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Enzyme Nomenclature
Information on EC 2.8.1.2 - 3-mercaptopyruvate sulfurtransferase
for references in articles please use BRENDA:EC2.8.1.2
Word Map on EC 2.8.1.2
- 2.8.1.2
- h2s
- cystathionine
- rhodanese
-
sulfane
- thiosulfate
-
gaseous
-
h2s-producing
- nahs
-
gasotransmitter
- persulfide
-
polysulfides
-
gamma-lyase
-
transsulfuration
-
desulfuration
- thiocyanate
-
h2s-generating
-
trisulfide
-
beta-synthase
- d-cysteine
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The expected taxonomic range for this enzyme is: Eukaryota, Bacteria
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EC NUMBER 
COMMENTARY 
2.8.1.2
-
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RECOMMENDED NAME
GeneOntology No.
3-mercaptopyruvate sulfurtransferase
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
3-mercaptopyruvate + reduced thioredoxin = pyruvate + hydrogen sulfide + oxidized thioredoxin
3-mercaptopyruvate + [3-mercaptopyruvate sulfurtransferase]-L-cysteine = pyruvate + [3-mercaptopyruvate sulfurtransferase]-S-sulfanyl-L-cysteine
(1a)
-
-
-
[3-mercaptopyruvate sulfurtransferase]-S-sulfanyl-L-cysteine + reduced thioredoxin = hydrogen sulfide + [3-mercaptopyruvate sulfurtransferase]-L-cysteine + oxidized thioredoxin
(1b)
-
-
-
3-mercaptopyruvate + reduced thioredoxin = pyruvate + hydrogen sulfide + oxidized thioredoxin
rapid equilibrium-ordered mechanism with 3-mercaptopyruvate as the first substrate; sequential formal mechanism; when 2-mercaptoethanol is the sulfur acceptor addition of the substrate is random
-
3-mercaptopyruvate + reduced thioredoxin = pyruvate + hydrogen sulfide + oxidized thioredoxin
rapid equilibrium-ordered mechanism
-
3-mercaptopyruvate + reduced thioredoxin = pyruvate + hydrogen sulfide + oxidized thioredoxin
sequential formal mechanism
-
3-mercaptopyruvate + reduced thioredoxin = pyruvate + hydrogen sulfide + oxidized thioredoxin
mechanism
-
3-mercaptopyruvate + reduced thioredoxin = pyruvate + hydrogen sulfide + oxidized thioredoxin
mechanism; sulfur transfer mechanism involving C237 as the nucleophilic species and H66, R102 and D262 as residues assisting catalysis
3-mercaptopyruvate + reduced thioredoxin = pyruvate + hydrogen sulfide + oxidized thioredoxin
-
-
-
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
sulfur atom transfer
-
-
-
-
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
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SYSTEMATIC NAME
IUBMB Comments
3-mercaptopyruvate:cyanide sulfurtransferase
Sulfite, sulfinates, mercaptoethanol and mercaptopyruvate can also act as acceptors. The bacterial enzyme is a zinc protein.
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CAS REGISTRY NUMBER
COMMENTARY
9026-05-5
-
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
-
-
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
malfunction
metabolism
physiological function
malfunction
-
mercaptolactate-cysteine disulfiduria is caused by enzyme defect with or without mental retardation
malfunction
-
3-mercaptopyruvate sulfurtransferase-knockout mice exhibit increased anxiety-like behaviors with an increase in serotonin level in the prefrontal cortex, but not with abnormal morphological changes in the brain
metabolism
-
the enzyme interacts with proteins involved in Moco and FeS cluster biosynthesis like L-cysteine desulfurase NFS1 and the rhodanese-like protein MOCS3
metabolism
-
the enzyme is, together with cysteine aminotransferase, primarily responsible for H2S production in peripheral neurons
metabolism
-
the enzyme functions as an antioxidant protein and can produce H2S (or HS2) and SOx
physiological function
-
3MST and cytosolic and mitochondrial cysteine aminotransferases are localized to endothelial cells of the thoracic aorta and together enzymes produce H2S in this cell type. H2S is a smooth muscle relaxant released from endothelium
physiological function
-
changes in MST activity in response to variation in the supply of exogenous cysteine are suggestive of a role for the mercaptopyruvate pathway in the removal of excess intracellular cysteine, redox homeostasis, and antioxidant defense
physiological function
-
the enzyme serves not only as an enzyme in cysteine catabolism, but also as an antioxidant protein
physiological function
-
the enzyme serves not only as an enzyme in cysteine catabolism, but also as an antioxidant protein
physiological function
-
3-mercaptopyruvate sulfurtransferase coupled with cysteine (aspartate) aminotransferase is responsible for the production of H2S in the vascular endothelium of the thoracic aorta
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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
3-mercaptopyruvate + cyanide
H2S + ?
