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Information on EC 2.8.1.2 - 3-mercaptopyruvate sulfurtransferase and Organism(s) Rattus norvegicus and UniProt Accession P97532
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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
-
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: Rattus norvegicus
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
-
-
-
-
beta-mercaptopyruvate sulfurtransferase
-
-
-
-
beta-mercaptopyruvate trans-sulfurase
-
-
-
-
SseA
-
-
-
-
sulfurtransferase, 3-mercaptopyruvate
-
-
-
-
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
3-mercaptopyruvate + reduced thioredoxin = pyruvate + hydrogen sulfide + oxidized thioredoxin
mechanism
-
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
3-mercaptopyruvate + cyanide
pyruvate + thiocyanate
-
-
-
?
3-mercaptopyruvate + thioredoxin
pyruvate + persulfurated thioredoxin
-
-
-
?
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
-
-
-
-
?
additional information
?
-
-
MST contributes to maintain redox homeostasis
-
-
?
additional information
?
-
MST contributes to maintain redox homeostasis
-
-
?
additional information
?
-
MST contributes to maintain redox homeostasis via exerting control over cysteine catabolism
-
-
?
additional information
?
-
after prolonged incubation of MST with thiosulfate, a trisulfide adduct becomes predominant at the sulfurated catalytic-site cysteine. When these adducts are reduced by Trx with reducing system H2S2 first appears, and then H2S and H2S3
-
-
-
additional information
?
-
-
role in metabolism of some amino acids and low molecular weight sulfur compounds
-
-
?
additional information
?
-
-
3MST and cytosolic and mitochondrial cysteine aminotransferases are localized to endothelial cells of the thoracic aorta and together enzymes produce H2S in this cell type. H2S is a smooth muscle relaxant released from endothelium
-
-
?
additional information
?
-
-
in the catalytic process of the enzyme, hydrogen peroxide is possibly produced by persulfide of the sulfur-accepted substrate and sulfur oxides are possibly produced in the redox cycle of persulfide formed at the catalytic site cysteine of the reaction intermediate
-
-
?
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
-
-
-
?
3-mercaptopyruvate + thioredoxin
pyruvate + persulfurated thioredoxin
-
-
-
?
3-mercaptopyruvate + cyanide
pyruvate + thiocyanate
-
-
-
-
?
additional information
?
-
-
MST contributes to maintain redox homeostasis
-
-
?
additional information
?
-
MST contributes to maintain redox homeostasis
-
-
?
additional information
?
-
MST contributes to maintain redox homeostasis via exerting control over cysteine catabolism
-
-
?
additional information
?
-
-
role in metabolism of some amino acids and low molecular weight sulfur compounds
-
-
?
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
-
-
?
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
3-Chloropyruvate
-
one-on-one manner of inactivation, pseudo first-order kinetics
hydrogen peroxide
-
together with stoichiometric concentration of tetrathionate, renaturation by dithiothreitol or thioredoxin. Excess molar ratio of hydrogen peroxide inactivates
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
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
dithiothreitol
activates MST chiefly via reduction of a sulfenyl Cys247
thioredoxin
a low redox potential sulfenate is reversibly formed at a catalytic site cysteine so as to inhibit MST, and thioredoxin-dependent reduction of the sulfenate restored the MST activity
thioredoxin
an intermolecular disulfide bond serves as a thioredoxin-dependent redox-sensing switch for the regulation of the enzymatic activity of 3-mercaptopyruvate sulfurtransferase. A cysteine residue on the surface of each subunit is oxidized to form an intersubunit disulfide bond so as to decrease MST activity, and thioredoxin-specific conversion of a dimer to a monomer increased MST acitvity
thioredoxin
Escherichia coli or rat reduced thioredoxin (Trx) cleaves the intersubunit disulfide bond to activate MST to 2.3- and 4.9fold the levels of activation of dithiothreitol (DTT)-treated and DTT-untreated MST, respectively. An intersubunit disulfide bond serves as a redox switch for enzyme activation
thioredoxin
Escherichia coli and rat thioredoxin activate the enzyme to 2.3- and 4.9fold the levels of activation by dithiothreitol-treated and -untreated enzyme, resp. Activation occurs via cleavage of the intersubunit bonds of the enzyme dimer at C154 and C263. Escherichia coli thioredoxin with substitution C35S forms adducts with the enzyme and activates after treatment with dithiotreitol
thioredoxin
-
rat-reduced thioredoxin activates the enzyme 2.3fold after treatment with dithiothreitol, but dithiothreitol does not increase enzyme activity. The Escherichia coli thioredoxin-thioredoxin reductase-NADPH system more effectively increases enzyme activity to 4.5fold that of the control than the rat thioredoxin-thioredoxin reductase-NADPH system, which increases enzyme activity to 3fold that of the control
additional information
-
reduced glutathione does not affect MST activity
-
additional information
reduced glutathione does not affect MST activity
-
additional information
reduced glutathione does not affect MST activity
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
-
3MST and cytosolic and mitochondrial cysteine aminotransferases are localized to endothelial cells of the thoracic aorta
-
