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Information on EC 2.8.1.2 - 3-mercaptopyruvate sulfurtransferase and Organism(s) Homo sapiens
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EC Tree
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
-
gaseous
-
gasotransmitter
-
sulfane
- nahs
- polysulfides
- persulfide
-
cytoprotective
-
h2s-synthesizing
- beta-synthase
-
desulfuration
-
h2s-generating
- d-cysteine
-
gamma-lyase
- analysis
-
trisulfide
-
aminooxyacetic
-
sulfhydration
- medicine
The taxonomic range for the selected organisms is: Homo sapiens
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
Reaction Schemes
hide(Overall reactions are displayed. Show all >>)
Synonyms
3-mercaptopyruvate sulfurtransferase, 3-mst, mercaptopyruvate sulfurtransferase, 3-mercaptopyruvate sulphurtransferase, 3-mpst, 3-mercaptopyruvate:cyanide sulfurtransferase, beta-mercaptopyruvate sulfurtransferase, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
3-MPST
-
-
-
-
3MST
beta-mercaptopyruvate sulfurtransferase
-
-
-
-
beta-mercaptopyruvate trans-sulfurase
-
-
-
-
MPST
SseA
-
-
-
-
sulfurtransferase, 3-mercaptopyruvate
-
-
-
-
additional information
-
rhodanese activity, EC 2.8.1.1 is a minor function of human erythrocyte beta-mercaptopyruvate sulfurtransferase
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
sulfur atom transfer
-
-
-
-
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).
CAS REGISTRY NUMBER
COMMENTARY
9026-05-5
-
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 + thioredoxin
?
thioredoxin is the preferred persulfide acceptor
-
-
?
[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 + thioredoxin
pyruvate + persulfurated thioredoxin
-
-
-
?
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
-
-
?
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
pyruvate + thiocyanate
-
-
-
-
?
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-[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-[(benzenesulfonyl)amino]benzoic acid
more than 80% inhibition at 0.01 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
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
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
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
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
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
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
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
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
SwissProt
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
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
two splice variants of MPST, differing by 20 amino acids at the N-terminus, give rise to the cytosolic MPST1 and mitochondrial MPST2 isoforms
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
metabolism
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
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 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
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). THTM_HUMAN
297
0
33178
Swiss-Prot
Mitochondrion (Reliability: 5)
PDB
SCOP
CATH
UNIPROT
ORGANISM
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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
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
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
glutathione-agarose column chromatography and benzamidine Sepharose column chromatography
Ni-NTA agarose column chromatography and DEAE-Sepharose column chromatography
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli BL21(DE3) cells
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
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
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.
97
1334-1338
1980
Homo sapiens
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
-
Wrobel, M.; Jurkowska, H.
Menadione effect on L-cysteine desulfuration in U373 cells
Acta Biochim. Pol.
54
407-411
2007
Homo sapiens
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
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
Tanizawa, K.
Production of H2S by 3-mercaptopyruvate sulphurtransferase
J. Biochem.
149
357-359
2011
Homo sapiens
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
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
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
-
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
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
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
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
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
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)
EXTERNAL LINKS (specific for EC-Number 2.8.1.2)
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Release 2023.1 (January 2023)
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