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3-mercaptopyruvate + cyanide
pyruvate + thiocyanate
-
-
-
?
3-mercaptopyruvate + dithiothreitol
?
-
-
-
?
3-mercaptopyruvate + thioredoxin
pyruvate + persulfurated thioredoxin
-
-
-
?
thiosulfate + cyanide
SO32- + thiocyanate
-
-
-
?
thiosulfate + [3-mercaptopyruvate sulfurtransferase]-L-cysteine
sulfate + [3-mercaptopyruvate sulfurtransferase]-S-sulfanyl-L-cysteine
-
-
-
?
[3-mercaptopyruvate sulfurtransferase]-S-sulfanyl-L-cysteine + reduced thioredoxin
hydrogen sulfide + [3-mercaptopyruvate sulfurtransferase]-L-cysteine + oxidized thioredoxin
-
-
-
?
2-mercaptoethanol + cyanide
ethanol + thiocyanate
-
-
-
-
?
3-mercaptopyruvate + cyanide
pyruvate + thiocyanate
additional information
?
-
3-mercaptopyruvate + cyanide
pyruvate + thiocyanate
-
-
-
?
3-mercaptopyruvate + cyanide
pyruvate + thiocyanate
-
-
-
-
?
additional information
?
-
-
MST contributes to maintain redox homeostasis
-
-
?
additional information
?
-
MST contributes to maintain redox homeostasis
-
-
?
additional information
?
-
MST contributes to maintain redox homeostasis via exerting control over cysteine catabolism
-
-
?
additional information
?
-
after prolonged incubation of MST with thiosulfate, a trisulfide adduct becomes predominant at the sulfurated catalytic-site cysteine. When these adducts are reduced by Trx with reducing system H2S2 first appears, and then H2S and H2S3
-
-
-
additional information
?
-
-
role in metabolism of some amino acids and low molecular weight sulfur compounds
-
-
?
additional information
?
-
-
cyanide detoxification
-
-
?
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
-
-
?
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dithiothreitol
activates MST chiefly via reduction of a sulfenyl Cys247
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
thioredoxin
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
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
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
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
additional information
-
reduced glutathione does not affect MST activity
-
additional information
reduced glutathione does not affect MST activity
-
additional information
reduced glutathione does not affect MST activity
-
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33000
x * 33000, SDS-PAGE
32800
-
2 * 32800, calculated from amino acid sequence
33000
-
2 * 33000, SDS-PAGE
33000 - 34000
-
gel filtration
34500
-
two peaks with molecular masses of 34500 Da and 53500 Da, enzyme exists as a monomer and homodimer, gel filtration
53000
-
two peaks with molecular masses of 34500 Da and 53500 Da, enzyme exists as a monomer and homodimer, gel filtration
32800
-
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
34000
-
1 * 34000, enzyme exists as a monomer and homodimer, SDS-PAGE, gel filtration
34000
-
2 * 34000, enzyme exists as a monomer and homodimer, SDS-PAGE, gel filtration
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C154S
site-directed mutagenesis, expression in Escherichia coli BL21 (DE3), overexpressed, structurally resembles an active form of MST
C248R
slightly increased Km
C254S
site-directed mutagenesis, expression in Escherichia coli BL21 (DE3), overexpressed, activation with reduced thioredoxin
C263S
site-directed mutagenesis, expression in Escherichia coli BL21 (DE3), overexpressed, structurally resembles an active form of MST
C32S
mutant lacks formation of a disulfide bond with a protein and is not able to produce H2Sn
C64S
site-directed mutagenesis, expression in Escherichia coli BL21 (DE3), overexpressed, activation with reduced thioredoxin
R248G
facilitated catalysis of thiosulfate
S249A
no significant difference in Km compared to wild-type enzyme
S249K
facilitated catalysis of thiosulfate
C247S
-
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
C64S
-
SH group titration, susceptibility to hydrogen peroxide and tetrathionate and renaturation by dithiothreitol similar to wild-type
R187G
-
Ki-value for 3-chloropyruvate similar to wild-type
S249K
-
decrease in kcat/Km
C154S
-
active site mutant
C154S
-
SH group titration, susceptibility to hydrogen peroxide and tetrathionate and renaturation by dithiothreitol similar to wild-type
C263S
-
active site mutant
C263S
-
SH group titration, susceptibility to hydrogen peroxide and tetrathionate and renaturation by dithiothreitol similar to wild-type
R196G
-
decrease in kcat/Km
R196G
-
5fold increase in Ki-value for 3-chloropyruvate
additional information
-
C154S/C263S mutant, site-directed mutagenesis, expression in Escherichia coli BL21 (DE3), overexpressed, structurally resembles an active form of MST
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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Van den Hamer, C.J.A.; morell, A.G.; Scheinberg, I.H.
A study of the cooper content of beta-mercaptopyruvate trans-sulfurase
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242
2514-2516
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Rattus norvegicus
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3-Mercaptopyruvate sulphurtransferase from rat erythrocytes
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Rattus norvegicus (P97532)
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280
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282
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8
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19
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Rattus norvegicus
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130
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8
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496
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