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Information on EC 2.8.1.2 - 3-mercaptopyruvate sulfurtransferase
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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 enzyme appears in viruses and cellular organisms
Reaction Schemes
Synonyms
3-mercaptopyruvate sulfurtransferase, 3-mst, mercaptopyruvate sulfurtransferase, 3-mercaptopyruvate sulphurtransferase, 3-mpst, 3-mercaptopyruvate:cyanide sulfurtransferase, beta-mercaptopyruvate sulfurtransferase, 
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
3-mercaptopyruvate sulfurtransferase
3-mercaptopyruvate sulphurtransferase
3-MPST
3-MST
3MST
beta-mercaptopyruvate sulfurtransferase
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-
-
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beta-mercaptopyruvate trans-sulfurase
-
-
-
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CysA2
mercaptopyruvate sulfurtransferase
MPST
MST
Rv0815
SseA
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-
-
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sulfurtransferase, 3-mercaptopyruvate
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-
-
-
additional information
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rhodanese activity, EC 2.8.1.1 is a minor function of human erythrocyte beta-mercaptopyruvate sulfurtransferase
3-MPST
-
-
-
-
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
3-mercaptopyruvate + reduced thioredoxin = pyruvate + hydrogen sulfide + oxidized thioredoxin
3-mercaptopyruvate + [3-mercaptopyruvate sulfurtransferase]-L-cysteine = pyruvate + [3-mercaptopyruvate sulfurtransferase]-S-sulfanyl-L-cysteine
(1a)
-
-
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[3-mercaptopyruvate sulfurtransferase]-S-sulfanyl-L-cysteine + reduced thioredoxin = hydrogen sulfide + [3-mercaptopyruvate sulfurtransferase]-L-cysteine + oxidized thioredoxin
(1b)
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-
-
3-mercaptopyruvate + reduced thioredoxin = pyruvate + hydrogen sulfide + oxidized thioredoxin
mechanism
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3-mercaptopyruvate + reduced thioredoxin = pyruvate + hydrogen sulfide + oxidized thioredoxin
mechanism
3-mercaptopyruvate + reduced thioredoxin = pyruvate + hydrogen sulfide + oxidized thioredoxin
rapid equilibrium-ordered mechanism with 3-mercaptopyruvate as the first substrate
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3-mercaptopyruvate + reduced thioredoxin = pyruvate + hydrogen sulfide + oxidized thioredoxin
sequential formal mechanism
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3-mercaptopyruvate + reduced thioredoxin = pyruvate + hydrogen sulfide + oxidized thioredoxin
when 2-mercaptoethanol is the sulfur acceptor addition of the substrate is random
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3-mercaptopyruvate + reduced thioredoxin = pyruvate + hydrogen sulfide + oxidized thioredoxin
rapid equilibrium-ordered mechanism
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3-mercaptopyruvate + reduced thioredoxin = pyruvate + hydrogen sulfide + oxidized thioredoxin
sulfur transfer mechanism involving C237 as the nucleophilic species and H66, R102 and D262 as residues assisting catalysis
3-mercaptopyruvate + reduced thioredoxin = pyruvate + hydrogen sulfide + oxidized thioredoxin
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
sulfur atom transfer
-
-
-
-
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PATHWAY SOURCE
PATHWAYS
BRENDA
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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).
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CAS REGISTRY NUMBER
COMMENTARY
9026-05-5
-
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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 + 2 glutathione
pyruvate + glutathione disulfide
-
-
-
?
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 + thioredoxin
?
thioredoxin is the preferred persulfide acceptor
-
-
?
thiosulfate + glutathione
sulfite + glutathione disulfide
-
-
-
?
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
-
-
-
-
?
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
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-
-
-
?
3-mercaptopyruvate + thioredoxin
pyruvate + persulfurated thioredoxin
-
-
-
-
?
3-mercaptopyruvate + thioredoxin
pyruvate + persulfurated thioredoxin
-
-
-
-
?
3-mercaptopyruvate + thioredoxin
pyruvate + persulfurated thioredoxin
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-
-
?
3-mercaptopyruvate + thioredoxin
pyruvate + persulfurated thioredoxin
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-
-
?
3-mercaptopyruvate + thioredoxin
pyruvate + persulfurated thioredoxin
-
-
-
?
thiosulfate + [3-mercaptopyruvate sulfurtransferase]-L-cysteine
sulfate + [3-mercaptopyruvate sulfurtransferase]-S-sulfanyl-L-cysteine
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-
-
?
thiosulfate + [3-mercaptopyruvate sulfurtransferase]-L-cysteine
sulfate + [3-mercaptopyruvate sulfurtransferase]-S-sulfanyl-L-cysteine
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-
-
?
