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Literature summary extracted from

  • Nagahara, N.; Yoshii, T.; Abe, Y.; Matsumura, T.
    Thioredoxin-dependent enzymatic activation of mercaptopyruvate sulfurtransferase. An intersubunit disulfide bond serves as a redox switch for activation (2007), J. Biol. Chem., 282, 1561-1569.
    View publication on PubMed

Activating Compound

EC Number Activating Compound Comment Organism Structure
2.8.1.2 1,4-dithiothreitol
-
Rattus norvegicus
2.8.1.2 dithiothreitol activates MST chiefly via reduction of a sulfenyl Cys247 Rattus norvegicus
2.8.1.2 additional information reduced glutathione does not affect MST activity Rattus norvegicus
2.8.1.2 thioredoxin Escherichia coli and rat thioredoxin activate the enzyme to 2.3- and 4.9fold the levels of activation by dithiothreitol-treated and -untreated enzyme, resp. Activation occurs via cleavage of the intersubunit bonds of the enzyme dimer at C154 and C263. Escherichia coli thioredoxin with substitution C35S forms adducts with the enzyme and activates after treatment with dithiotreitol Rattus norvegicus
2.8.1.2 thioredoxin Escherichia coli or rat reduced thioredoxin (Trx) cleaves the intersubunit disulfide bond to activate MST to 2.3- and 4.9fold the levels of activation of dithiothreitol (DTT)-treated and DTT-untreated MST, respectively. An intersubunit disulfide bond serves as a redox switch for enzyme activation Rattus norvegicus

Cloned(Commentary)

EC Number Cloned (Comment) Organism
2.8.1.2 expression in Escherichia coli BL21 (DE3) Rattus norvegicus

Protein Variants

EC Number Protein Variants Comment Organism
2.8.1.2 C154S site-directed mutagenesis, expression in Escherichia coli BL21 (DE3), overexpressed, structurally resembles an active form of MST Rattus norvegicus
2.8.1.2 C254S site-directed mutagenesis, expression in Escherichia coli BL21 (DE3), overexpressed, activation with reduced thioredoxin Rattus norvegicus
2.8.1.2 C263S site-directed mutagenesis, expression in Escherichia coli BL21 (DE3), overexpressed, structurally resembles an active form of MST Rattus norvegicus
2.8.1.2 C64S site-directed mutagenesis, expression in Escherichia coli BL21 (DE3), overexpressed, activation with reduced thioredoxin Rattus norvegicus
2.8.1.2 additional information C154S/C263S mutant, site-directed mutagenesis, expression in Escherichia coli BL21 (DE3), overexpressed, structurally resembles an active form of MST Rattus norvegicus

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
2.8.1.2 32800
-
monomer, gel filtration HPLC analysis, MST exhibits monomer-dimer equilibrium, the monomer to dimer ratio is nearly 9 to 1 in 0.2 M potassium phosphate buffer, pH 7.0 Rattus norvegicus
2.8.1.2 66600
-
dimer, gel filtration HPLC analysis, MST exhibits monomer-dimer equilibrium, the dimer is formed via intersubunit disulfide bond 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 additional information Rattus norvegicus MST contributes to maintain redox homeostasis ?
-
?

Organism

EC Number Organism UniProt Comment Textmining
2.8.1.2 Rattus norvegicus
-
-
-
2.8.1.2 Rattus norvegicus P97532 expression in Escherichia coli BL21 (DE3)
-

Purification (Commentary)

EC Number Purification (Comment) Organism
2.8.1.2
-
Rattus norvegicus

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2.8.1.2 additional information MST contributes to maintain redox homeostasis Rattus norvegicus ?
-
?

Subunits

EC Number Subunits Comment Organism
2.8.1.2 dimer 2*32800, HPLC, MST exhibits monomer-dimer equilibrium, the dimer is formed via intersubunit disulfide bond Rattus norvegicus
2.8.1.2 monomer 32800, HPLC, MST exhibits monomer-dimer equilibrium Rattus norvegicus

Synonyms

EC Number Synonyms Comment Organism
2.8.1.2 3-mercaptopyruvate sulfurtransferase
-
Rattus norvegicus
2.8.1.2 mercaptopyruvate sulfurtransferase
-
Rattus norvegicus
2.8.1.2 MST
-
Rattus norvegicus