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Information on EC 2.8.1.2 - 3-mercaptopyruvate sulfurtransferase
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2.8.1.2 3-mercaptopyruvate sulfurtransferaseIUBMB Comments
The enzyme catalyses a transsulfuration reaction from 2-oxo-3-sulfanylpropanoate to an internal cysteine residue. In the presence of a dithiol such as reduced thioredoxin or dihydrolipoate, the sulfanyl sulfur is released as hydrogen sulfide. The enzyme participates in a sulfur relay process that leads to the 2-thiolation of some tRNAs and to protein urmylation by transferring sulfur between the NFS1 cysteine desulfurase (EC 2.8.1.7) and the MOCS3 sulfurtransferase (EC 2.8.1.11).
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Word Map
- 2.8.1.2
- h2s
- cystathionine
- rhodanese
-
h2s-producing
- thiosulfate
-
sulfane
-
gasotransmitter
-
gaseous
- polysulfides
- nahs
-
cytoprotective
- persulfide
-
gamma-lyase
- beta-synthase
- d-cysteine
-
h2s-generating
-
h2s-synthesizing
-
desulfuration
- analysis
- hydrosulfide
-
trisulfide
-
aminooxyacetic
- medicine
-
sulfhydration
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
Reaction Schemes
Synonyms
3-mercaptopyruvate sulfurtransferase, 3-mercaptopyruvate sulphurtransferase, 3-mercaptopyruvate:cyanide sulfurtransferase, 3-MPST, 3-MST, 3MST, AT1G79230, beta-mercaptopyruvate sulfurtransferase, beta-mercaptopyruvate trans-sulfurase, CysA2, 
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
3-mercaptopyruvate sulfurtransferase
3-mercaptopyruvate sulphurtransferase
3-MPST
3-MST
3MST
beta-mercaptopyruvate sulfurtransferase
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-
-
-
beta-mercaptopyruvate trans-sulfurase
-
-
-
-
CysA2
mercaptopyruvate sulfurtransferase
MPST
MST
Rv0815
SseA
-
-
-
-
sulfurtransferase, 3-mercaptopyruvate
-
-
-
-
additional information
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rhodanese activity, EC 2.8.1.1 is a minor function of human erythrocyte beta-mercaptopyruvate sulfurtransferase
3-MPST
-
-
-
-
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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
mechanism
-
3-mercaptopyruvate + reduced thioredoxin = pyruvate + hydrogen sulfide + oxidized thioredoxin
mechanism
3-mercaptopyruvate + reduced thioredoxin = pyruvate + hydrogen sulfide + oxidized thioredoxin
rapid equilibrium-ordered mechanism with 3-mercaptopyruvate as the first substrate
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3-mercaptopyruvate + reduced thioredoxin = pyruvate + hydrogen sulfide + oxidized thioredoxin
sequential formal mechanism
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3-mercaptopyruvate + reduced thioredoxin = pyruvate + hydrogen sulfide + oxidized thioredoxin
when 2-mercaptoethanol is the sulfur acceptor addition of the substrate is random
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3-mercaptopyruvate + reduced thioredoxin = pyruvate + hydrogen sulfide + oxidized thioredoxin
rapid equilibrium-ordered mechanism
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3-mercaptopyruvate + reduced thioredoxin = pyruvate + hydrogen sulfide + oxidized thioredoxin
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 SOURCE
PATHWAYS
BRENDA
MetaCyc
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SYSTEMATIC NAME
IUBMB Comments
3-mercaptopyruvate:cyanide sulfurtransferase
The enzyme catalyses a transsulfuration reaction from 2-oxo-3-sulfanylpropanoate to an internal cysteine residue. In the presence of a dithiol such as reduced thioredoxin or dihydrolipoate, the sulfanyl sulfur is released as hydrogen sulfide. The enzyme participates in a sulfur relay process that leads to the 2-thiolation of some tRNAs and to protein urmylation by transferring sulfur between the NFS1 cysteine desulfurase (EC 2.8.1.7) and the MOCS3 sulfurtransferase (EC 2.8.1.11).
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CAS REGISTRY NUMBER
COMMENTARY
9026-05-5
-
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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
2-oxo-3-sulfanylpropanoate + [3-mercaptopyruvate sulfurtransferase]-L-cysteine
pyruvate + [3-mercaptopyruvate sulfurtransferase]-S-sulfanyl-L-cysteine
-
-
-
?
3-mercaptopyruvate + 2 glutathione
pyruvate + glutathione disulfide
-
-
-
?
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
-
-
?
thiosulfate + glutathione
sulfite + glutathione disulfide
-
-
-
?
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
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
-
-
-
-
?
3-mercaptopyruvate + cyanide
pyruvate + thiocyanate
-
-
-
?
3-mercaptopyruvate + cyanide
pyruvate + thiocyanate
-
-
-
-
?
3-mercaptopyruvate + thioredoxin
pyruvate + persulfurated thioredoxin
-
-
-
-
?
3-mercaptopyruvate + thioredoxin
pyruvate + persulfurated thioredoxin
-
-
-
-
?
3-mercaptopyruvate + thioredoxin
pyruvate + persulfurated thioredoxin
-
-
-
?
3-mercaptopyruvate + thioredoxin
pyruvate + persulfurated thioredoxin
-
-
-
?
3-mercaptopyruvate + thioredoxin
pyruvate + persulfurated thioredoxin
-
-
-
?
thiosulfate + [3-mercaptopyruvate sulfurtransferase]-L-cysteine
sulfate + [3-mercaptopyruvate sulfurtransferase]-S-sulfanyl-L-cysteine
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-
-
?
thiosulfate + [3-mercaptopyruvate sulfurtransferase]-L-cysteine
sulfate + [3-mercaptopyruvate sulfurtransferase]-S-sulfanyl-L-cysteine
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-
-
?
[3-mercaptopyruvate sulfurtransferase]-S-sulfanyl-L-cysteine + reduced thioredoxin
hydrogen sulfide + [3-mercaptopyruvate sulfurtransferase]-L-cysteine + oxidized thioredoxin
-
-
-
?
[3-mercaptopyruvate sulfurtransferase]-S-sulfanyl-L-cysteine + reduced thioredoxin
hydrogen sulfide + [3-mercaptopyruvate sulfurtransferase]-L-cysteine + oxidized thioredoxin
-
-
-
?
additional information
?
-
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the enzyme plays a role in iron-sulfur chromophore formation in adrenal cortex
-
-
?
additional information
?
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3-mercaptopyruvate sulfurtransferase in conjunction with cysteine (aspartate) aminotransferase contributes significantly in generating H2S from L-cysteine in the presence of alpha-ketoglutarate
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-
?
additional information
?
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3-mercaptopyruvate sulfurtransferase produces bound sulfane sulfur
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-
?
additional information
?
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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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-
?
additional information
?
