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2-mercaptoethanol + cyanide
ethanol + thiocyanate
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 + 2-mercaptoethanol
?
-
-
-
?
3-mercaptopyruvate + 2-mercaptoethanol
pyruvate + ?
-
-
-
-
?
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 + dihydrolipoic acid
?
-
-
-
?
3-mercaptopyruvate + dithiothreitol
?
3-mercaptopyruvate + glutathione
?
-
-
-
?
3-mercaptopyruvate + HSO3-
pyruvate + S2O3-
-
-
-
-
?
3-mercaptopyruvate + HSO3-
pyruvate + S2O32-
-
-
-
?
3-mercaptopyruvate + L-cysteine
?
3-mercaptopyruvate + L-homocysteine
?
-
-
-
?
3-mercaptopyruvate + N-acetyl-L-cysteine
?
3-mercaptopyruvate + thioredoxin
?
thioredoxin is the preferred persulfide acceptor
-
-
?
3-mercaptopyruvate + thioredoxin
pyruvate + persulfurated thioredoxin
3-mercaptopyruvate + thiosulfate
pyruvate + H2S
-
-
-
-
?
7-azido-4-methylcoumarin + L-cysteine
?
-
-
-
?
7-azido-4-methylcoumarin + N-acetyl-L-cysteine
?
-
-
-
?
cysteine + 2-mercaptoethanol
? + ?
-
-
-
-
?
sulfane sulfur + cyanide
thiocyanate + ?
thioredoxin + 2-mercaptoethanol
thioredoxin persulfide + ?
-
-
-
-
?
thiosulfate + 2-mercaptoethanol
sulfate + ?
-
-
-
-
?
thiosulfate + cyanide
SO32- + thiocyanate
-
-
-
?
thiosulfate + cyanide
sulfite + thiocyanate
thiosulfate + glutathione
sulfite + glutathione disulfide
-
-
-
?
thiosulfate + 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
additional information
?
-
2-mercaptoethanol + cyanide
ethanol + thiocyanate
-
-
-
-
?
2-mercaptoethanol + cyanide
ethanol + 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 + 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 + 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 + dithiothreitol
?
-
-
-
?
3-mercaptopyruvate + dithiothreitol
?
-
-
-
-
?
3-mercaptopyruvate + dithiothreitol
?
-
-
-
?
3-mercaptopyruvate + L-cysteine
?
-
-
-
?
3-mercaptopyruvate + L-cysteine
?
-
-
-
-
?
3-mercaptopyruvate + L-cysteine
?
-
-
-
?
3-mercaptopyruvate + N-acetyl-L-cysteine
?
-
-
-
?
3-mercaptopyruvate + N-acetyl-L-cysteine
?
-
-
-
?
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
-
-
-
?
3-mercaptopyruvate + thioredoxin
pyruvate + persulfurated thioredoxin
-
-
-
?
sulfane sulfur + cyanide
thiocyanate + ?
-
-
?
sulfane sulfur + cyanide
thiocyanate + ?
-
-
?
thiosulfate + cyanide
sulfite + thiocyanate
-
-
-
?
thiosulfate + cyanide
sulfite + thiocyanate
-
-
-
?
thiosulfate + thioredoxin
?
-
-
-
?
thiosulfate + thioredoxin
?
-
-
-
?
thiosulfate + [3-mercaptopyruvate sulfurtransferase]-L-cysteine
sulfate + [3-mercaptopyruvate sulfurtransferase]-S-sulfanyl-L-cysteine
-
-
-
?
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 sulfurtransferase]-S-sulfanyl-L-cysteine + reduced thioredoxin
hydrogen sulfide + [3-mercaptopyruvate sulfurtransferase]-L-cysteine + oxidized thioredoxin
-
-
-
?
additional information
?
-
-
the enzyme plays a role in iron-sulfur chromophore formation in adrenal cortex
-
-
?
additional information
?