H2S is produced by 3-mercaptopyruvate sulfurtransferase with cysteine aminotransferase in the presence of cysteine and alpha-ketoglutarate, supporting the existence of 3-mercaptopyruvate which has not been identified. Mercaptopyruvate can be provided by the metabolism of cysteine and alpha-ketoglutarate by cysteine aminotransferase (CAT)
a major source of H2S production in the brain is from the enzyme 3-mercaptopyruvate sulfurtransferase
-
?
3-mercaptopyruvate + thioredoxin
?
thioredoxin is the preferred persulfide acceptor
-
-
?
3-mercaptopyruvate + thioredoxin
pyruvate + persulfurated thioredoxin
-
-
-
-
?
3-mercaptopyruvate + cyanide
pyruvate + thiocyanate
-
-
-
-
?
3-mercaptopyruvate + cyanide
pyruvate + thiocyanate
-
-
-
-
?
3-mercaptopyruvate + cyanide
pyruvate + thiocyanate
-
-
-
-
?
3-mercaptopyruvate + cyanide
pyruvate + thiocyanate
-
-
-
-
?
3-mercaptopyruvate + cyanide
pyruvate + thiocyanate
-
-
-
-
?
3-mercaptopyruvate + cyanide
pyruvate + thiocyanate
-
-
-
-
?
additional information
?
-
-
the enzyme plays a role in iron-sulfur chromophore formation in adrenal cortex
-
-
-
additional information
?
-
-
3-mercaptopyruvate sulfurtransferase in conjunction with cysteine (aspartate) aminotransferase contributes significantly in generating H2S from L-cysteine in the presence of alpha-ketoglutarate
-
-
-
additional information
?
-
3-mercaptopyruvate sulfurtransferase produces bound sulfane sulfur
-
-
-
additional information
?
-
-
in the catalytic process of the enzyme, hydrogen peroxide is possibly produced by persulfide of the sulfur-accepted substrate and sulfur oxides are possibly produced in the redox cycle of persulfide formed at the catalytic site cysteine of the reaction intermediate
-
-
-
additional information
?
-
-
the enzyme produces hydrogen sulfide in the presence of both cysteine and 2-oxoglutarate. Thioredoxin and dihydrolipoic acid associate with 3-mercaptopyruvate sulfurtransferase to produce hydrogen sulfide. Other reducing substances, such as NADPH, NADH, GSH, cysteine and CoA, do not have any effect on the reaction
-
-
-
additional information
?
-
-
the enzyme 3MST also produces H2S2 and H2S5 from 3-mercaptopyruvate. H2S3 production from H2S occurs by the enzyme rhodanese
-
-
-
additional information
?
-
-
role in metabolism of some amino acids and low molecular weight sulfur compounds
-
-
-
additional information
?
-
MST contributes to maintain redox homeostasis
-
-
-
additional information
?
-
-
MST contributes to maintain redox homeostasis via exerting control over cysteine catabolism
-
-
-
additional information
?
