Information on EC 2.8.1.2 - 3-mercaptopyruvate sulfurtransferase

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The expected taxonomic range for this enzyme is: Eukaryota, Bacteria

EC NUMBER
COMMENTARY hide
2.8.1.2
-
RECOMMENDED NAME
GeneOntology No.
3-mercaptopyruvate sulfurtransferase
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
3-mercaptopyruvate + cyanide = pyruvate + thiocyanate
show the reaction diagram
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
sulfur atom transfer
-
-
-
-
PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
Cysteine and methionine metabolism
-
-
L-cysteine degradation III
-
-
Metabolic pathways
-
-
cysteine metabolism
-
-
SYSTEMATIC NAME
IUBMB Comments
3-mercaptopyruvate:cyanide sulfurtransferase
Sulfite, sulfinates, mercaptoethanol and mercaptopyruvate can also act as acceptors. The bacterial enzyme is a zinc protein.
CAS REGISTRY NUMBER
COMMENTARY hide
9026-05-5
-
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
SwissProt
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
malfunction
metabolism
physiological function
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
2-mercaptoethanol + cyanide
ethanol + thiocyanate
show the reaction diagram
3-mercaptopyruvate + 2-mercaptoethanol
?
show the reaction diagram
-
-
-
?
3-mercaptopyruvate + 2-mercaptoethanol
pyruvate + ?
show the reaction diagram
-
-
-
-
?
3-mercaptopyruvate + cyanide
H2S + ?
show the reaction diagram
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
show the reaction diagram
3-mercaptopyruvate + dihydrolipoic acid
?
show the reaction diagram
-
-
-
?
3-mercaptopyruvate + dithiothreitol
?
show the reaction diagram
3-mercaptopyruvate + glutathione
?
show the reaction diagram
-
-
-
?
3-mercaptopyruvate + HSO3-
pyruvate + S2O3-
show the reaction diagram
-
-
-
-
?
3-mercaptopyruvate + HSO3-
pyruvate + S2O32-
show the reaction diagram
-
-
-
?
3-mercaptopyruvate + L-cysteine
?
show the reaction diagram
-
-
-
?
3-mercaptopyruvate + L-homocysteine
?
show the reaction diagram
-
-
-
?
3-mercaptopyruvate + thioredoxin
?
show the reaction diagram
thioredoxin is the preferred persulfide acceptor
-
-
?
3-mercaptopyruvate + thioredoxin
pyruvate + persulfurated thioredoxin
show the reaction diagram
-
-
-
-
?
3-mercaptopyruvate + thiosulfate
pyruvate + H2S
show the reaction diagram
-
-
-
-
?
cysteine + 2-mercaptoethanol
? + ?
show the reaction diagram
-
-
-
-
?
sulfane sulfur + cyanide
thiocyanate + ?
show the reaction diagram
thioredoxin + 2-mercaptoethanol
thioredoxin persulfide + ?
show the reaction diagram
-
-
-
-
?
thiosulfate + 2-mercaptoethanol
sulfate + ?
show the reaction diagram
-
-
-
-
?
thiosulfate + cyanide
SO32- + thiocyanate
show the reaction diagram
-
-
-
-
?
thiosulfate + thioredoxin
?
show the reaction diagram
additional information
?
-
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
3-mercaptopyruvate + cyanide
H2S + ?
show the reaction diagram
Q99J99
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
show the reaction diagram
3-mercaptopyruvate + HSO3-
pyruvate + S2O32-
show the reaction diagram
Q99J99
-
-
-
?
3-mercaptopyruvate + thioredoxin
pyruvate + persulfurated thioredoxin
show the reaction diagram
-
-
-
-
?
thiosulfate + cyanide
SO32- + thiocyanate
show the reaction diagram
-
-
-
-
?
additional information
?
