EC Number   |
Activating Compound |
Reference |
|---|
    2.8.1.2 | 1,4-dithiothreitol |
- |
674808 |
| 2.8.1.2 | 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 |
673461 |
| 2.8.1.2 | 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 |
645566 |
| 2.8.1.2 | dithiothreitol |
activates MST chiefly via reduction of a sulfenyl Cys247 |
674808, 694056 |
| 2.8.1.2 | more |
reduced glutathione does not affect MST activity |
674808, 694056 |
| 2.8.1.2 | thioredoxin |
a low redox potential sulfenate is reversibly formed at a catalytic site cysteine so as to inhibit MST, and thioredoxin-dependent reduction of the sulfenate restored the MST activity |
694056 |
| 2.8.1.2 | thioredoxin |
an intermolecular disulfide bond serves as a thioredoxin-dependent redox-sensing switch for the regulation of the enzymatic activity of 3-mercaptopyruvate sulfurtransferase. A cysteine residue on the surface of each subunit is oxidized to form an intersubunit disulfide bond so as to decrease MST activity, and thioredoxin-specific conversion of a dimer to a monomer increased MST acitvity |
694056 |
| 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 |
674808 |
| 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 |
674808 |
| 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 |
723958 |