-
-
3MST and cytosolic and mitochondrial cysteine aminotransferases are localized to endothelial cells of the thoracic aorta and together enzymes produce H2S in this cell type. H2S is a smooth muscle relaxant released from endothelium
-
-
-
additional information
?
-
-
in the catalytic process of the enzyme, hydrogen peroxide is possibly produced by persulfide of the sulfur-accepted substrate and sulfur oxides are possibly produced in the redox cycle of persulfide formed at the catalytic site cysteine of the reaction intermediate
-
-
-
additional information
?
-
-
role in metabolism of some amino acids and low molecular weight sulfur compounds
-
-
-
additional information
?
-
-
has high activity with 3-MP as a sulfur donor and can use several thiol compounds as sulfur acceptor substrates
-
-
-
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NATURAL SUBSTRATES
NATURAL PRODUCTS
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
3-mercaptopyruvate + cyanide
H2S + ?
Q99J99
H2S is produced by 3-mercaptopyruvate sulfurtransferase with cysteine aminotransferase in the presence of cysteine and alpha-ketoglutarate, supporting the existence of 3-mercaptopyruvate which has not been identified. Mercaptopyruvate can be provided by the metabolism of cysteine and alpha-ketoglutarate by cysteine aminotransferase (CAT)
a major source of H2S production in the brain is from the enzyme 3-mercaptopyruvate sulfurtransferase
-
?
3-mercaptopyruvate + thioredoxin
pyruvate + persulfurated thioredoxin
-
-
-
-
?
3-mercaptopyruvate + cyanide
pyruvate + thiocyanate
-
-
-
-
?
3-mercaptopyruvate + cyanide
pyruvate + thiocyanate
-
-
-
-
?
3-mercaptopyruvate + cyanide
pyruvate + thiocyanate
-
-
-
-
?
3-mercaptopyruvate + cyanide
pyruvate + thiocyanate
-
-
-
-
?
3-mercaptopyruvate + cyanide
pyruvate + thiocyanate
-
-
-
-
?
3-mercaptopyruvate + cyanide
pyruvate + thiocyanate
-
-
-
-
?
additional information
?
-
-
the enzyme plays a role in iron-sulfur chromophore formation in adrenal cortex
-
-
-
additional information
?
-
Q99J99
3-mercaptopyruvate sulfurtransferase produces bound sulfane sulfur
-
-
-
additional information
?
-
-
role in metabolism of some amino acids and low molecular weight sulfur compounds
-
-
-
additional information
?
-
P97532
MST contributes to maintain redox homeostasis
-
-
-
additional information
?
-
-
MST contributes to maintain redox homeostasis via exerting control over cysteine catabolism
-
-
-
additional information
?
-
-
3MST and cytosolic and mitochondrial cysteine aminotransferases are localized to endothelial cells of the thoracic aorta and together enzymes produce H2S in this cell type. H2S is a smooth muscle relaxant released from endothelium
-
-
-
additional information
?
