Any feedback?
Information on EC 2.8.1.2 - 3-mercaptopyruvate sulfurtransferase and Organism(s) Mus musculus and UniProt Accession Q99J99
for references in articles please use BRENDA:EC2.8.1.2Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
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).
Specify your search results
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: Mus musculus
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 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
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 + cyanide
pyruvate + thiocyanate
-
-
-
?
3-mercaptopyruvate + thioredoxin
pyruvate + persulfurated thioredoxin
-
-
-
?
thiosulfate + [3-mercaptopyruvate sulfurtransferase]-L-cysteine
sulfate + [3-mercaptopyruvate sulfurtransferase]-S-sulfanyl-L-cysteine
-
-
-
?
additional information
?
-
3-mercaptopyruvate sulfurtransferase produces bound sulfane sulfur
-
-
?
additional information
?
-
the enzyme 3MST also produces H2S2 and H2S5 from 3-mercaptopyruvate. H2S3 production from H2S occurs by the enzyme rhodanese
-
-
?
additional information
?
-
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
-
-
-
additional information
?
-
-
in the catalytic process of the enzyme, hydrogen peroxide is possibly produced by persulfide of the sulfur-accepted substrate and sulfur oxides are possibly produced in the redox cycle of persulfide formed at the catalytic site cysteine of the reaction intermediate
-
-
?
additional information
?
-
-
the enzyme produces hydrogen sulfide in the presence of both cysteine and 2-oxoglutarate. Thioredoxin and dihydrolipoic acid associate with 3-mercaptopyruvate sulfurtransferase to produce hydrogen sulfide. Other reducing substances, such as NADPH, NADH, GSH, cysteine and CoA, do not have any effect on the reaction
-
-
?
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 + cyanide
pyruvate + thiocyanate
-
-
-
?
additional information
?
-
3-mercaptopyruvate sulfurtransferase produces bound sulfane sulfur
-
-
?
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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)
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
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
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
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
low protein expression level, bronchiolar cells are preferentially stained
additional information
high protein expression level, neural and glial cells are positively stained
high protein expression level, hepatocytes around central veins are more strongly stained
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
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
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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
physiological function
malfunction
-
mercaptolactate-cysteine disulfiduria is caused by enzyme defect with or without mental retardation
physiological function
-
the enzyme serves not only as an enzyme in cysteine catabolism, but also as an antioxidant protein
metabolism
the enzyme functions as an antioxidant protein and can produce H2S (or HS2) and SOx
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
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
histological observation reveals no remarkable findings in MST gene-deficient mice
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_MOUSE
297
0
33097
Swiss-Prot
Mitochondrion (Reliability: 4)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
homodimer
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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
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
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
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
OXIDATION STABILITY
ORGANISM
UNIPROT
LITERATURE
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
the hepatic and renal enzyme activity increases by 0.5 LD50 potassium cyanide. Elevated renal cyanide level is also accompanied by increased enzyme activity
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
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
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)
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
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
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
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
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)
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)
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)
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
Tomita, M.; Nagahara, N.; Ito, T.
Expression of 3-mercaptopyruvate sulfurtransferase in the mouse
Molecules
21
1707
2016
Mus musculus (Q99J99), Mus musculus
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)
EXTERNAL LINKS (specific for EC-Number 2.8.1.2)
Use of this online version of BRENDA is free under the CC BY 4.0 license. See terms of use for full details.
Release 2023.1 (January 2023)
Legal
Curated at
Member of