-
-
cyanide detoxification
-
-
?
additional information
?
-
-
participates in L-cysteine desulfuration
-
-
?
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
-
-
?
additional information
?
-
3-mercaptopyruvate sulfurtransferase produces bound sulfane sulfur
-
-
?
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
-
-
?
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
?
-
-
role in metabolism of some amino acids and low molecular weight sulfur compounds
-
-
?
additional information
?
-
-
cyanide detoxification
-
-
?
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
?
-
-
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
?
-
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
?
-
-
has high activity with 3-MP as a sulfur donor and can use several thiol compounds as sulfur acceptor substrates
-
-
?
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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 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
Potential role of the 3-mercaptopyruvate sulfurtransferase (3-MST)-hydrogen sulfide (H2S) pathway in cancer cells.
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.
Glioma
Is development of high-grade gliomas sulfur-dependent?
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 and Polysulfide Signaling.
Neoplasms
Hydrogen Sulfide-Synthesizing Enzymes Are Altered in a Case of Oral Cavity Mucoepidermoid Carcinoma.
Neoplasms
Is development of high-grade gliomas sulfur-dependent?
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.
Obesity
[Adipocytic Endogenous Hydrogen Sulfide-Function,Regulation and Diseases].
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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19 - 155
2-mercaptoethanol
0.015 - 73
3-Mercaptopyruvate
8.2
cysteine
-
pH 8.4, 30°C
4.4
dihydrolipoic acid
in 200 mM of HEPES, pH 7.4, at 37°C
2.59 - 4.6
dithiothreitol
28
glutathione
in 200 mM of HEPES, pH 7.4, at 37°C
12.5
L-homocysteine
in 200 mM of HEPES, pH 7.4, at 37°C
11.4 - 17
N-acetyl-L-cysteine
0.3
reduced thioredoxin
pH 7.3, 37°C
0.0025 - 0.0031
thioredoxin
19
2-mercaptoethanol
-
pH 8.4, 30°C
108
2-mercaptoethanol
in 200 mM of HEPES, pH 7.4, at 37°C
152 - 155
2-mercaptoethanol
-
-
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
0.053
3-Mercaptopyruvate
-
pH 8.4, 30°C
0.13
3-Mercaptopyruvate
using 2-mercaptoethanol as cosubstrate, in 200 mM of HEPES, pH 7.4, at 37°C
0.2
3-Mercaptopyruvate
pH 7.3, 37°C
0.24
3-Mercaptopyruvate
-
mutant S239A, pH 8.0, 30°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
0.43
3-Mercaptopyruvate
-
mutant H66A, pH 8.0, 30°C
0.49
3-Mercaptopyruvate
S249A mutant
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
0.9
3-Mercaptopyruvate
-
mutant R102L, pH 8.0, 30°C
1
3-Mercaptopyruvate
-
wild-type, pH 8.0, 30°C
1
3-Mercaptopyruvate
-
mutant H66A/R102L, pH 8.0, 30°C
1
3-Mercaptopyruvate
-
mutant R102K, pH 8.0, 30°C
1.1
3-Mercaptopyruvate
S249K mutant
1.2
3-Mercaptopyruvate
wild-type enzyme
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
1.4
3-Mercaptopyruvate
-
mutant H66N, pH 8.0, 30°C
1.7
3-Mercaptopyruvate
wild-type, enzyme displays kinetic cooperativity with respect to 3-mercaptopyruvate and thioredoxin, pH 8.0, 30°C
2 - 3
3-Mercaptopyruvate
-
mutant R178L/R187L, pH 8.0, 30°C
2.1
3-Mercaptopyruvate
G248R mutant
2.4
3-Mercaptopyruvate
-
mutant D53A, pH 8.0, 30°C
4
3-Mercaptopyruvate
-
mutant R187L, pH 8.0, 30°C
4.08
3-Mercaptopyruvate
-
pH 8, 30°C
7.02
3-Mercaptopyruvate
pH 8.0, 37°C
7.3
3-Mercaptopyruvate
-
cytosolic enzyme
7.4 - 7.7
3-Mercaptopyruvate
-
-
7.6
3-Mercaptopyruvate
-
mitochondrial enzyme
8.34
3-Mercaptopyruvate
-
determination of pyruvate formation, 37°C, pH 9.55
11
3-Mercaptopyruvate
R196G mutant
11
3-Mercaptopyruvate
MST1, 30°C
12.5
3-Mercaptopyruvate
-
determination of thiocyanate formation, 37°C, pH 9.55
15
3-Mercaptopyruvate
-
mutant R178L, pH 8.0, 30°C
70
3-Mercaptopyruvate