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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
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-
?
additional information
?
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the enzyme 3MST also produces H2S2 and H2S5 from 3-mercaptopyruvate. H2S3 production from H2S occurs by the enzyme rhodanese
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-
?
additional information
?
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3MST produces Cys-SSH and GSSH together with the potential signaling molecules hydrogen per- and tri-sulfide (H2S2 and H2S3). Cys-SSH and GSSH are produced in the presence of physiological concentrations of cysteine and glutathione, while those with longer sulfur chains, Cys-SSnH and GSSnH, are produced in the presence of lower than physiological concentrations of cysteine and glutathione
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-
additional information
?
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role in metabolism of some amino acids and low molecular weight sulfur compounds
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-
?
additional information
?
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MST contributes to maintain redox homeostasis
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-
?
additional information
?
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MST contributes to maintain redox homeostasis
-
-
?
additional information
?
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MST contributes to maintain redox homeostasis via exerting control over cysteine catabolism
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-
?
additional information
?
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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
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-
?
additional information
?
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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
?
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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
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-
-
additional information
?
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role in metabolism of some amino acids and low molecular weight sulfur compounds
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-
?
additional information
?
-
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has high activity with 3-MP as a sulfur donor and can use several thiol compounds as sulfur acceptor substrates
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-
?
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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
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
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
?
-
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the enzyme plays a role in iron-sulfur chromophore formation in adrenal cortex
-
-
?
additional information
?
-
3-mercaptopyruvate sulfurtransferase produces bound sulfane sulfur
-
-
?
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
-
-
?
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
additional information
-
no effect: 0.02 M CdCl2, 0.5 mM arsenite, 0.01 mM copper acetate
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
1-(2,4-dihydroxyphenyl)-2-[(4-hydroxy-5,6-dimethylthieno[2,3-d]pyrimidin-2-yl)sulfanyl]ethan-1-one
more than 80% inhibition at 0.01 mM
-
2-mercaptopropionic acid
-
uncompetitive inhibitor with respect to 3-mercaptopyruvate
2-[2-[(4-oxo-3,4,4a,8a-tetrahydroquinazolin-2-yl)sulfanyl]acetamido]thiophene-3-carboxamide
more than 80% inhibition at 0.01 mM
2-[[2-(1,4-dihydronaphthalen-1-yl)-2-oxoethyl]sulfanyl]-6-methylpyrimidin-4(3H)-one
more than 80% inhibition at 0.01 mM, almost inactive towards cystathionine gamma-lyase and cystathionine beta-synthase, very low inhibiution of thiosulfate sulfurtransferase, Type II
3-Chloropyruvate
-
one-on-one manner of inactivation, pseudo first-order kinetics
3-[(benzenesulfonyl)amino]benzoic acid
more than 80% inhibition at 0.01 mM
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
S-allyl-L-cysteine
significant decrease in MPST activity at 2245 microM after 24 h and 48 h incubation vs. 1000 microM is associated with decrease in sulfane sulfur levels
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
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
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
-
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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DISEASE
TITLE OF PUBLICATION
LINK TO PUBMED
3-mercaptopyruvate sulfurtransferase deficiency
Effect of 3-mercaptopyruvate Sulfurtransferase Deficiency on the Development of Multiorgan Failure, Inflammation, and Wound Healing in Mice Subjected to Burn Injury.
3-mercaptopyruvate sulfurtransferase deficiency
The Effects of Genetic 3-Mercaptopyruvate Sulfurtransferase Deficiency in Murine Traumatic-Hemorrhagic Shock.
Adenocarcinoma
Potential role of the 3-mercaptopyruvate sulfurtransferase (3-MST)-hydrogen sulfide (H2S) pathway in cancer cells.
Adenocarcinoma of Lung
Potential role of the 3-mercaptopyruvate sulfurtransferase (3-MST)-hydrogen sulfide (H2S) pathway in cancer cells.
Anaphylaxis
Increased Urinary 3-Mercaptolactate Excretion and Enhanced Passive Systemic Anaphylaxis in Mice Lacking Mercaptopyruvate Sulfurtransferase, a Model of Mercaptolactate-Cysteine Disulfiduria.
Astrocytoma
The expression and activity of cystathionine-gamma-lyase and 3-mercaptopyruvate sulfurtransferase in human neoplastic cell lines.
Brain Injuries, Traumatic
Upregulation of 3-MST Relates to Neuronal Autophagy After Traumatic Brain Injury in Mice.
Carcinoma
Potential role of the 3-mercaptopyruvate sulfurtransferase (3-MST)-hydrogen sulfide (H2S) pathway in cancer cells.
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.
Cardiomegaly
?MST and the Regulation of Cardiac CSE and OTR Expression in Trauma and Hemorrhage.
Cardiomegaly
Cardiovascular phenotype of mice lacking 3-mercaptopyruvate sulfurtransferase.
Cerebral Infarction
3-Mercaptopyruvate sulfurtransferase/hydrogen sulfide protects cerebral endothelial cells against oxygen-glucose deprivation/reoxygenation-induced injury via mitoprotection and inhibition of the RhoA/ROCK pathway.
Colonic Neoplasms
N-Acetylcysteine Serves as Substrate of 3-Mercaptopyruvate Sulfurtransferase and Stimulates Sulfide Metabolism in Colon Cancer Cells.
Colonic Neoplasms
Novel Aryl-Substituted Pyrimidones as Inhibitors of 3-Mercaptopyruvate Sulfurtransferase with Antiproliferative Efficacy in Colon Cancer.
Colonic Neoplasms
Role of 3-Mercaptopyruvate Sulfurtransferase in the Regulation of Proliferation, Migration, and Bioenergetics in Murine Colon Cancer Cells.
Down Syndrome
Role of 3-Mercaptopyruvate Sulfurtransferase in the Regulation of Proliferation and Cellular Bioenergetics in Human Down Syndrome Fibroblasts.
Dyspnea
Three-minute constant rate step test for detecting exertional dyspnea relief after bronchodilation in COPD.
Endotoxemia
Effect of endotoxemia in mice genetically deficient in cystathionine-?-lyase, cystathionine-?-synthase or 3-mercaptopyruvate sulfurtransferase.
Glaucoma
Relevant variations and neuroprotecive effect of hydrogen sulfide in a rat glaucoma model.
Hypertension
?MST and the Regulation of Cardiac CSE and OTR Expression in Trauma and Hemorrhage.
Hypertension
Cardiovascular phenotype of mice lacking 3-mercaptopyruvate sulfurtransferase.
Hypertension
Maternal N-acetylcysteine therapy regulates hydrogen sulfide-generating pathway and prevents programmed hypertension in male offspring exposed to prenatal dexamethasone and postnatal high-fat diet.
Hypertension
N-Acetylcysteine Prevents Programmed Hypertension in Male Rat Offspring Born to Suramin-Treated Mothers.