-
-
role in metabolism of some amino acids and low molecular weight sulfur compounds
-
-
-
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Cu2+
Zn2+
additional information
Zn2+
-
no indication of a function in the mechanism of catalysis; zinc protein, 1 atom/mol
additional information
-
no effect: 0.02 M CdCl2, 0.5 mM arsenite, 0.01 mM copper acetate
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INHIBITORS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
2-mercaptopropionic acid
-
uncompetitive inhibitor with respect to 3-mercaptopyruvate
3-Chloropyruvate
-
one-on-one manner of inactivation, pseudo first-order kinetics
alpha-Ketobutyrate
-
uncompetitive inhibitor with respect to 3-mercaptopyruvate, 50% inhibition at 13.7 mM
alpha-ketoglutarate
-
uncompetitive inhibitor with respect to 3-mercaptopyruvate, 50% inhibition at 9.5 mM
cyanide
-
inhibits at short-time intervals, slight enhancement at longer periods
dithiothreitol
-
inhibits from 3 mM to 4 mM at a 3-mercaptopyruvate concentration of 15 mM
menadione
-
1 h incubation at 0.02 mM leads to loss of the activity of 3-mercaptosulfurtransferase by 20%. In addition, thiosulfate sulfurtransferase and the level of sulfane sulfur and glutathione are decreased
N-alpha-4-tosyl-L-lysine chloromethyl ketone
-
interferes with Ser-255, 50% inhibition at 0.044 mM
hydrogen peroxide
-
hydrogen peroxide (0.1-0.5 mM) causes a concentration-dependent decrease in the activity of recombinant enzyme (54% inhibition at 0.1 mM, 87% inhibition at 0.5 mM)
hydrogen peroxide
-
together with stoichiometric concentration of tetrathionate, renaturation by dithiothreitol or thioredoxin. Excess molar ratio of hydrogen peroxide inactivates
pyruvate
-
product inhibition, competitive with 3-mercaptopyruvate and 2-mercaptoethanol
pyruvate
-
uncompetitive inhibitor with respect to 3-mercaptopyruvate, 50% inhibition at 13.1 mM
tetrathionate
-
reduced GSH and GSH together with the reducing system partially restore the activity of tetrathionate-inhibited enzyme. Enzyme that is oxidized by an excess molar dose of tetrathionate is completely reactivated by dithiothreitol, reduced thioredoxin, and thioredoxin together with the reducing system
tetrathionate
-
reduced GSH and GSH together with the reducing system partially restore the activity of tetrathionate-inhibited enzyme. Enzyme that is oxidized by an excess molar dose of tetrathionate is completely reactivated by dithiothreitol, reduced thioredoxin, and thioredoxin together with the reducing system
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
diallyl disulfide
-
increase in activity of 3-mercaptosulfotransferase and gamma-cystathionase and elevation of hepatic sulfane sulfur level after intraperitoneal treatment with diallyl disulfie. In Ehrlich ascites cells, diallyl disulfide does not enzymic activites or sulfane sulfur level
additional information
-
reduced glutathione does not affect MST activity
-
dithiothreitol
-
activates from 0.4 mM to 2 mM at a 3-mercaptopyruvate concentration of 0.625 mM, inhibition at 3 mM and 4 mM dithiothreitol
dithiothreitol
-
activates MST chiefly via reduction of a sulfenyl Cys247
thioredoxin
-
rat-reduced thioredoxin activates the enzyme 2.3fold after treatment with dithiothreitol, but dithiothreitol does not increase enzyme activity. The Escherichia coli thioredoxin-thioredoxin reductase-NADPH system more effectively increases enzyme activity to 4.5fold that of the control than the rat thioredoxin-thioredoxin reductase-NADPH system, which increases enzyme activity to 3fold that of the control
thioredoxin
Escherichia coli and rat thioredoxin activate the enzyme to 2.3- and 4.9fold the levels of activation by dithiothreitol-treated and -untreated enzyme, resp. Activation occurs via cleavage of the intersubunit bonds of the enzyme dimer at C154 and C263. Escherichia coli thioredoxin with substitution C35S forms adducts with the enzyme and activates after treatment with dithiotreitol; Escherichia coli or rat reduced thioredoxin (Trx) cleaves the intersubunit disulfide bond to activate MST to 2.3- and 4.9fold the levels of activation of dithiothreitol (DTT)-treated and DTT-untreated MST, respectively. An intersubunit disulfide bond serves as a redox switch for enzyme activation
