Beta Mercaptolactate-Cysteine Disulfide: Analog of Cystine in the Urine of a Mentally Retarded Patient

Crawhall, J. C.; Parker, R. A.; Sneddon, W. Bruce; Young, Elizabeth P.; Ampola, Mary G.; Efron, Mary L.; Bixby, Emily M.

doi:10.1126/science.160.3826.419

Cited by 56 publications

(27 citation statements)

References 4 publications

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“…Alternatively, H 2 S can be released from TUM1 in the presence of reducing systems like thioredoxin or glutathione (45,46). Inhibition of TUM1 conserves cysteine and contributes to an increase in the cysteine pool (47,48). An increase in the cysteine content in the cell results in an increase in the content of cellular reductants such as thioredoxin or glutathione.…”

Section: Discussionmentioning

confidence: 99%

Characterization and Interaction Studies of Two Isoforms of the Dual Localized 3-Mercaptopyruvate Sulfurtransferase TUM1 from Humans

Fräsdorf

Radon

Leimkühler

2014

Journal of Biological Chemistry

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Background: Localization and identification of interaction partners of two splice variants of the human 3-mercaptopyruvate sulfurtransferase TUM1. Results: We show that TUM1 interacts with proteins involved in Moco and FeS cluster biosynthesis. Conclusion: Human TUM1 is a dual localized protein in the cytosol and mitochondria with distinct roles in sulfur transfer and interaction partners. Significance: The study contributes to the sulfur transfer pathway for the biosynthesis of sulfur-containing biofactors.

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Section: Discussionmentioning

confidence: 99%

Characterization and Interaction Studies of Two Isoforms of the Dual Localized 3-Mercaptopyruvate Sulfurtransferase TUM1 from Humans

Fräsdorf

Radon

Leimkühler

2014

Journal of Biological Chemistry

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“…It is noteworthy that the concentration of H 2 S is very low in brains with Alzheimer's disease, due to a decreased Congenital insufficiency or deficiency of mercaptopyruvate sulfurtransferase activity causes an inherited disease, mercaptolactate-cysteine disulfiduria. The symptom is oversecretion of mercaptolactate-cysteine disulfide in the urine, with or without mental retardation [88][89][90][91][92][93][94]. When the enzyme activity is absent, mercaptopyruvate is converted to mercaptolactate by lactate dehydrogenase (EC 1.1.1.27) [95] (Fig.…”

Section: H 2 S Production By Mercaptopyruvate Sulfurtransferase Mercamentioning

confidence: 99%

The Mercaptopyruvate Pathway in Cysteine Catabolism: A Physiologic Role and Related Disease of the Multifunctional 3-Mercaptopyruvate Sulfurtransferase

Nagahara

Sawada²

2006

CMC

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The conversion of cysteine to 3-sulfino-alanine is a major pathway in cysteine catabolism. Cysteine dioxygenase catalyzes the reaction and dietary intake of the essential amino acid methionine and the semi-essential amino acid cysteine increases the level of this enzyme by suppressing enzyme degradation via polyubiquitination. The production of cellular antioxidants such as glutathione, thioredoxin, and their families is important in cysteine metabolism, and these cellular antioxidants have critical roles in the maintenance of the cellular redox status. The mercaptopyruvate pathway, in which cysteine or aspartate transaminase catalyzes the transamination from cysteine to 3-mercaptopyruvate and then 3-mercaptopyruvate sulfurtransferase catalyzes the transsulfuration from 3-mercaptopyruvate to pyruvate, also contributes to maintain the cellular redox. 3-Mercaptopyruvate sulfurtransferase serves as an antioxidant protein: when the enzyme is exposed to stoichiometric amounts of the oxidant hydrogen peroxide, it is inhibited via the formation of low redox sulfenate at the catalytic site cysteine. On the other hand, activity is restored by the reductant dithiothreitol or reduced thioredoxin. 3-Mercaptopyruvate sulfurtransferase also detoxifies cyanide via transsulfuration from a stable persulfide at the catalytic site cysteine, a reaction intermediate, suggesting that cyanide detoxification is not necessarily an enzymatic reaction. Furthermore, a congenital defect of the enzyme causes mercaptolactate-cysteine disulfiduria associated with or without mental retardation, although the pathogenesis remains unclear. These facts suggest that 3-mercaptopyruvate sulfurtransferase has physiologic roles as an antioxidant and a cyanide antidote; is essential for neural function, and participates in cysteine degradation.

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“…Mutations in the MST gene lead to mercaptolactate-cysteine disulfiduria, an inborn error of metabolism (18). Recent studies support the role of MST as a potentially important generator of H 2 S in some organisms and tissues (19 -22).…”

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confidence: 99%

Structure and Kinetic Analysis of H2S Production by Human Mercaptopyruvate Sulfurtransferase

Yadav

Yamada

Chiku

et al. 2013

Journal of Biological Chemistry

207

278

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Beta Mercaptolactate-Cysteine Disulfide: Analog of Cystine in the Urine of a Mentally Retarded Patient

Abstract: beta-Mercaptolactate-cysteine disulfide, a hitherto undescribed analog of cystine, was isolated from the urine of a mentally retarded patient. The propertis of this substance are described, and its structure is confirmed by mass spectrometry and by partial synthesis.

Cited by 56 publications

References 4 publications

Characterization and Interaction Studies of Two Isoforms of the Dual Localized 3-Mercaptopyruvate Sulfurtransferase TUM1 from Humans

Characterization and Interaction Studies of Two Isoforms of the Dual Localized 3-Mercaptopyruvate Sulfurtransferase TUM1 from Humans

The Mercaptopyruvate Pathway in Cysteine Catabolism: A Physiologic Role and Related Disease of the Multifunctional 3-Mercaptopyruvate Sulfurtransferase

Structure and Kinetic Analysis of H2S Production by Human Mercaptopyruvate Sulfurtransferase

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