Hyperthyroidism
Altered gene expression of hydrogen sulfide-producing enzymes in the liver and muscles tissues of hyperthyroid rats.
Melanoma
The expression and activity of cystathionine-gamma-lyase and 3-mercaptopyruvate sulfurtransferase in human neoplastic cell lines.
Mucopolysaccharidosis III
Murine cellular model of mucopolysaccharidosis, type IIIB (MPS IIIB) - A preliminary study with particular emphasis on the non-oxidative l-cysteine metabolism.
Myocardial Ischemia
Cardiovascular phenotype of mice lacking 3-mercaptopyruvate sulfurtransferase.
Neoplasms
A Review of Hydrogen Sulfide Synthesis, Metabolism, and Measurement: Is Modulation of Hydrogen Sulfide a Novel Therapeutic for Cancer?
Neoplasms
Aerobic Training-induced Upregulation of YAP1 and Prevention of Cardiac Pathological Hypertrophy in Male Rats.
Neoplasms
Crocin reverses 1-methyl-3-nitroso-1-nitroguanidine (MNNG)-induced malignant transformation in GES-1 cells through the Nrf2/Hippo signaling pathway.
Neoplasms
Cysteine Aminotransferase (CAT): A Pivotal Sponsor in Metabolic Remodeling and an Ally of 3-Mercaptopyruvate Sulfurtransferase (MST) in Cancer.
Neoplasms
Endogenous H2S producing enzymes are involved in apoptosis induction in clear cell renal cell carcinoma.
Neoplasms
Hydrogen Sulfide and Hydrogen Sulfide-Synthesizing Enzymes Are Altered in a Case of Oral Adenoid Cystic Carcinoma.
Neoplasms
Hydrogen Sulfide-Synthesizing Enzymes Are Altered in a Case of Oral Cavity Mucoepidermoid Carcinoma.
Neoplasms
Novel Aryl-Substituted Pyrimidones as Inhibitors of 3-Mercaptopyruvate Sulfurtransferase with Antiproliferative Efficacy in Colon Cancer.
Neoplasms
Polysulfide inhibits hypoxia-elicited hypoxia-inducible factor activation in a mitochondria-dependent manner.
Neoplasms
Potential role of the 3-mercaptopyruvate sulfurtransferase (3-MST)-hydrogen sulfide (H2S) pathway in cancer cells.
Neoplasms
Role of 3-Mercaptopyruvate Sulfurtransferase in the Regulation of Proliferation, Migration, and Bioenergetics in Murine Colon Cancer Cells.
Neoplasms
Transamination and transsulphuration of L-cysteine in Ehrlich ascites tumor cells and mouse liver. The nonenzymatic reaction of L-cysteine with pyruvate.
Neuroblastoma
Inhibition of Human Neuroblastoma Cell Proliferation by N-acetyl-L-cysteine as a Result of Increased Sulfane Sulfur Level.
Neuroblastoma
The expression and activity of cystathionine-gamma-lyase and 3-mercaptopyruvate sulfurtransferase in human neoplastic cell lines.
Non-alcoholic Fatty Liver Disease
Fatty acids promote fatty liver disease via the dysregulation of 3-mercaptopyruvate sulfurtransferase/hydrogen sulfide pathway.
Osteoarthritis
The protective role of the 3-mercaptopyruvate sulfurtransferase (3-MST)-hydrogen sulfide (H2S) pathway against experimental osteoarthritis.
Osteoporosis
Association of Hydrogen Sulfide with Femoral Bone Mineral Density in Osteoporosis Patients: A Preliminary Study.
Polycythemia Vera
The activity of 3-mercaptopyruvate sulfurtransferase in erythrocytes from patients with polycythemia vera.
Pulmonary Disease, Chronic Obstructive
Three-minute constant rate step test for detecting exertional dyspnea relief after bronchodilation in COPD.
Reperfusion Injury
Cardiovascular phenotype of mice lacking 3-mercaptopyruvate sulfurtransferase.
Sepsis
Hydrogen sulfide prevents diaphragm weakness in cecal ligation puncture-induced sepsis by preservation of mitochondrial function.
Stroke
Brain 3-Mercaptopyruvate Sulfurtransferase (3MST): Cellular Localization and Downregulation after Acute Stroke.
Stroke
Sequential butylphthalide therapy combined with dual antiplatelet therapy in the treatment of acute cerebral infarction.
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.015
3-Mercaptopyruvate
cosubstrate N-acetyl-L-cysteine, mitochondrial splice variant MPST2, Hill coefficient 1.1, pH 7.4, 37°C
0.02
3-Mercaptopyruvate
glutathione as cosubstrate, in 200 mM of HEPES, pH 7.4, at 37°C
0.02
3-Mercaptopyruvate
cosubstrate N-acetyl-L-cysteine, cytosolic splice variant MPST1, Hill coefficient 1.3, pH 7.4, 37°C
0.022
3-Mercaptopyruvate
using L-cysteine as cosubstrate, in 200 mM of HEPES, pH 7.4, at 37°C
0.022
3-Mercaptopyruvate
cosubstrate L-cysteine, mitochondrial splice variant MPST2, Hill coefficient 1.4, pH 7.4, 37°C
0.024
3-Mercaptopyruvate
cosubstrate L-cysteine, cytosolic splice variant MPST1, Hill coefficient 1.6, pH 7.4, 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
0.35
3-Mercaptopyruvate
using thioredoxin as cosubstrate, in 200 mM of HEPES, pH 7.4, at 37°C
0.358
3-Mercaptopyruvate
cosubstrate thioredoxin, cytosolic splice variant MPST1, Hill coefficient 2.0, pH 7.4, 37°C
0.36
3-Mercaptopyruvate
cosubstrate thioredoxin, mitochondrial splice variant MPST2, Hill coefficient 2.1, pH 7.4, 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
0.6
3-Mercaptopyruvate
mutant S239A, enzyme displays kinetic cooperativity with respect to 3-mercaptopyruvate and thioredoxin, pH 8.0, 30°C
0.79
3-Mercaptopyruvate
mutant H66A, enzyme displays kinetic cooperativity with respect to 3-mercaptopyruvate and thioredoxin, pH 8.0, 30°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
1.7
3-Mercaptopyruvate
wild-type, enzyme displays kinetic cooperativity with respect to 3-mercaptopyruvate and thioredoxin, pH 8.0, 30°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
3.8
L-cysteine
cytosolic splice variant MPST1, Hill coefficient 1.4, pH 7.4, 37°C
4.5
L-cysteine
mitochondrial splice variant MPST2, Hill coefficient 1.6, pH 7.4, 37°C
16
N-acetyl-L-cysteine
mitochondrial splice variant MPST2, Hill coefficient 2.7, pH 7.4, 37°C
17
N-acetyl-L-cysteine
cytosolic splice variant MPST1, Hill coefficient 2.2, pH 7.4, 37°C
0.003
thioredoxin
cytosolic splice variant MPST1, Hill coefficient 1.6, pH 7.4, 37°C
0.0031
thioredoxin
mitochondrial splice variant MPST2, Hill coefficient 1.4, pH 7.4, 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
0.44
L-cysteine
cytosolic splice variant MPST1, Hill coefficient 1.4, pH 7.4, 37°C
0.5
L-cysteine
mitochondrial splice variant MPST2, Hill coefficient 1.4, pH 7.4, 37°C
0.22
N-acetyl-L-cysteine
cytosolic splice variant MPST1, Hill coefficient 2.2, pH 7.4, 37°C
0.27
N-acetyl-L-cysteine
mitochondrial splice variant MPST2, Hill coefficient 2.2, pH 7.4, 37°C
0.4
thioredoxin
cytosolic splice variant MPST1, Hill coefficient 1.6, pH 7.4, 37°C
0.44
thioredoxin
mitochondrial splice variant MPST2, Hill coefficient 1.6, pH 7.4, 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
38.2
3-Mercaptopyruvate
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
2
cyanide
isoform TUM1-Iso1, 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
0.11
L-cysteine
cytosolic splice variant MPST1, Hill coefficient 1.4, pH 7.4, 37°C
0.11
L-cysteine
mitochondrial splice variant MPST2, Hill coefficient 1.4, pH 7.4, 37°C
0.013
N-acetyl-L-cysteine
cytosolic splice variant MPST1, Hill coefficient 2., pH 7.4, 37°C
0.017
N-acetyl-L-cysteine
mitochondrial splice variant MPST2, Hill coefficient 2.2, pH 7.4, 37°C
0.44
thioredoxin
mitochondrial splice variant MPST2, Hill coefficient 1.6, pH 7.4, 37°C
133
thioredoxin
cytosolic splice variant MPST1, Hill coefficient 1.6, pH 7.4, 37°C
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Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.0063
