Interaction of methocarbamol and yeast sucrase induces enzyme inhibition.

ABSTRACT

BACKGROUND: Methocarbamol is a skeletal muscle relaxant and is widely used to relieve pain in muscles. Many drugs may have interactions with each other when used at the same time. Yeast sucrase is taken as a drug by patients with congenital sucrase-isomaltase deficiency (CSID). METHODS: In this study, the interaction between methocarbamol and yeast sucrase was investigated. RESULTS: Our results showed that methocarbamol can inhibit sucrase activity and reduce the maximum reaction velocity (Vmax) of the enzyme by a non-competitive pattern. Measurement of IC50 and Ki of the drug revealed that methocarbamol did not bind the enzyme with high affinity. Fluorescence measurement showed that the drug binds to free enzyme and enzyme-substrate complexes that were accompanied by structural changes on the enzyme. Guaifenesin, which has a similar structure to methocarbamol, does not affect the activity of sucrase. CONCLUSIONS: Methocarbamol inhibits sucrase activity and its carbamate group plays a main role in the binding of drug to sucrase.