R187G mutant
72
3-Mercaptopyruvate
MST2, 30°C
73
3-Mercaptopyruvate
-
pH 9.6
1.66
cyanide
pH 8.0, 37°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
6
cyanide
in 200 mM of HEPES, pH 7.4, at 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
4.6
dithiothreitol
in 200 mM of HEPES, pH 7.4, at 37°C
3.8
L-cysteine
cytosolic splice variant MPST1, Hill coefficient 1.4, pH 7.4, 37°C
4.1
L-cysteine
in 200 mM of HEPES, pH 7.4, at 37°C
4.5
L-cysteine
mitochondrial splice variant MPST2, Hill coefficient 1.6, pH 7.4, 37°C
6
L-cysteine
pH 8.0, 37°C
11.4
N-acetyl-L-cysteine
pH 8.0, 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
0.0025
thioredoxin
in 200 mM of HEPES, pH 7.4, at 37°C
0.0028
thioredoxin
-
pH 8.4, 30°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
1.7
thiosulfate
pH 7.3, 37°C
266
thiosulfate
-
pH 8.4, 30°C
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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
H66N
-
kinetic properties are identical with those of the wild type
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
S239A
-
strong decrease in kcat value
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
-
H66N
-
kinetic properties are identical with those of the wild type
-
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
C154S
-
active site mutant
C263S
-
active site mutant
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
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
C248R
slightly increased Km
C32S
mutant lacks formation of a disulfide bond with a protein and is not able to produce H2Sn
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
C247S
-
inactive
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
-
inactive
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
R196G
-
the mutant shows reduced H2S-producing activity
C154S
-
active site mutant
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
no enzyme activity
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
-
active site mutant
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
R196G
increased Km
R196G
-
decrease in kcat/Km
R196G
-
5fold increase in Ki-value for 3-chloropyruvate
S249K
-
decrease in kcat/Km
S249K
facilitated catalysis of thiosulfate
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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Role of 3-mercaptopyruvate sulfurtransferase in the regulation of proliferation and cellular bioenergetics in human Down syndrome fibroblasts
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Homo sapiens (P25325), Homo sapiens
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N-acetylcysteine serves as substrate of 3-mercaptopyruvate sulfurtransferase and stimulates sulfide metabolism in colon cancer cells
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Escherichia coli, Escherichia coli BW25113
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Effect of S-allyl-L-cysteine on MCF-7 cell line 3-mercaptopyruvate sulfurtransferase/sulfane sulfur system, viability and apoptosis
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Yadav, P.; Vitvitsky, V.; Carballal, S.; Seravalli, J.; Banerjee, R.
Thioredoxin regulates human mercaptopyruvate sulfurtransferase at physiologically-relevant concentrations
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Tomita, M.; Nagahara, N.; Ito, T.
Expression of 3-mercaptopyruvate sulfurtransferase in the mouse
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Hoefler, S.; Lorenz, C.; Busch, T.; Brinkkoetter, M.; Tohge, T.; Fernie, A.R.; Braun, H.P.; Hildebrandt, T.M.
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Mus musculus (Q99J99)
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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)
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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)
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