1-(2,4-dihydroxyphenyl)-2-[(4-hydroxy-5,6-dimethylthieno[2,3-d]pyrimidin-2-yl)sulfanyl]ethan-1-one
Homo sapiens
pH 7.4, 23°C
-
0.0017
2-[2-[(4-oxo-3,4,4a,8a-tetrahydroquinazolin-2-yl)sulfanyl]acetamido]thiophene-3-carboxamide
Homo sapiens
pH 7.4, 23°C
0.0027
2-[[2-(1,4-dihydronaphthalen-1-yl)-2-oxoethyl]sulfanyl]-6-methylpyrimidin-4(3H)-one
Homo sapiens
pH 7.4, 23°C
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
0.7
mitochondrial splice variant MPST2, mutant S250A, substrate L-cysteine, pH 7.4, 37°C
1
mitochondrial splice variant MPST2, mutant D63A, substrate thioredoxin, pH 7.4, 37°C
1.2
mitochondrial splice variant MPST2, mutant H74A, substrate thioredoxin, pH 7.4, 37°C
1.4
mitochondrial splice variant MPST2, mutant D63A, substrate L-cysteine, pH 7.4, 37°C
1.6
mitochondrial splice variant MPST2, mutant H74A, substrate L-cysteine, pH 7.4, 37°C
1.8
wild-type mitochondrial splice variant MPST2, substrate L-cysteine, pH 7.4, 37°C
2.3
2.3
mitochondrial splice variant MPST2, mutant S250A, substrate thioredoxin, pH 7.4, 37°C
2.3
wild-type mitochondrial splice variant MPST2, substrate thioredoxin, pH 7.4, 37°C
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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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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
SwissProt
brenda
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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
brenda
additional information
high protein expression level, neural and glial cells are positively stained
brenda
high protein expression level, hepatocytes around central veins are more strongly stained
brenda
low protein expression level, bronchiolar cells are preferentially stained
brenda
-
3MST and cytosolic and mitochondrial cysteine aminotransferases are localized to endothelial cells of the thoracic aorta
brenda
additional information
MST protein is found in all organs exmained, in fetal tissues, MST expression is similar before and after birth. High expression level is found in endocrine organs
brenda
additional information
-
MST protein is found in all organs exmained, in fetal tissues, MST expression is similar before and after birth. High expression level is found in endocrine organs
brenda
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
two splice variants of MPST, differing by 20 amino acids at the N-terminus, give rise to the cytosolic MPST1 and mitochondrial MPST2 isoforms
brenda
two splice variants of MPST, differing by 20 amino acids at the N-terminus, give rise to the cytosolic MPST1 and mitochondrial MPST2 isoforms
brenda
-
highest activity in the matrix, followed by intramembrane space, low activity in inner and outer membrane
brenda
-
highest activity in the matrix, followed by intramembrane space, low activity in inner and outer membrane
-
brenda
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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 functions as an antioxidant protein and can produce H2S (or HS2) and SOx
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
3MST produces Cys-SSH and GSSH together with the potential signaling molecules hydrogen per- and tri-sulfide (H2S2 and H2S3). Cys-SSH and GSSH are produced in the brain of wild-type mice but not in those of 3MST-KO mice. The levels of total persulfurated species in the brain of 3MST-KO mice are less than 50% of that in the brain of wild-type mice. Cys-SSH and GSSH are produced in the presence of physiological concentrations of cysteine and glutathione, while those with longer sulfur chains, Cys-SSnH and GSSnH, are produced in the presence of lower than physiological concentrations of cysteine and glutathione
metabolism
a mitochondrial sulfur catabolic pathway catalyzes the complete oxidation of L-cysteine to pyruvate and thiosulfate. After transamination to 3-mercaptopyruvate, the sulfhydryl group from L-cysteine is transferred to glutathione by sulfurtransferase Str1 and oxidized to sulfite by the sulfur dioxygenase Ethe1. Sulfite is then converted to thiosulfate by addition of a second persulfide group by sulfurtransferase 1. This pathway is most relevant during early embryo development and for vegetative growth under light-limiting conditions
metabolism
-
the first step of sulfur transfer that leads to pyruvate release and formation of the persulfide intermediate is very efficient. It critically depends on the electrostatic contribution provided by the CGSGVT catalytic loop, any role of the so-called Ser/His/Asp triad can be excluded. In a concerted mechanism, the water-mediated protonation of the pyruvate enolate and S0 transfer from the deprotonated 3-mercaptopyruvate to the thiolate form of the catalytic cysteine occur concomitantly
metabolism
the first step of sulfur transfer that leads to pyruvate release and formation of the persulfide intermediate is very efficient. It critically depends on the electrostatic contribution provided by the CGSGVT catalytic loop, any role of the so-called Ser/His/Asp triad can be excluded. In a concerted mechanism, the water-mediated protonation of the pyruvate enolate and S0 transfer from the deprotonated 3-mercaptopyruvate to the thiolate form of the catalytic cysteine occur concomitantly
metabolism
-
the first step of sulfur transfer that leads to pyruvate release and formation of the persulfide intermediate is very efficient. It critically depends on the electrostatic contribution provided by the CGSGVT catalytic loop, any role of the so-called Ser/His/Asp triad can be excluded. In a concerted mechanism, the water-mediated protonation of the pyruvate enolate and S0 transfer from the deprotonated 3-mercaptopyruvate to the thiolate form of the catalytic cysteine occur concomitantly
-
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
physiological function
attenuation of 3MST by shRNA or pharmacological inhibition of 3MST significantly reduces endothelial cell proliferation,migration, and tube-like network formation. 3MST silencing also suppresses VEGF-induced endothelial cell migration. 3MST attenuation decreases mitochondrial respiration and mitochondrial ATP production, increases glucose uptake, and perturbes the entire endothelia cell metabolome
physiological function
-
cysteine desulfurase (IscS, EC 2.8.1.7), not 3-MST, is the primary source of endogenous H2S in Escherichia coli under anaerobic conditions. A significant decrease in H2S production under anaerobic conditions is observed in Escherichia coli upon deletion of IscS, but not in 3-MST-deficient bacteria
physiological function
embryo development of the thiosulfate sulfurtransferase Str1/sulfur dioxygenase Ethe1 double mutant is comparable with Str1 mutant lines and severyl impaired in comparison to wild-type. Embryogenesis is severely delayed in Str1 mutants and the Ethe1/Str1 double mutant
physiological function
histological observation reveals no remarkable findings in MST gene-deficient mice
physiological function
-
cysteine desulfurase (IscS, EC 2.8.1.7), not 3-MST, is the primary source of endogenous H2S in Escherichia coli under anaerobic conditions. A significant decrease in H2S production under anaerobic conditions is observed in Escherichia coli upon deletion of IscS, but not in 3-MST-deficient bacteria