-
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
K2SO4
-
0.02 M, 70% activation
KCl
-
0.02 M, 70% activation
Na2SO4
-
0.02 M, 70% activation
additional information
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
2-mercaptoethanol
-
high concentrations
2-mercaptopropionic acid
-
uncompetitive inhibitor with respect to 3-mercaptopyruvate
2-oxobutyrate
-
uncompetitive inhibition
3-Chloropyruvate
-
one-on-one manner of inactivation, pseudo first-order kinetics
3-Mercaptopropionic acid
-
non-competitive inhibitor
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
cysteamine
-
slight
cysteine
-
-
dithiothreitol
-
inhibits from 3 mM to 4 mM at a 3-mercaptopyruvate concentration of 15 mM
ethylene
-
fumigation with ethylene decreases activity to less than 50%
glutathione
-
-
hydrogen peroxide
iodoacetate
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
Mercaptosuccinamic acid
-
slight
N-alpha-4-tosyl-L-lysine chloromethyl ketone
-
interferes with Ser-255, 50% inhibition at 0.044 mM
phenylmethanesulfonyl chloride
-
50% inhibition at 0.7 mM
pyruvate
sulfite
-
H2S production by the enzyme is suppressed by sulfite
tetrathionate
thioglycolic acid
-
slight
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
1,4-dithiothreitol
-
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
thioredoxin
additional information
-
reduced glutathione does not affect MST activity
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
19 - 155
2-mercaptoethanol
0.02 - 73
3-Mercaptopyruvate
4.45 - 6
cyanide
8.2
cysteine
-
pH 8.4, 30C
4.4
Dihydrolipoic acid
-
in 200 mM of HEPES, pH 7.4, at 37C
2.59 - 4.6
dithiothreitol
28
glutathione
-
in 200 mM of HEPES, pH 7.4, at 37C
4.1
L-cysteine
-
in 200 mM of HEPES, pH 7.4, at 37C
12.5
L-homocysteine
-
in 200 mM of HEPES, pH 7.4, at 37C
0.3
reduced thioredoxin
pH 7.3, 37C
0.0025 - 0.0028
thioredoxin
1.7 - 266
thiosulfate
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
229 - 5310
2-mercaptoethanol
0.0783 - 2260
3-Mercaptopyruvate
2.4
cyanide
Homo sapiens
-
in 200 mM of HEPES, pH 7.4, at 37C
2240
cysteine
Trichomonas vaginalis
-
pH 8.4, 30C
1.7
Dihydrolipoic acid
Homo sapiens
-
in 200 mM of HEPES, pH 7.4, at 37C
6.1
dithiothreitol
Homo sapiens
-
in 200 mM of HEPES, pH 7.4, at 37C
0.3
glutathione
Homo sapiens
-
in 200 mM of HEPES, pH 7.4, at 37C
1.1
L-cysteine
Homo sapiens
-
in 200 mM of HEPES, pH 7.4, at 37C
0.8
L-homocysteine
Homo sapiens
-
in 200 mM of HEPES, pH 7.4, at 37C
1.3 - 172
thioredoxin
11.3
thiosulfate
Trichomonas vaginalis
-
pH 8.4, 30C
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
2.1 - 390
2-mercaptoethanol
63
6.6 - 35000
3-Mercaptopyruvate
1122
0.4 - 2
cyanide
118
270
cysteine
Trichomonas vaginalis
-
pH 8.4, 30C
153
0.39
Dihydrolipoic acid
Homo sapiens
-
in 200 mM of HEPES, pH 7.4, at 37C
3464
1.3 - 7.8
dithiothreitol
45
0.01
glutathione
Homo sapiens
-
in 200 mM of HEPES, pH 7.4, at 37C
44
0.27
L-cysteine
Homo sapiens
-
in 200 mM of HEPES, pH 7.4, at 37C
74
0.06
L-homocysteine
Homo sapiens
-
in 200 mM of HEPES, pH 7.4, at 37C
305
520 - 62000
thioredoxin
121
0.0427
thiosulfate
Trichomonas vaginalis
-
pH 8.4, 30C
475
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
3.74 - 20
3-Chloropyruvate
17
3-Mercaptopropionic acid
-
pH 8, 30C
6.1
alpha-Ketobutyrate
-
pH 8, 30C
6.1
alpha-ketoglutarate
-
pH 8, 30C
0.12
hydrogen peroxide
-
pH 7.4, 0C
6.4
pyruvate
-
pH 8, 30C
0.178
tetrathionate
-
pH 7.4, 0C
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
1.74
-
liver, cytosolic fraction
5.26
-
liver, mitochondrial fraction
24.27
-
mitochondrial fraction
232
-
liver enzyme
334
-
-
498
-
erythrocyte enzyme
additional information
-
-
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6.9 - 7.6
9.3 - 9.6
