Reference: Caccuri AM, et al. (1993) Reinvestigation of the role of thiol groups of glyoxalase I purified from yeast (Saccharomyces cerevisiae). Biochim Biophys Acta 1202(1):157-60

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Abstract


Glyoxalase I has been purified to homogeneity from Saccharomyces cerevisiae and tested with two different thiol reagents, i.e., 5,5'-dithiobis-(2-nitrobenzoic acid) (DTNB) and 1-chloro-2,4-dinitrobenzene (CDNB). DTNB reacts with four thiol groups per molecule of enzyme and leads to a complete inhibition which is not reversed by addition of the disulfide-reducing agent dithiothreitol. On the other hand, CDNB slightly affects the glyoxalase-I activity and alkylates only one thiol residue/enzyme. In agreement, DTNB reacts with three thiol residues of the CDNB-reacted enzyme and no reactivation is observed after dithiothreitol treatment. The peptide containing the CDNB-reactive thiol group has been isolated and the sequence overlaps the segment 58-63 of the only known primary structure of glyoxalase I from Pseudomonas putida.

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Journal Article | Research Support, Non-U.S. Gov't
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Caccuri AM, Risitano A, Marmocchi F, Venardi G, Aureli G, Petruzzelli R, Desideri A
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