-
Show AA Sequence and Transmembrane Helices (3370 entries)
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PDB
SCOP
CATH
UNIPROT
ORGANISM
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
32000
32800
33000
34000
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
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
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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SUBUNIT
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
-
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
in complex with inhibitors 2-[2-[(4-oxo-3,4,4a,8a-tetrahydroquinazolin-2-yl)sulfanyl]acetamido]thiophene-3-carboxamide and 2-[[2-(1,4-dihydronaphthalen-1-yl)-2-oxoethyl]sulfanyl]-6-methylpyrimidin-4(3H)-one. Persulfurated residue C248 interacts with the 4-pyrimidone-like aromatic ring of both compounds, and direct hydrogen bonding by R188 and S250 and water-mediated hydrogen bonding by E195 and R197 are observed
sitting drop vapor diffusion method, using 2 M ammonium sulfate, 0.1 M sodium acetate pH 4.5 and 0.02 M betaine hydrochloride
structure of CysA2 at 2.29 A shows two alpha/beta domains. The N domain is inactive, whereas the C domain is responsible for the catalytic activity. The conserved catalytic cysteine of the active site is Cys233
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
D53A
-
mutation of catalytic triad, does not change the kinetic parameters of for the first reaction step
H66A
-
the first step of sulfur transfer becomes rate-limiting in the mutant
H66A/R102L
-
the first step of sulfur transfer becomes rate-limiting in the mutant, with cumulative effects of the mutations
R102K
-
the first step of sulfur transfer becomes rate-limiting in the mutant
R102L
-
the first step of sulfur transfer becomes rate-limiting in the mutant
R178L
-
moderate decrease in kmax1/K3-mercaptopyruvate, the first step of sulfur transfer is not drastically impaired
R178L/R187L
-
substituting both Arg residues does not fully abolish the sulfur transfer step
R187L
-
moderate decrease in kmax1/K3-mercaptopyruvate, the first step of sulfur transfer is not drastically impaired
D53A
-
mutation of catalytic triad, does not change the kinetic parameters of for the first reaction step
-
H66A
-
the first step of sulfur transfer becomes rate-limiting in the mutant
-
R102L
-
the first step of sulfur transfer becomes rate-limiting in the mutant
-
R187L
-
moderate decrease in kmax1/K3-mercaptopyruvate, the first step of sulfur transfer is not drastically impaired
-
D63A
mitochondrial splice variant MPST2, mutation of catalytic triad, mutation of catalytic triad, specific activity in presence of cysteine is comparable to wild-type, specific activity with thioredoxin is 2.3fold decreased
H66A
10fold decrease in kmax1/K3-mercaptopyruvate ratio relative to the wild-type
H74A
mitochondrial splice variant MPST2, mutation of catalytic triad, specific activity in presence of cysteine is comparable to wild-type, specific activity with thioredoxin is 1.9fold decreased
S239A
no key role of residue S239 in the activation of the 3-mercaptopyruvate thiol group
S250A
mitochondrial splice variant MPST2, mutation of catalytic triad, specific activity with cysteine is 2.6fold lower than wild-type, with thioredoxin, specific activity is similar to wild-type
C247S
D63A
mitochondrial splice variant MPST2, mutation of catalytic triad, mutation of catalytic triad, specific activity in presence of cysteine is comparable to wild-type, specific activity with thioredoxin is 2.3fold decreased
H74A
mitochondrial splice variant MPST2, mutation of catalytic triad, specific activity in presence of cysteine is comparable to wild-type, specific activity with thioredoxin is 1.9fold decreased
R187G
R196G
S250A
mitochondrial splice variant MPST2, mutation of catalytic triad, specific activity with cysteine is 2.6fold lower than wild-type, with thioredoxin, specific activity is similar to wild-type
C154S
C247S
C254S
C263S
C32S
mutant lacks formation of a disulfide bond with a protein and is not able to produce H2Sn
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
-
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
-
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
-
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
-
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
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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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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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
-
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
homogeneity
Ni-NTA agarose column chromatography and DEAE-Sepharose column chromatography
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
expressed in Escherichia coli BL21(DE3) cells
expression in Escherichia coli
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
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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RENATURED/Commentary
ORGANISM
UNIPROT
LITERATURE
enzyme inhibited by hydrogen peroxide together with stoichiometric concentration of tetrathionate, complete renaturation by dithiothreitol or thioredoxin
-
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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APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
analysis
high-throughput screening of a large chemical library with a H2S-selective fluorescent probe, HSip-1, based on azamacrocyclic Cu2+ complex chemistry. HSip-1 can detect H2S in aqueous solution with high selectivity over biothiols, inorganic sulfur compounds, reactive oxygen species and reactive nitrogen species
medicine
medicine
a significantly higher level of 3-MST protein expression is observed in Down syndrome (trisomy of human chromosome 21) fibroblasts compared to cells from healthy control individuals. The excess 3-MST is mainly localized to the mitochondrial compartment. Pharmacological inhibition of 3-MST activity improves mitochondrial electron transport and oxidative phosphorylation parameters and enhances cell proliferation in Down syndrome cells but not in healthy control cells
medicine
after 24 h and 48 h incubation of MCF-7 cells with 2245 microM S-allyl-L-cysteine, induction of late apoptosis is observed. A decrease in cell viability is observed with increasing S-allyl-L-cysteine concentration and incubation time. S-allyl-L-cysteine has no significant cytotoxic effect on the MCF-7 cells upon all analyzed concentrations
medicine
colon cancer cells exposed to N-acetylcysteine for 24 h display increased expression and activity of MST and sulfide:quinone oxidoreductase. N-acetylcysteine persists at detectable levels inside the cells exposed to the drug for up to 24 h and sustains H2S synthesis by MST more effectively than cysteine
medicine
CysA2 interacts with pulmonary cells, and it is capable to activate macrophages and dendritic cells
medicine
-
CysA2 interacts with pulmonary cells, and it is capable to activate macrophages and dendritic cells
-
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Scott, E.M.; Wright, R.C.
