In vivo, Mad1 acts as a competitive inhibitor of the Mad2-Cdc20 complex.

Inhibition of this step requires competitive inhibitors, such as perchlorate and thiocyanate.

Most competitive inhibitors function by binding reversibly to the active site of the enzyme.

As a result, many sources state that this is the defining feature of competitive inhibitors.

Fumarate has been shown to be a competitive inhibitor of prolyl hydroxylase.

The active ingredient in roundup, glyphosate, is a competitive inhibitor of the enzyme.

This is the case for antibodies and for competitive inhibitors.

Recent studies revealed this acid is a competitive inhibitor of fumarate reduction.

It is generally accepted that non-depolarizing agents block by acting as reversible competitive inhibitors.

Often competitive inhibitors strongly resemble the real substrate of the enzyme.