Abstract
Aliphatic monocarboxylic acids are demonstrated to be substrate competitive inhibitors of bacterial glutamate decarboxylase. A chain-length effect is observed in the inhibition by the monocarboxylic acids with n-valeric acid functioning as the most effective inhibitor. The inhibitor dissociation constant for the enzyme complex with n-valeric acid is dependent on pH. It would appear that the protonated form of valeric acid is the ionic form which interacts most effectively with the enzyme. n-Valeric acid and glutaric acid, another substrate-competitive inhibitor of glutamate decarboxylase, compete for interaction with the enzyme. Chloride, an allosteric activator of the enzyme, inhibits the binding of glutaric acid, but not the binding of valeric acid to the enzyme.
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