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

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The sequence of amino acid residues around the oxidation-reduction active disulfide in yeast glutathione reductase.

A 14-residue peptide containing the oxidation-reduction active cystine residue from yeast glutathione reductase has been isolated from proteolytic digests of the enzyme in which the free sulfhydryl groups had been reacted with N-ethylmaleimide. The sequence of this disulfide-containing peptide was found to be:(see article).The sequence was highly homologous with the active cystine regions in Escherichia coli and pig heart lipoamide dehydrogenase. The sequences of three of the postulated four thiol-containing regions of the enzyme are also presented, as well as evidence supporting the view that the enzyme is composed of two identical subunits.[1]

References

  1. The sequence of amino acid residues around the oxidation-reduction active disulfide in yeast glutathione reductase. Jones, E.T., Williams, C.H. J. Biol. Chem. (1975) [Pubmed]
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