Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)

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Chemical Compound Review:

AC1O56JP (4S)-4-amino-4-[[(1S)-1...

Synonyms:

Pourmotabbed, T. et al., Chari, R.V. et al.

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High impact information on S-Pyruvoylglutathione

Formaldehyde dehydrogenases isolated from several different biological sources have been reported to catalyze the NAD+-dependent oxidative acylation of glutathione by methylglyoxal to form S-pyruvylglutathione, suggesting the involvement of this enzyme in the metabolism of methylglyoxal [1].
Fluoromethylglyoxal in the presence of glutathione has been shown to undergo a novel glyoxalase I-catalyzed product partitioning to S-fluorolactoylglutathione and S-pyruvylglutathione with fluoride elimination [2].

References

Substrate specificity of bovine liver formaldehyde dehydrogenase. Pourmotabbed, T., Creighton, D.J. J. Biol. Chem. (1986) [Pubmed]
Deuterium isotope effects on the product partitioning of fluoromethylglyoxal by glyoxalase I. Proof of a proton transfer mechanism. Chari, R.V., Kozarich, J.W. J. Biol. Chem. (1981) [Pubmed]

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