thioredoxin
-
a low redox potential sulfenate is reversibly formed at a catalytic site cysteine so as to inhibit MST, and thioredoxin-dependent reduction of the sulfenate restored the MST activity; an intermolecular disulfide bond serves as a thioredoxin-dependent redox-sensing switch for the regulation of the enzymatic activity of 3-mercaptopyruvate sulfurtransferase. A cysteine residue on the surface of each subunit is oxidized to form an intersubunit disulfide bond so as to decrease MST activity, and thioredoxin-specific conversion of a dimer to a monomer increased MST acitvity
thioredoxin
-
rat-reduced thioredoxin activates the enzyme 2.3fold after treatment with dithiothreitol, but dithiothreitol does not increase enzyme activity. The Escherichia coli thioredoxin-thioredoxin reductase-NADPH system more effectively increases enzyme activity to 4.5fold that of the control than the rat thioredoxin-thioredoxin reductase-NADPH system, which increases enzyme activity to 3fold that of the control
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.02
3-Mercaptopyruvate
-
glutathione as cosubstrate, in 200 mM of HEPES, pH 7.4, at 37°C
0.022
3-Mercaptopyruvate
-
using L-cysteine as cosubstrate, in 200 mM of HEPES, pH 7.4, at 37°C
0.025
3-Mercaptopyruvate
-
using dihydrolipioic acid as cosubstrate, in 200 mM of HEPES, pH 7.4, at 37°C
0.026
3-Mercaptopyruvate
-
using dithiothreitol as cosubstrate, in 200 mM of HEPES, pH 7.4, at 37°C
0.03
3-Mercaptopyruvate
-
using L-homocysteine as cosubstrate, in 200 mM of HEPES, pH 7.4, at 37°C
0.13
3-Mercaptopyruvate
-
using 2-mercaptoethanol as cosubstrate, in 200 mM of HEPES, pH 7.4, at 37°C
0.35
3-Mercaptopyruvate
-
using cyanide as cosubstrate, in 200 mM of HEPES, pH 7.4, at 37°C; using thioredoxin as cosubstrate, in 200 mM of HEPES, pH 7.4, at 37°C
0.54
3-Mercaptopyruvate
-
isoform TUM1-Iso2, with dithiothreitol as cosubstrate, at pH 10.5 and 37°C
0.55
3-Mercaptopyruvate
-
isoform TUM1-Iso1, with dithiothreitol as cosubstrate, at pH 10.5 and 37°C
1.29
3-Mercaptopyruvate
-
isoform TUM1-Iso2, with cyanide as cosubstrate, at pH 10.5 and 37°C
1.33
3-Mercaptopyruvate
-
isoform TUM1-Iso1, with cyanide as cosubstrate, at pH 10.5 and 37°C
8.34
3-Mercaptopyruvate
-
determination of pyruvate formation, 37°C, pH 9.55
12.5
3-Mercaptopyruvate
-
determination of thiocyanate formation, 37°C, pH 9.55
4.45
cyanide
-
isoform TUM1-Iso1, with cyanide as cosubstrate, at pH 10.5 and 37°C
4.5
cyanide
-
isoform TUM1-Iso2, with cyanide as cosubstrate, at pH 10.5 and 37°C
2.59
dithiothreitol
-
isoform TUM1-Iso2, with dithiothreitol as cosubstrate, at pH 10.5 and 37°C
2.69
dithiothreitol
-
isoform TUM1-Iso1, with dithiothreitol as cosubstrate, at pH 10.5 and 37°C
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
8.6
3-Mercaptopyruvate
-
isoform TUM1-Iso2, with cyanide as cosubstrate, at pH 10.5 and 37°C
8.8
3-Mercaptopyruvate
-
isoform TUM1-Iso1, with cyanide as cosubstrate, at pH 10.5 and 37°C
20.2
3-Mercaptopyruvate
-
isoform TUM1-Iso2, with dithiothreitol as cosubstrate, at pH 10.5 and 37°C
20.9
3-Mercaptopyruvate
-
isoform TUM1-Iso1, with dithiothreitol as cosubstrate, at pH 10.5 and 37°C
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kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
6.6
3-Mercaptopyruvate
-
isoform TUM1-Iso1, with cyanide as cosubstrate, at pH 10.5 and 37°C
6.7
3-Mercaptopyruvate
-
isoform TUM1-Iso2, with cyanide as cosubstrate, at pH 10.5 and 37°C
38.2
3-Mercaptopyruvate
-
isoform TUM1-Iso1, with dithiothreitol as cosubstrate, at pH 10.5 and 37°C; isoform TUM1-Iso2, with dithiothreitol as cosubstrate, at pH 10.5 and 37°C
1.9
cyanide
-
isoform TUM1-Iso2, with cyanide as cosubstrate, at pH 10.5 and 37°C
7.7
dithiothreitol
-
isoform TUM1-Iso2, with dithiothreitol as cosubstrate, at pH 10.5 and 37°C
7.8
dithiothreitol
-
isoform TUM1-Iso1, with dithiothreitol as cosubstrate, at pH 10.5 and 37°C
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Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
6.9 - 7.6
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
30
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TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
