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J. Biol. Chem., Vol. 259, Issue 2, 1043-1050, Jan, 1984
J Chaudiere, EC Wilhelmsen and AL Tappel
In a systematic search for effectors of glutathione peroxidase, a number of
mercaptocarboxylic acids and tertiary mercaptans were found to be strong
and specific inhibitors of the enzyme glutathione peroxidase. Assessment of
various models was made by linear and nonlinear least squares fitting
techniques. The results support the formation of reversible
enzyme-inhibitor complexes. The active site selenium is trapped by the
rapid binding of the inhibitor in competition with GSH. Data are consistent
with the formation of thioselenenate adducts of the active site. The
kinetic model which best describes the observed inhibition by the very
strong inhibitor mercaptosuccinate implies that a selenenic acid with a
kinetically significant lifetime is not formed when hydroperoxide is
reduced. A noncovalent binding site for GSH or the presence of a cysteine
residue at the active site of the enzyme provides a mechanistic rationale
for the observed kinetics. Three of the most potent inhibitors found in
this study, mercaptosuccinate, penicillamine, and alpha-
mercaptopropionylglycine, are currently used as slow-acting drugs in the
treatment of rheumatoid arthritis. Overall, the evidence suggests that
glutathione peroxidase may be involved in the etiology of this disease.
Mechanism of selenium-glutathione peroxidase and its inhibition by mercaptocarboxylic acids and other mercaptans
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