Nucleotide Inhibition of Glyoxalase II Page: 3
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been proposed as being the true substrate for glyoxalase activity. An alternative path, in
which glyoxalase activity utilizes both GSH and methylglyoxal as substrates in a bi-
molecular substrate reaction, has also been proposed (10,11).
In 1936, further research into the mechanism of glyoxalase activity led to the
detection of a novel intermediate that was formed by glyoxalase activity subsequent to
the addition of methylglyoxal to liver extracts (12). This compound, distinct from that of
the hemithioacetal adduct, was proposed as being formed initially from the
hemithioacetal and then subsequently converted to the carboxylic acid product by
glyoxalase activity. The isolation and identification of this intermediate proved to be an
obstacle that impaired further developments in this field for the next fifteen years.
It was not until 1951, when Racker (2) discovered that glyoxalase activity was
dependent on the presence of two distinct enzymes, that the pathway from
oc-ketoaldehydes to their corresponding oc-hydroxycarboxylic acids was resolved.
Furthermore, he isolated and identified the aforementioned novel intermediate S-D-
lactoylglutathione (SLG), the methylglyoxal-derived oa-hydroxyacidthioester. This
discovery led to the development of a direct spectrophotometric assay for the rate of the
formation or of the degradation of SLG that could be utilized to measure the glyoxalase
activity of cell extracts.
Racker proposed that the first enzymatic reaction of this pathway involved the
conversion of the oa-ketoaldehyde/GSH substrate (hemithioacetal) to the corresponding
oa-D-hydroxyacid-thioester. Support for this proposal was obtained by demonstrating that
this reaction, when utilizing methylglyoxal as the oa-ketoaldehyde, subsequently produced
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Gillis, Glen S. Nucleotide Inhibition of Glyoxalase II, dissertation, May 1999; Denton, Texas. (https://digital.library.unt.edu/ark:/67531/metadc2183/m1/12/: accessed April 24, 2024), University of North Texas Libraries, UNT Digital Library, https://digital.library.unt.edu; .