-
3MST and cytosolic and mitochondrial cysteine aminotransferases are localized to endothelial cells of the thoracic aorta
-
3MST and cytosolic and mitochondrial cysteine aminotransferases are localized to endothelial cells of the thoracic aorta
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
-
highest activity in the matrix, followed by intramembrane space, low activity in inner and outer membrane
-
highest activity in the matrix, followed by intramembrane space, low activity in inner and outer membrane
-
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PDB
SCOP
CATH
ORGANISM
UNIPROT
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
32000
32800
33000
34000
-
1 * 34000, enzyme exists as a monomer and homodimer, SDS-PAGE, gel filtration; 2 * 34000, enzyme exists as a monomer and homodimer, SDS-PAGE, gel filtration
34500
-
two peaks with molecular masses of 34500 Da and 53500 Da, enzyme exists as a monomer and homodimer, gel filtration
36000
40000
53000
-
two peaks with molecular masses of 34500 Da and 53500 Da, enzyme exists as a monomer and homodimer, gel filtration
66600
32800
monomer, gel filtration HPLC analysis, MST exhibits monomer-dimer equilibrium, the monomer to dimer ratio is nearly 9 to 1 in 0.2 M potassium phosphate buffer, pH 7.0
32800
-
monomer, HPLC analysis, MST exhibits monomer-dimer equilibrium, monomer to dimer ratio is nearly 9 to 1 in 0.2 M potassium phosphate buffer, pH 7.0
66600
dimer, gel filtration HPLC analysis, MST exhibits monomer-dimer equilibrium, the dimer is formed via intersubunit disulfide bond
66600
-
dimer, HPLC analysis, MST exhibits monomer-dimer equilibrium, the dimer is formed via intersubunit disulfide bond, inactive form
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SUBUNITS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
dimer
homodimer
monomer
dimer
-
2 * 34000, enzyme exists as a monomer and homodimer, SDS-PAGE, gel filtration
dimer
2*32800, HPLC, MST exhibits monomer-dimer equilibrium, the dimer is formed via intersubunit disulfide bond
dimer
-
2*32800, HPLC, MST exhibits monomer-dimer equilibrium, the dimer is formed via intersubunit disulfide bond, inactive form
dimer
-
2 * 34000, enzyme exists as a monomer and homodimer, SDS-PAGE, gel filtration
-
homodimer
-
2 * 32800, calculated from amino acid sequence; 2 * 33000, SDS-PAGE
monomer
-
1 * 34000, enzyme exists as a monomer and homodimer, SDS-PAGE, gel filtration
monomer
-
1 * 34000, enzyme exists as a monomer and homodimer, SDS-PAGE, gel filtration
-
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POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
sitting drop vapor diffusion method, using 2 M ammonium sulfate, 0.1 M sodium acetate pH 4.5 and 0.02 M betaine hydrochloride
-
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GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
dialysis against urea inactivates, effect is reversed by dialysis, dilution or electrophoresis
-
markedly stabilized during purification and storage by the presence of monovalent cations, maximal stability is obtained if purification and storage are carried out at pH 6.5-7.5 in presence of 0.8 M KCl and 2 mM 2-mercaptoethanol
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very unstable, spontanous inactivation can be partly prevented by glycerol
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OXIDATION STABILITY
ORGANISM
UNIPROT
LITERATURE
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-20°C, stable for at least 12 months without loss of activity
-35°C, 50 mM potassium phosphate buffer, pH 7.4, 0.5 mg/ml bovine serum albumin, 50% glycerol, slow decrease of activity
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Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
glutathione-agarose column chromatography and benzamidine Sepharose column chromatography
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homogeneity
partial
wild-type and 4 truncated versions lacking 10, 32, 50 and 70 amino acids at the C-terminus
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Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
wild-type and 4 truncated versions lacking 10, 32, 50 and 70 amino acids at the C-terminus
