzyme activity in the second week of post-natal development is associated with ultradian components, and around 8 weeks of post-natal development the circadian rhythm is stabilized
-
-
brenda
comparison of enzyme activity with several tissues of cattle, goat, camel, horse, dog, chicken and human
-
-
brenda
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
additional information
-
fundus muscle, fundus epithelium, pylore muscle and pylore epithelium
brenda
-
sites of enzyme activity are revealed as punctuate, granular dark dots, abundant in the region of the telencephalon in the astroglia cells and in the region of the mesencephalon in the hippocampus
brenda
-
colocalization with mercaptopyruvate sulfurtransferase in luminal mucosal surface. Both enzymes are expressed by colonocytes, but not in mucin-secrteting goblet cells
brenda
-
-
brenda