3MST and cytosolic and mitochondrial cysteine aminotransferases are localized to endothelial cells of the thoracic aorta
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
-
highest activity in the matrix, followed by intramembrane space, low activity in inner and outer membrane
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
metabolism
the enzyme is, together with cysteine aminotransferase, primarily responsible for H2S production in peripheral neurons
physiological function
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
-
the enzyme serves not only as an enzyme in cysteine catabolism, but also as an antioxidant protein
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_RAT
297
0
32940
Swiss-Prot
Mitochondrion (Reliability: 4)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
32800
66600
34000
34500
-
two peaks with molecular masses of 34500 Da and 53500 Da, enzyme exists as a monomer and homodimer, gel filtration
53000
-
two peaks with molecular masses of 34500 Da and 53500 Da, enzyme exists as a monomer and homodimer, gel filtration
32800
monomer, gel filtration HPLC analysis, MST exhibits monomer-dimer equilibrium, the monomer to dimer ratio is nearly 9 to 1 in 0.2 M potassium phosphate buffer, pH 7.0
32800
monomer, HPLC analysis, MST exhibits monomer-dimer equilibrium, monomer to dimer ratio is nearly 9 to 1 in 0.2 M potassium phosphate buffer, pH 7.0
66600
dimer, gel filtration HPLC analysis, MST exhibits monomer-dimer equilibrium, the dimer is formed via intersubunit disulfide bond
66600
dimer, HPLC analysis, MST exhibits monomer-dimer equilibrium, the dimer is formed via intersubunit disulfide bond, inactive form
34000
-
1 * 34000, enzyme exists as a monomer and homodimer, SDS-PAGE, gel filtration
34000
-
2 * 34000, enzyme exists as a monomer and homodimer, SDS-PAGE, gel filtration
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
dimer
dimer
-
2 * 34000, enzyme exists as a monomer and homodimer, SDS-PAGE, gel filtration
homodimer
monomer
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
monomer
-
1 * 34000, enzyme exists as a monomer and homodimer, SDS-PAGE, gel filtration
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
C154S
site-directed mutagenesis, expression in Escherichia coli BL21 (DE3), overexpressed, structurally resembles an active form of MST
C254S
site-directed mutagenesis, expression in Escherichia coli BL21 (DE3), overexpressed, activation with reduced thioredoxin
C263S
site-directed mutagenesis, expression in Escherichia coli BL21 (DE3), overexpressed, structurally resembles an active form of MST
C32S
mutant lacks formation of a disulfide bond with a protein and is not able to produce H2Sn
C64S
site-directed mutagenesis, expression in Escherichia coli BL21 (DE3), overexpressed, activation with reduced thioredoxin
C154S
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
C263S
C64S
-
SH group titration, susceptibility to hydrogen peroxide and tetrathionate and renaturation by dithiothreitol similar to wild-type
R196G
additional information
C154S
-
SH group titration, susceptibility to hydrogen peroxide and tetrathionate and renaturation by dithiothreitol similar to wild-type
C263S
-
SH group titration, susceptibility to hydrogen peroxide and tetrathionate and renaturation by dithiothreitol similar to wild-type
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
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
very unstable, spontanous inactivation can be partly prevented by glycerol
-
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
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
RENATURED/Commentary
ORGANISM
UNIPROT
LITERATURE
enzyme inhibited by hydrogen peroxide together with stoichiometric concentration of tetrathionate, complete renaturation by dithiothreitol or thioredoxin
-
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Van den Hamer, C.J.A.; morell, A.G.; Scheinberg, I.H.
A study of the cooper content of beta-mercaptopyruvate trans-sulfurase
J. Biol. Chem.
242
2514-2516
1967
Rattus norvegicus
Wlodek, L.; Ostrowski, W.S.
3-Mercaptopyruvate sulphurtransferase from rat erythrocytes
Acta Biochim. Pol.
29
121-133
1982
Rattus norvegicus
Kasperczyk, H.; Koj, A.; Wasylewski, Z.
Similarity of some molecular and catalytic parameters of mitochondrial and cytosolic mercaptopyruvate sulfurtransferase from rat liver
Bull. Acad. Pol. Sci. Biol. Sci.
25
7-13
1977
Rattus norvegicus
Koj, A.; Frendo, J.; Wojtczak, L.
Subcellular distribution and intramitochondrial localization of three sulfurtransferases in rat liver
FEBS Lett.
57
42-46
1975
Rattus norvegicus, Rattus norvegicus Wistar
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
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
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)
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
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
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
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)
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)
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
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
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
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)
Nagahara, N.; Nagano, M.; Ito, T.; Suzuki, H.
Redox regulation of mammalian 3-mercaptopyruvate sulfurtransferase
Methods Enzymol.
554
229-254
2015
Rattus norvegicus (P97532)
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)
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)
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