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EXPRESSION
ORGANISM
UNIPROT
LITERATURE
following permanent middle cerebral artery occlusion, the enzyme is down-regulated in both the cortex and striatum, but not in the corpus collosum
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the hepatic and renal enzyme activity increases by 0.5 LD50 potassium cyanide. Elevated renal cyanide level is also accompanied by increased enzyme activity
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ENGINEERING
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
C247S
R187G
R196G
C154S
C247S
C254S
C263S
C64S
R196G
S249K
additional information
C247S
site-directed mutagenesis, transient transfection of human embryonic kidney HEK 293-F cells, mutant completely lose the activity to metabolize 3-mercaptopyruvate that is assessed by measuring its products either pyruvate or H2S, the levels of bound sulfane sulfur are not increased
R187G
site-directed mutagenesis, transient transfection of human embryonic kidney HEK 293-F cells, mutant, which greatly lose the activity, decreases the levels of bound sulfane sulfur, but not statistically significant, no H2S production
R196G
site-directed mutagenesis, transient transfection of human embryonic kidney HEK 293-F cells, mutant, which partially lose the activity, does not decrease the levels of bound sulfane sulfur, no H2S production
C154S
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SH group titration, susceptibility to hydrogen peroxide and tetrathionate and renaturation by dithiothreitol similar to wild-type
C154S
site-directed mutagenesis, expression in Escherichia coli BL21 (DE3), overexpressed, structurally resembles an active form of MST
C247S
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SH group titration, susceptibility to hydrogen peroxide and tetrathionate and renaturation by dithiothreitol similar to wild-type
C254S
-
SH group titration, susceptibility to hydrogen peroxide and tetrathionate and renaturation by dithiothreitol similar to wild-type
C254S
site-directed mutagenesis, expression in Escherichia coli BL21 (DE3), overexpressed, activation with reduced thioredoxin
C263S
-
SH group titration, susceptibility to hydrogen peroxide and tetrathionate and renaturation by dithiothreitol similar to wild-type
C263S
site-directed mutagenesis, expression in Escherichia coli BL21 (DE3), overexpressed, structurally resembles an active form of MST
C64S
-
SH group titration, susceptibility to hydrogen peroxide and tetrathionate and renaturation by dithiothreitol similar to wild-type
C64S
site-directed mutagenesis, expression in Escherichia coli BL21 (DE3), overexpressed, activation with reduced thioredoxin
additional information
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the level of 3-mercaptopyruvate sulfurtransferase remains largely unaffected in mutants mecB, cysB, metR, metG, sconB, metG/mecB of Aspergillus nidulans, which are impaired in regulatory genes involved in the sulfur metabolite repression system
additional information
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identification of two intronic polymorphisms and a nonsense mutation in the enzyme gene of 50 unrelated French individuals. The nonsense mutation Y85Stop likely results in a severely truncated protein without enzymatic activity
additional information
C154S/C263S mutant, site-directed mutagenesis, expression in Escherichia coli BL21 (DE3), overexpressed, structurally resembles an active form of MST
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Renatured/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
enzyme inhibited by hydrogen peroxide together with stoichiometric concentration of tetrathionate, complete renaturation by dithiothreitol or thioredoxin
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enzyme regains full activity without the need for assistance in the form of a chaperone or detergent after denaturation is 6 M urea and renaturation using dialysis or dilution
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LINKS TO OTHER DATABASES (specific for EC-Number 2.8.1.2)
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