-
-
10.5
-
-
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
-
-
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
45 - 50
-
-
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
45 - 60
-
45-50C: temperature optimum, 60C: no activity
pI VALUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5.1
-
two or three forms
5.5
-
four enzymically active forms
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
-
3MST and cytosolic and mitochondrial cysteine aminotransferases are localized to endothelial cells of the thoracic aorta
Manually annotated by BRENDA team
-
highest expression
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
-
-
-
Manually annotated by BRENDA team
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
10900
-
mitochondria, gel filtration
23800
-
sedimentation equilibrium ultracentrifugation
30000
-
x * 30000, SDS-PAGE
30200
-
cytosol, gel filtration
32700
-
x * 32700, calculated, x * 33000, SDS-PAGE
33000 - 34000
-
gel filtration
34000
-
1 * 34000, enzyme exists as a monomer and homodimer, SDS-PAGE, gel filtration; 2 * 34000, enzyme exists as a monomer and homodimer, SDS-PAGE, gel filtration
34500
-
two peaks with molecular masses of 34500 Da and 53500 Da, enzyme exists as a monomer and homodimer, gel filtration
50000
-
gel filtration
53000
-
two peaks with molecular masses of 34500 Da and 53500 Da, enzyme exists as a monomer and homodimer, gel filtration
60000
-
gel filtration
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
homodimer
monomer
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
sialoprotein
-
219 amino acids and 38 carbohydrate residues
additional information
-
redox state controls enzyme activity
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
sitting drop vapor diffusion method, using 2 M ammonium sulfate, 0.1 M sodium acetate pH 4.5 and 0.02 M betaine hydrochloride
-
hanging drop vapor diffusion method
-
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
-
stabilized in 0.8 M KCl
-
unstable to thawing and refreezing
-
very unstable, spontanous inactivation can be partly prevented by glycerol
-
OXIDATION STABILITY
ORGANISM
UNIPROT
LITERATURE
oxidative stress (0.1-0.5 mM H2O2) inhibits enzyme activity
-
724194
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-20C, stable for at least 12 months without loss of activity
-35C, 50 mM potassium phosphate buffer, pH 7.4, 0.5 mg/ml bovine serum albumin, 50% glycerol, slow decrease of activity
-
4C, no loss of activity after 10 days
-
4C, several days
-
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
glutathione-agarose column chromatography and benzamidine Sepharose column chromatography
-
GST Spin Trap column chromatography
-
GSTrap FF affinity 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
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expressed in COS cells and Escherichia coli BL21 cells
-
expressed in Escherichia coli BL21(DE3) cells
expressed in Escherichia coli BL21(DE3) Codon Plus cells
-
expression in Escherichia coli BL21 (DE3)
liver enzyme
-
transient transfection of human embryonic kidney HEK 293-F cells
wild-type and 4 truncated versions lacking 10, 32, 50 and 70 amino acids at the C-terminus
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
-
ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
C154S
-
active site mutant
C263S
-
active site mutant
C248R
-
slightly increased Km
R178G
-
increased Km
R187G
-
Ki-value for 3-chloropyruvate similar to wild-type
R248G
-
facilitated catalysis of thiosulfate
S249A
-
no significant difference in Km compared to wild-type enzyme
additional information
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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