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Chemical Compound Review:

MMTS methylsulfonylsulfanylmethane

Synonyms: PubChem14140, CCRIS 7217, AG-F-05982, ACMC-209h9g, CHEBI:74357, ...

Zhang, H. et al., Paliwal, V. et al., Valentine, W.N. et al., Krauth-Siegel, R.L. et al., Davenport, J.W. et al.

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High impact information on mesylthiomethane

Blocking the sulfydryl group in YC with methylmethanethiosulfonate (that formed YCSSCH(3)) totally inhibited thiyl radical formation as did substitution of Tyr with Phe (i.e. FC) in the presence of MPO/H(2)O(2)/NO(2)(-) [1].
Reduction of TcsF with DTT followed by alkylation with methylmethanethiosulfonate (MMTS), demonstrated that the active subunit of TcsF bound to and eluted from anti-TCR-alpha, but not to anti-TCR-beta columns [2].
(d) Upon reaction of methylmethanethiosulfonate at the slow site, the K1/2 for MgATP hydrolysis is reduced from 0.65 to 0.25 mM [3].
8-Mercapto-FAD X glutathione reductase, for instance, reacted readily and stoichiometrically with the thiol reagent methylmethanethiosulfonate [4].
Acid pH alone and the simultaneous presence of Mg++, K+ and PEP prior to MMTS treatment protected against the effects on PEP kinetics, but did not alter the induction of thermolability [5].

References

Intramolecular electron transfer between tyrosyl radical and cysteine residue inhibits tyrosine nitration and induces thiyl radical formation in model peptides treated with myeloperoxidase, H2O2, and NO2-: EPR SPIN trapping studies. Zhang, H., Xu, Y., Joseph, J., Kalyanaraman, B. J. Biol. Chem. (2005) [Pubmed]
Monoclonal, antigen-specific, T cell contrasuppressor factor expresses determinants of TCR alpha-chain (not necessarily TCR beta-chain), having a molecular mass of about 40 kDa. Paliwal, V., Friedman, A.M., Ptak, W., Askenase, P.W. J. Immunol. (1994) [Pubmed]
The plasma membrane H+-ATPase of Neurospora crassa. Properties of two reactive sulfhydryl groups. Davenport, J.W., Slayman, C.W. J. Biol. Chem. (1988) [Pubmed]
FAD analogues as prosthetic groups of human glutathione reductase. Properties of the modified enzyme species and comparisons with the active site structure. Krauth-Siegel, R.L., Schirmer, R.H., Ghisla, S. Eur. J. Biochem. (1985) [Pubmed]
Studies with human erythrocyte pyruvate kinase (PK): effects of modification of sulfhydryl groups. Valentine, W.N., Paglia, D.E. Br. J. Haematol. (1983) [Pubmed]

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