A glutathione-dependent formaldehyde-activating enzyme (Gfa) from Paracoccus denitrificans detected and purified via two-dimensional proton exchange NMR spectroscopy.

@article{Goenrich2002AGF,
  title={A glutathione-dependent formaldehyde-activating enzyme (Gfa) from Paracoccus denitrificans detected and purified via two-dimensional proton exchange NMR spectroscopy.},
  author={Meike Goenrich and Stefan Bartoschek and Christoph H Hagemeier and Christian Griesinger and Julia A. Vorholt},
  journal={The Journal of biological chemistry},
  year={2002},
  volume={277 5},
  pages={3069-72}
}
The formation of S-hydroxymethylglutathione from formaldehyde and glutathione is a central reaction in the consumption of the cytotoxin formaldehyde in some methylotrophic bacteria as well as in many other organisms. We describe here the discovery of an enzyme from Paracoccus denitrificans that accelerates this spontaneous condensation reaction. The rates of S-hydroxymethylglutathione formation and cleavage were determined under equilibrium conditions via two-dimensional proton exchange NMR… CONTINUE READING
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Sequence data was obtained from the Oak Ridge National Laboratory webpage at genome.ornl.gov/microbial/rsph

  • J. A. Vorholt, C. J. Marx, M. E. Lidstrom, R. K. Thauer
  • J. Bacteriol
  • 2000

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