Publications

• A study of the cooper content of beta-mercaptopyruvate trans-sulfurase.

  Van den Hamer C.J., Morell A.G., Scheinberg I.H.

  J Biol Chem 242:2514-2516(1967) [PubMed] [EuropePMC]

  This publication is cited by 2 other entries.

• Post-translational regulation of mercaptopyruvate sulfurtransferase via a low redox potential cysteine-sulfenate in the maintenance of redox homeostasis.

  Nagahara N., Katayama A.

  3-Mercaptopyruvate sulfurtransferase (MST) (EC 2.8.1.2), a multifunctional enzyme, catalyzes a transsulfuration from mercaptopyruvate to pyruvate in the degradation process of cysteine. A stoichiometric concentration of hydrogen peroxide and of tetrathionate (S(4)O(6)(2-)) inhibited rat MST (k(i) ... >> More

  3-Mercaptopyruvate sulfurtransferase (MST) (EC 2.8.1.2), a multifunctional enzyme, catalyzes a transsulfuration from mercaptopyruvate to pyruvate in the degradation process of cysteine. A stoichiometric concentration of hydrogen peroxide and of tetrathionate (S(4)O(6)(2-)) inhibited rat MST (k(i) = 3.3 min(-1), K(i) = 120.5 microM and k(i) = 2.5 min(-1), K(i) = 178.6 microM, respectively). The activity was completely restored by dithiothreitol or thioredoxin with a reducing system containing thioredoxin reductase and NADPH, but glutathione did not restore the activity. On the other hand, an excess molar ratio dose of hydrogen peroxide inactivated MST. Oxidation with a stoichiometric concentration of hydrogen peroxide protected the enzyme against reaction by iodoacetate, which modifies a catalytic Cys(247), suggesting that Cys(247) is a target of the oxidants. A matrix-assisted laser desorption/ionization-time-of-flight mass spectrometric analysis revealed that hydrogen peroxide- and tetrathionate-inhibited MSTs were increased in molecular mass consistent with the addition of atomic oxygen and with a thiosulfate (S(2)O(3)(-)), respectively. Treatment with dithiothreitol restored modified MST to the original mass. These findings suggested that there was no nearby cysteine with which to form a disulfide, and mild oxidation of MST resulted in formation of a sulfenate (SO(-)) at Cys(247), which exhibited exceptional stability and a lower redox potential than that of glutathione. Oxidative stress decreases MST activity so as to increase the amount of cysteine, a precursor of thioredoxin or glutathione, and furthermore, these cellular reductants restore the activity. Thus the redox state regulates MST activity at the enzymatic level, and on the other hand, MST controls redox to maintain cellular redox homeostasis. << Less

  J. Biol. Chem. 280:34569-34576(2005) [PubMed] [EuropePMC]

  This publication is cited by 2 other entries.

• Enzymic transfer of sulfur from mercaptopyruvate to sulfate or sulfinates.

  SORBO B.

  Biochim Biophys Acta 24:324-329(1957) [PubMed] [EuropePMC]

  This publication is cited by 2 other entries.

• Thioredoxin and dihydrolipoic acid are required for 3-mercaptopyruvate sulfurtransferase to produce hydrogen sulfide.

  Mikami Y., Shibuya N., Kimura Y., Nagahara N., Ogasawara Y., Kimura H.

  H2S (hydrogen sulfide) has recently been recognized as a signalling molecule as well as a cytoprotectant. We recently demonstrated that 3MST (3-mercaptopyruvate sulfurtransferase) produces H2S from 3MP (3-mercaptopyruvate). Although a reducing substance is required for an intermediate persulfide a ... >> More

  H2S (hydrogen sulfide) has recently been recognized as a signalling molecule as well as a cytoprotectant. We recently demonstrated that 3MST (3-mercaptopyruvate sulfurtransferase) produces H2S from 3MP (3-mercaptopyruvate). Although a reducing substance is required for an intermediate persulfide at the active site of 3MST to release H2S, the substance has not been identified. In the present study we show that Trx (thioredoxin) and DHLA (dihydrolipoic acid) associate with 3MST to release H2S. Other reducing substances, such as NADPH, NADH, GSH, cysteine and CoA, did not have any effect on the reaction. We also show that 3MST produces H2S from thiosulfate. The present study provides a new insight into a mechanism for the production of H2S by 3MST. << Less

  Biochem. J. 439:479-485(2011) [PubMed] [EuropePMC]

  This publication is cited by 2 other entries.

• Enzymatic formation of polysulfides from mercaptopyruvate.

  HYLIN J.W., WOOD J.L.

  J Biol Chem 234:2141-2144(1959) [PubMed] [EuropePMC]

  This publication is cited by 2 other entries.

• Purification and properties of mercaptopyruvate sulfur transferase of Escherichia coli.

  Vachek H., Wood J.L.

  Biochim Biophys Acta 258:133-146(1972) [PubMed] [EuropePMC]

  This publication is cited by 2 other entries.

• 3-Mercaptopyruvate sulfurtransferase produces hydrogen sulfide and bound sulfane sulfur in the brain.

  Shibuya N., Tanaka M., Yoshida M., Ogasawara Y., Togawa T., Ishii K., Kimura H.

  Hydrogen sulfide (H(2)S) is a synaptic modulator as well as a neuroprotectant. Currently, pyridoxal-5'-phosphate (PLP)-dependent cystathionine beta-synthase (CBS) is thought to be the major H(2)S-producing enzyme in the brain. We recently found that brain homogenates of CBS-knockout mice, even in ... >> More

  Hydrogen sulfide (H(2)S) is a synaptic modulator as well as a neuroprotectant. Currently, pyridoxal-5'-phosphate (PLP)-dependent cystathionine beta-synthase (CBS) is thought to be the major H(2)S-producing enzyme in the brain. We recently found that brain homogenates of CBS-knockout mice, even in the absence of PLP, produce H(2)S at levels similar to those of wild-type mice, suggesting the presence of another H(2)S-producing enzyme. Here we show that 3-mercaptopyruvate sulfurtransferase (3MST) in combination with cysteine aminotransferase (CAT) produces H(2)S from cysteine. In addition, 3MST is localized to neurons, and the levels of bound sulfane sulfur, the precursor of H(2)S, are greatly increased in the cells expressing 3MST and CAT but not increased in cells expressing functionally defective mutant enzymes. These data present a new perspective on H(2)S production and storage in the brain. << Less

  Antioxid. Redox Signal. 11:703-714(2009) [PubMed] [EuropePMC]

  This publication is cited by 2 other entries.

• Specificity studies on the beta-mercaptopyruvate-cyanide transsulfuration system.

  FIEDLER H., WOOD J.L.

  J Biol Chem 222:387-397(1956) [PubMed] [EuropePMC]

  This publication is cited by 2 other entries.