Identity of beta-mercaptopyruvate sulfurtransferase and rhodanese in human erythrocytes
Biochem. Biophys. Res. Commun.
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1980
Homo sapiens
brenda
Wrobel, M.; Frendo, J.
Comparison of some molecular and catalytic properties of mitochondrial and cytosolic rhodanese and mercaptopyruvate sulphurtransferase from frog (Rana temporaria) liver
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1984
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Van den Hamer, C.J.A.; morell, A.G.; Scheinberg, I.H.
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Rattus norvegicus
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Purification and properties of mercaptopyruvate sulfur transferase of Escherichia coli
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1972
Escherichia coli
brenda
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3-Mercaptopyruvate sulphurtransferase from rat erythrocytes
Acta Biochim. Pol.
29
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Rattus norvegicus
brenda
Kasperczyk, H.; Koj, A.; Wasylewski, Z.
Similarity of some molecular and catalytic parameters of mitochondrial and cytosolic mercaptopyruvate sulfurtransferase from rat liver
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25
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Rattus norvegicus
brenda
Jarabak, R.
3-Mercaptopyruvate sulfurtransferase
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Bos taurus
brenda
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3-Mercaptopyruvate sulfurtransferase: rapid equilibrium-ordered mechanism with cyanide as the acceptor substrate
Biochemistry
19
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1980
Bos taurus
brenda
Koj, A.; Frendo, J.; Wojtczak, L.
Subcellular distribution and intramitochondrial localization of three sulfurtransferases in rat liver
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1975
Rattus norvegicus, Rattus norvegicus Wistar
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Steady-state kinetics of 3-mercaptopyruvate sulfurtransferase from bovine kidney
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185
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1978
Bos taurus
brenda
Taniguchi, T.; Kimura, T.
Role of 3-mercaptopyruvate sulfurtransferase in the formation of the iron-sulfur chromophore of adrenal ferredoxin
Biochim. Biophys. Acta
364
284-295
1974
Bos taurus
brenda
Alphey, M.S.; Williams, R.A.; Mottram, J.C.; Coombs, G.H.; Hunter, W.N.
The crystal structure of Leishmania major 3-mercaptopyruvate sulfurtransferase. A three-domain architecture with a serine protease-like triad at the active site
J. Biol. Chem.
278
48219-48227
2003
Leishmania major
brenda
Frendo, J.; Wrobel, M.; Was, K.
3-Mercaptopyruvate sulfurtransferase and rhodanese activities in human myometrium and leiomyomas of the uterus
Nowotwory J. Oncol.
52
123-125
2002
Homo sapiens
-
brenda
Meyer, T.; Burow, M.; Bauer, M.; Papenbrock, J.
Arabidopsis sulfurtransferases: investigation of their function during senescence and in cyanide detoxification
Planta
217
1-10
2003
Arabidopsis thaliana
brenda
Nagahara, N.; Ito, T.; Kitamura, H.; Nishino, T.
Tissue and subcellular distribution of mercaptopyruvate sulfurtransferase in the rat: confocal laser fluorescence and immunoelectron microscopic studies combined with biochemical analysis
Histochem. Cell Biol.
110
243-250
1998
Rattus norvegicus
brenda
Magahara, N.; Ito, T.; Minami, M.
Mercaptopyruvate sulfurtransferase as a defense against cyanide toxication: molecular properties and mode of detoxification
Histol. Histopathol.
14
1277-1286
1999
Rattus norvegicus
brenda
Magahara, N.; Nishino, T.
Role of amino acid residues in the active site of rat liver mercaptopyruvate sulfurtransferase. CDNA cloning, overexpression, and site-directed mutagenesis
J. Biol. Chem.
271
27395-27401
1996
Rattus norvegicus (P97532)
brenda
Magahara, N.; Okazaki, T.; Nishino, T.
Cytosolic mercaptopyruvate sulfurtransferase is evolutionarily related to mitochondrial rhodanese. Striking similarity in active site amino acid sequence and the increase in the mercaptopyruvate sulfurtransferase activity of rhodanese by site-directed mutagenesis
J. Biol. Chem.
270
16230-16235
1995
Rattus norvegicus, Rattus norvegicus Wistar
brenda
Makamura, T.; Yamaguchi, Y.; Sano, H.
Plant mercaptopyruvate sulfurtransferases: molecular cloning, subcellular localization and enzymatic activities
Eur. J. Biochem.
267
5621-5630
2000
Arabidopsis thaliana (Q24JL3)
brenda
Porter, D.W.; Baskin, S.I.
Specificity studies of 3-mercaptopyruvate sulfurtransferase
J. Biochem. Toxicol.
10
287-292
1995
Bos taurus
brenda
Porter, D.W.; Baskin, S.I.
The effect of three alpha-keto acids on 3-mercaptopyruvate sulfurtransferase activity
J. Biochem. Toxicol.
11
45-50
1996
Bos taurus
brenda
Spallarossa, A.; Forlani, F.; Carpen, A.; Armirotti, A.; Pagani, S.; Bolognesi, M.; Bordo, D.
The "rhodanese" fold and catalytic mechanism of 3-mercaptopyruvate sulfurtransferases: Crystal structure of SseA from Escherichia coli
J. Mol. Biol.
335
583-593
2004
Escherichia coli (P31142)
brenda
Williams, R.A.; Kelly, S.M.; Mottram, J.C.; Coombs, G.H.
3-Mercaptopyruvate sulfurtransferase of Leishmania contains an unusual C-terminal extension and is involved in thioredoxin and antioxidant metabolism
J. Biol. Chem.
278
1480-1486
2003
Leishmania major (Q7K9G0), Leishmania major, Leishmania mexicana (Q8T381), Leishmania mexicana
brenda
Nagahara, N.; Sawada, N.; Nakagawa, T.
