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Literature summary extracted from

  • Nagahara, N.
    Regulation of mercaptopyruvate sulfurtransferase activity via intrasubunit and intersubunit redox-sensing switches (2013), Antioxid. Redox Signal., 19, 1792-1802.
    View publication on PubMed

Activating Compound

EC Number Activating Compound Comment Organism Structure
2.8.1.2 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 Mus musculus
2.8.1.2 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 Rattus norvegicus

Protein Variants

EC Number Protein Variants Comment Organism
2.8.1.2 C154S active site mutant Mus musculus
2.8.1.2 C154S active site mutant Rattus norvegicus
2.8.1.2 C263S active site mutant Mus musculus
2.8.1.2 C263S active site mutant Rattus norvegicus

Inhibitors

EC Number Inhibitors Comment Organism Structure
2.8.1.2 iodoacetate
-
Mus musculus
2.8.1.2 iodoacetate
-
Rattus norvegicus
2.8.1.2 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 Mus musculus
2.8.1.2 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 Rattus norvegicus

Localization

EC Number Localization Comment Organism GeneOntology No. Textmining
2.8.1.2 cytosol
-
Mus musculus 5829
-
2.8.1.2 cytosol
-
Rattus norvegicus 5829
-
2.8.1.2 mitochondrion
-
Mus musculus 5739
-
2.8.1.2 mitochondrion
-
Rattus norvegicus 5739
-

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
2.8.1.2 32800
-
2 * 32800, calculated from amino acid sequence Mus musculus
2.8.1.2 32800
-
2 * 32800, calculated from amino acid sequence Rattus norvegicus
2.8.1.2 33000
-
2 * 33000, SDS-PAGE Mus musculus
2.8.1.2 33000
-
2 * 33000, SDS-PAGE Rattus norvegicus
2.8.1.2 66600
-
gel filtration Mus musculus
2.8.1.2 66600
-
gel filtration Rattus norvegicus

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
2.8.1.2 3-mercaptopyruvate + cyanide Mus musculus
-
pyruvate + thiocyanate
-
?
2.8.1.2 3-mercaptopyruvate + cyanide Rattus norvegicus
-
pyruvate + thiocyanate
-
?

Organism

EC Number Organism UniProt Comment Textmining
2.8.1.2 Mus musculus
-
-
-
2.8.1.2 Rattus norvegicus
-
-
-

Source Tissue

EC Number Source Tissue Comment Organism Textmining
2.8.1.2 liver
-
Mus musculus
-
2.8.1.2 liver
-
Rattus norvegicus
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2.8.1.2 3-mercaptopyruvate + cyanide
-
Mus musculus pyruvate + thiocyanate
-
?
2.8.1.2 3-mercaptopyruvate + cyanide
-
Rattus norvegicus pyruvate + thiocyanate
-
?
2.8.1.2 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 Mus musculus ?
-
?
2.8.1.2 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 Rattus norvegicus ?
-
?

Subunits

EC Number Subunits Comment Organism
2.8.1.2 homodimer 2 * 33000, SDS-PAGE Mus musculus
2.8.1.2 homodimer 2 * 33000, SDS-PAGE Rattus norvegicus
2.8.1.2 homodimer 2 * 32800, calculated from amino acid sequence Mus musculus
2.8.1.2 homodimer 2 * 32800, calculated from amino acid sequence Rattus norvegicus

Synonyms

EC Number Synonyms Comment Organism
2.8.1.2 mercaptopyruvate sulfurtransferase
-
Mus musculus
2.8.1.2 mercaptopyruvate sulfurtransferase
-
Rattus norvegicus
2.8.1.2 MST
-
Mus musculus
2.8.1.2 MST
-
Rattus norvegicus

General Information

EC Number General Information Comment Organism
2.8.1.2 malfunction mercaptolactate-cysteine disulfiduria is caused by enzyme defect with or without mental retardation Mus musculus
2.8.1.2 physiological function the enzyme serves not only as an enzyme in cysteine catabolism, but also as an antioxidant protein Mus musculus
2.8.1.2 physiological function the enzyme serves not only as an enzyme in cysteine catabolism, but also as an antioxidant protein Rattus norvegicus