[3-mercaptopyruvate sulfurtransferase]-S-sulfanyl-L-cysteine + reduced thioredoxin
hydrogen sulfide + [3-mercaptopyruvate sulfurtransferase]-L-cysteine + oxidized thioredoxin
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-
-
?
[3-mercaptopyruvate sulfurtransferase]-S-sulfanyl-L-cysteine + reduced thioredoxin
hydrogen sulfide + [3-mercaptopyruvate sulfurtransferase]-L-cysteine + oxidized thioredoxin
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-
-
?
additional information
?
-
-
the enzyme plays a role in iron-sulfur chromophore formation in adrenal cortex
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-
?
additional information
?
-
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3-mercaptopyruvate sulfurtransferase in conjunction with cysteine (aspartate) aminotransferase contributes significantly in generating H2S from L-cysteine in the presence of alpha-ketoglutarate
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-
?
additional information
?
-
3-mercaptopyruvate sulfurtransferase produces bound sulfane sulfur
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-
?
additional information
?
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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
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-
?
additional information
?
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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
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-
?
additional information
?
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the enzyme 3MST also produces H2S2 and H2S5 from 3-mercaptopyruvate. H2S3 production from H2S occurs by the enzyme rhodanese
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-
?
additional information
?
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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
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additional information
?
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role in metabolism of some amino acids and low molecular weight sulfur compounds
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-
?
additional information
?
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MST contributes to maintain redox homeostasis
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-
?
additional information
?
-
MST contributes to maintain redox homeostasis
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-
?
additional information
?
-
MST contributes to maintain redox homeostasis via exerting control over cysteine catabolism
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-
?
additional information
?
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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
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-
?
additional information
?
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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
?
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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
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-
additional information
?
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role in metabolism of some amino acids and low molecular weight sulfur compounds
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-
?
additional information
?
-
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has high activity with 3-MP as a sulfur donor and can use several thiol compounds as sulfur acceptor substrates
-
-
?
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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 + thioredoxin
pyruvate + persulfurated thioredoxin
-
-
-
?
3-mercaptopyruvate + cyanide
pyruvate + thiocyanate
-
-
-
-
?
3-mercaptopyruvate + cyanide
pyruvate + thiocyanate
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-
-
-
?
3-mercaptopyruvate + cyanide
pyruvate + thiocyanate
-
-
-
?
3-mercaptopyruvate + cyanide
pyruvate + thiocyanate
-
-
-
-
?
3-mercaptopyruvate + cyanide
pyruvate + thiocyanate
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-
-
?
3-mercaptopyruvate + cyanide
pyruvate + thiocyanate
-
-
-
-
?
additional information
?
-
-
the enzyme plays a role in iron-sulfur chromophore formation in adrenal cortex
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-
?
additional information
?
-
3-mercaptopyruvate sulfurtransferase produces bound sulfane sulfur
-
-
?
additional information
?
-
-
role in metabolism of some amino acids and low molecular weight sulfur compounds
-
-
?
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
?
-
-
role in metabolism of some amino acids and low molecular weight sulfur compounds
-
-
?
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Cu2+
Zn2+
additional information
additional information
-
no effect: 0.02 M CdCl2, 0.5 mM arsenite, 0.01 mM copper acetate
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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-mercaptopropionic acid
-
uncompetitive inhibitor with respect to 3-mercaptopyruvate
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-Chloropyruvate
-
one-on-one manner of inactivation, pseudo first-order kinetics
3-[(benzenesulfonyl)amino]benzoic acid
more than 80% inhibition at 0.01 mM
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
dithiothreitol
-
inhibits from 3 mM to 4 mM at a 3-mercaptopyruvate concentration of 15 mM
menadione
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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
N-alpha-4-tosyl-L-lysine chloromethyl ketone
-
interferes with Ser-255, 50% inhibition at 0.044 mM
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
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)
hydrogen peroxide
-
together with stoichiometric concentration of tetrathionate, renaturation by dithiothreitol or thioredoxin. Excess molar ratio of hydrogen peroxide inactivates
pyruvate
-
product inhibition, competitive with 3-mercaptopyruvate and 2-mercaptoethanol
pyruvate
-
uncompetitive inhibitor with respect to 3-mercaptopyruvate, 50% inhibition at 13.1 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
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
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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
dithiothreitol
-
activates from 0.4 mM to 2 mM at a 3-mercaptopyruvate concentration of 0.625 mM, inhibition at 3 mM and 4 mM dithiothreitol
dithiothreitol
activates MST chiefly via reduction of a sulfenyl Cys247