Nucleotide Inhibition of Glyoxalase II Page: 28
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domains. The N-terminal region appears to be a highly compact, stable domain
consisting almost exclusively of beta-sheet. The active site is thought to be present in
this domain. The C-terminal region is predicted to exist almost exclusively as a flexible
a-helical domain void of, and non-essential for, catalytic activity.
1.9.5 Glyoxalase II- Substrate Specificity
The substrate specificity of Glo-II from a number of sources is summarized in
Table V.
With respect to the GSH moiety of the substrate, Glo-II is highly specific.
Neither the oa-hydroxyesters of coenzyme A nor those of thioglycolate serve as substrates
for the enzyme (168). The enzyme also exhibits no catalytic activity with substrates
containing oxygen esters (168). As with Glo-I, the role of GSH in Glo-II activity is
thought to be restricted to enzyme recognition.
With respect to the carboxylic acid moiety of the substrate, Glo-II exhibits the
ability to accept a broad variety of acids as substrates (168, 184, 185). As with Glo-I, the
ability to accept such a broad range of substrates is indicative of other detoxification
systems such as the cytochrome P-450 system (130) and GSH-S-transferase enzymes
(131). The ability of the enzyme to accept substrates is not limited only to carboxylic
acids that possess a hydroxyl moiety on the C2 position. This suggests that Glo-II
activity is not restricted to only the products of the Glo-I reaction, but may accept any
number of physiological substrates that possess the GSH ester linkage.28
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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/m1/37/: accessed April 19, 2024), University of North Texas Libraries, UNT Digital Library, https://digital.library.unt.edu; .