Affinity labeling of a catalytic site, cysteine(247), in rat mercaptopyruvate sulfurtransferase by chloropyruvate as an analog of a substrate
Biochimie
86
723-729
2004
Rattus norvegicus
brenda
Nagahara, N.; Katayama, A.
Post-translational regulation of mercaptopyruvate sulfurtransferase via a low redox potential cysteine-sulfenate in the maintenance of redox homeostasis
J. Biol. Chem.
280
34569-34576
2005
Rattus norvegicus
brenda
Wrobel, M.; Jurkowska, H.
Menadione effect on L-cysteine desulfuration in U373 cells
Acta Biochim. Pol.
54
407-411
2007
Homo sapiens
brenda
Iciek, M.; Marcinek, J.; Mleczko, U.; Wlodek, L.
Selective effects of diallyl disulfide, a sulfane sulfur precursor, in the liver and Ehrlich ascites tumor cells
Eur. J. Pharmacol.
569
1-7
2007
Mus musculus
brenda
Nagahara, N.; Yoshii, T.; Abe, Y.; Matsumura, T.
Thioredoxin-dependent enzymatic activation of mercaptopyruvate sulfurtransferase. An intersubunit disulfide bond serves as a redox switch for activation
J. Biol. Chem.
282
1561-1569
2007
Rattus norvegicus, Rattus norvegicus (P97532)
brenda
Billaut-Laden, I.; Rat, E.; Allorge, D.; Crunelle-Thibaut, A.; Cauffiez, C.; Chevalier, D.; Lo-Guidice, J.M.; Broly, F.
Evidence for a functional genetic polymorphism of the human mercaptopyruvate sulfurtransferase (MPST), a cyanide detoxification enzyme
Toxicol. Lett.
165
101-111
2006
Homo sapiens
brenda
Wrobel, M.; Lewandowska, I.; Bronowicka-Adamska, P.; Paszewski, A.
The level of sulfane sulfur in the fungus Aspergillus nidulans wild type and mutant strains
Amino Acids
37
565-571
2008
Aspergillus nidulans
brenda
Shibuya, N.; Tanaka, M.; Yoshida, M.; Ogasawara, Y.; Togawa, T.; Ishii, K.; Kimura, H.
3-Mercaptopyruvate sulfurtransferase produces hydrogen sulfide and bound sulfane sulfur in the brain
Antioxid. Redox Signal.
11
703-714
2009
Mus musculus (Q99J99)
brenda
Nagahara, N.
A novel mercaptopyruvate sulfurtransferase thioredoxin-dependent redox-sensing molecular switch: a mechanism for the maintenance of cellular redox equilibrium
Mini Rev. Med. Chem.
8
585-589
2008
Rattus norvegicus (P97532)
brenda
Shibuya, N.; Mikami, Y.; Kimura, Y.; Nagahara, N.; Kimura, H.
Vascular endothelium expresses 3-mercaptopyruvate sulfurtransferase and produces hydrogen sulfide
J. Biochem.
146
623-626
2009
Rattus norvegicus
brenda
Westrop, G.D.; Georg, I.; Coombs, G.H.
The mercaptopyruvate sulfurtransferase of Trichomonas vaginalis links cysteine catabolism to the production of thioredoxin persulfide
J. Biol. Chem.
284
33485-33494
2009
Trichomonas vaginalis
brenda
Jurkowska, H.; Placha, W.; Nagahara, N.; Wrobel, M.
The expression and activity of cystathionine-gamma-lyase and 3-mercaptopyruvate sulfurtransferase in human neoplastic cell lines
Amino Acids
41
151-158
2011
Homo sapiens
brenda
Nagahara, N.
Regulation of mercaptopyruvate sulfurtransferase activity via intrasubunit and intersubunit redox-sensing switches
Antioxid. Redox Signal.
19
1792-1802
2013
Mus musculus, Rattus norvegicus
brenda
Mikami, Y.; Shibuya, N.; Ogasawara, Y.; Kimura, H.
Hydrogen sulfide is produced by cystathionine gamma-lyase at the steady-state low intracellular Ca2+ concentrations
Biochem. Biophys. Res. Commun.
431
131-135
2013
Rattus norvegicus
brenda
Modis, K.; Asimakopoulou, A.; Coletta, C.; Papapetropoulos, A.; Szabo, C.
Oxidative stress suppresses the cellular bioenergetic effect of the 3-mercaptopyruvate sulfurtransferase/hydrogen sulfide pathway
Biochem. Biophys. Res. Commun.
433
401-407
2013
Mus musculus
brenda
Mikami, Y.; Shibuya, N.; Kimura, Y.; Nagahara, N.; Ogasawara, Y.; Kimura, H.
Thioredoxin and dihydrolipoic acid are required for 3-mercaptopyruvate sulfurtransferase to produce hydrogen sulfide
Biochem. J.
439
479-485
2011
Mus musculus
brenda
Tanizawa, K.
Production of H2S by 3-mercaptopyruvate sulphurtransferase
J. Biochem.
149
357-359
2011
Homo sapiens
brenda
Yadav, P.K.; Yamada, K.; Chiku, T.; Koutmos, M.; Banerjee, R.
Structure and kinetic analysis of H2S production by human mercaptopyruvate sulfurtransferase
J. Biol. Chem.
288
20002-20013
2013
Homo sapiens (P25325), Homo sapiens
brenda
Modis, K.; Coletta, C.; Erdelyi, K.; Papapetropoulos, A.; Szabo, C.
Intramitochondrial hydrogen sulfide production by 3-mercaptopyruvate sulfurtransferase maintains mitochondrial electron flow and supports cellular bioenergetics
FASEB J.
27
601-611
2013
Mus musculus (Q99J99), Mus musculus
brenda
Singh, P.; Rao, P.; Bhattacharya, R.
Dose and time-dependent effects of cyanide on thiosulfate sulfurtransferase, 3-mercaptopyruvate sulfurtransferase, and cystathionine lambda-lyase activities
J. Biochem. Mol. Toxicol.
27
499-507
2013
Mus musculus (Q99J99)
brenda
Fraesdorf, B.; Radon, C.; Leimkuehler, S.
Characterization and interaction studies of two isoforms of the dual localized 3-mercaptopyruvate sulfurtransferase TUM1 from humans
J. Biol. Chem.
289
34543-34556
2014
Homo sapiens (P25325), Homo sapiens
brenda
Miyamoto, R.; Otsuguro, K.; Yamaguchi, S.; Ito, S.
Contribution of cysteine aminotransferase and mercaptopyruvate sulfurtransferase to hydrogen sulfide production in peripheral neurons
J. Neurochem.
130
29-40
2014
Rattus norvegicus (P97532)
brenda
Nagahara, N.; Nagano, M.; Ito, T.; Suzuki, H.
