Dehydroepiandrosterone (DHEA) is a natural,
uncompetitive inhibitor of G6PD.
One of the metabolites, urolithin A, was the most potent
uncompetitive inhibitor of CYP1B1 exhibiting two fold selectivity over CYP1A1, while another, urolithin B, was a noncompetitive inhibitor with three fold selectivity.
An uncompetitive inhibitor of IMPDH inhibits by binding at the active site of the enzyme and does not compete with IMP or NAD for inhibition of the enzyme.
The first property is that an uncompetitive inhibitor as a target conjugate is preferred over a competitive inhibitor because uncompetitive inhibitors are rare in nature and should be less susceptible to interferences from drugs and naturally occurring substances, which frequently are competitive inhibitors of enzymes.
In contrast, both [gamma]-mangostin and garcinone C are
uncompetitive inhibitors, while [alpha]-mangostin is a mixed-mode inhibitor of BChE.
rhynchophylla were
uncompetitive inhibitors with respect to the substrate benzylamine (Fig.