Redox regulation of mammalian 3-mercaptopyruvate sulfurtransferase
Methods Enzymol.
554
229-254
2015
Rattus norvegicus (P97532)
brenda
Zhao, H.; Chan, S.J.; Ng, Y.K.; Wong, P.T.
Brain 3-mercaptopyruvate sulfurtransferase (3MST): cellular localization and downregulation after acute stroke
PLoS ONE
8
e67322
2013
Rattus norvegicus (P97532)
brenda
Nagahara, N.; Nagano, M.; Ito, T.; Shimamura, K.; Akimoto, T.; Suzuki, H.
Antioxidant enzyme, 3-mercaptopyruvate sulfurtransferase-knockout mice exhibit increased anxiety-like behaviors: a model for human mercaptolactate-cysteine disulfiduria
Sci. Rep.
3
1986
2013
Mus musculus (Q99J99)
brenda
Kimura, Y.; Toyofuku, Y.; Koike, S.; Shibuya, N.; Nagahara, N.; Lefer, D.; Ogasawara, Y.; Kimura, H.
Identification of H2S3 and H2S produced by 3-mercaptopyruvate sulfurtransferase in the brain
Sci. Rep.
5
14774
2015
Mus musculus (Q99J99)
brenda
Lec, J.; Boutserin, S.; Mazon, H.; Mulliert, G.; Boschi-Muller, S.; Talfournier, F.
Unraveling the mechanism of cysteine persulfide formation catalyzed by 3-mercaptopyruvate sulfurtransferases
ACS Catal.
8
2049-2059
2018
Escherichia coli, Homo sapiens (P25325), Escherichia coli DH5alpha
-
brenda
Nagahara, N.; Koike, S.; Nirasawa, T.; Kimura, H.; Ogasawara, Y.
Alternative pathway of H2S and polysulfides production from sulfurated catalytic-cysteine of reaction intermediates of 3-mercaptopyruvate sulfurtransferase
Biochem. Biophys. Res. Commun.
496
648-653
2018
Rattus norvegicus (P97532)
brenda
Panagaki, T.; Randi, E.B.; Szabo, C.
Role of 3-mercaptopyruvate sulfurtransferase in the regulation of proliferation and cellular bioenergetics in human Down syndrome fibroblasts
Biomolecules
10
653
2020
Homo sapiens (P25325), Homo sapiens
brenda
Abdollahi Govar, A.; Toero, G.; Szaniszlo, P.; Pavlidou, A.; Bibli, S.I.; Thanki, K.; Resto, V.A.; Chao, C.; Hellmich, M.R.; Szabo, C.; Papapetropoulos, A.; Modis, K.
3-Mercaptopyruvate sulfurtransferase supports endothelial cell angiogenesis and bioenergetics
Br. J. Pharmacol.
177
866-883
2020
Homo sapiens (P25325), Homo sapiens
brenda
Zuhra, K.; Tome, C.S.; Masi, L.; Giardina, G.; Paulini, G.; Malagrino, F.; Forte, E.; Vicente, J.B.; Giuffre, A.
N-acetylcysteine serves as substrate of 3-mercaptopyruvate sulfurtransferase and stimulates sulfide metabolism in colon cancer cells
Cells
8
828
2019
Homo sapiens (P25325), Homo sapiens
brenda
Wang, J.; Guo, X.; Li, H.; Qi, H.; Qian, J.; Yan, S.; Shi, J.; Niu, W.
Hydrogen sulfide from cysteine desulfurase, not 3-mercaptopyruvate sulfurtransferase, contributes to sustaining cell growth and bioenergetics in E. coli under anaerobic conditions
Front. Microbiol.
10
2357
2019
Escherichia coli, Escherichia coli BW25113
brenda
Bronowicka-Adamska, P.; Bentke, A.; Lasota, M.; Wrobel, M.
Effect of S-allyl-L-cysteine on MCF-7 cell line 3-mercaptopyruvate sulfurtransferase/sulfane sulfur system, viability and apoptosis
Int. J. Mol. Sci.
21
1090
2020
Homo sapiens (P25325), Homo sapiens
brenda
Yadav, P.; Vitvitsky, V.; Carballal, S.; Seravalli, J.; Banerjee, R.
Thioredoxin regulates human mercaptopyruvate sulfurtransferase at physiologically-relevant concentrations
J. Biol. Chem.
295
6299-6310
2020
Homo sapiens (P25325), Homo sapiens, Mus musculus (Q99J99), Mus musculus
brenda
Tomita, M.; Nagahara, N.; Ito, T.
Expression of 3-mercaptopyruvate sulfurtransferase in the mouse
Molecules
21
1707
2016
Mus musculus (Q99J99), Mus musculus
brenda
Hoefler, S.; Lorenz, C.; Busch, T.; Brinkkoetter, M.; Tohge, T.; Fernie, A.R.; Braun, H.P.; Hildebrandt, T.M.
Dealing with the sulfur part of cysteine four enzymatic steps degrade l-cysteine to pyruvate and thiosulfate in Arabidopsis mitochondria
Physiol. Plant.
157
352-366
2016
Arabidopsis thaliana (O64530)
brenda
Kimura, Y.; Koike, S.; Shibuya, N.; Lefer, D.; Ogasawara, Y.; Kimura, H.
3-Mercaptopyruvate sulfurtransferase produces potential redox regulators cysteine- and glutathione-persulfide (Cys-SSH and GSSH) together with signaling molecules H2S2, H2S3 and H2S
Sci. Rep.
7
10459
2017
Mus musculus (Q99J99)
brenda
Hanaoka, K.; Sasakura, K.; Suwanai, Y.; Toma-Fukai, S.; Shimamoto, K.; Takano, Y.; Shibuya, N.; Terai, T.; Komatsu, T.; Ueno, T.; Ogasawara, Y.; Tsuchiya, Y.; Watanabe, Y.; Kimura, H.; Wang, C.; Uchiyama, M.; Kojima, H.; Okabe, T.; Urano, Y.; Shimizu, T.; Nagano, T.
Discovery and mechanistic characterization of selective inhibitors of H2S-producing enzyme 3-mercaptopyruvate sulfurtransferase (3MST) targeting active-site cysteine persulfide
Sci. Rep.
7
40227
2017
Homo sapiens (P25325)
brenda
Meza, A.; Cambui, C.; Moreno, A.; Fessel, M.; Balan, A.
Mycobacterium tuberculosis CysA2 is a dual sulfurtransferase with activity against thiosulfate and 3-mercaptopyruvate and interacts with mammalian cells
Sci. Rep.
9
16791
2019
Mycobacterium tuberculosis (P9WHF9), Mycobacterium tuberculosis H37Rv (P9WHF9)
brenda
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