The inhibitor binds independently of substrate binding however km does not change

The inhibitor binds to the same site as the substrate, dropping the Km

The inhibitor competes with the substrate to bind to the active site, and drops the Vmax

The inhibitor binds to a separate site from the substrate and enhances enzyme activity

Vmax stays the same, however Km increases

They only affect enzymes that act on multiple substrates.

They bind to both the enzyme-substrate complex and the free enzyme.

They lower the concentration of free enzyme available to bind to substrate.

They decrease the apparent KM and increase the apparent VM on a Lineweaver-Burke plot.

There effect can be countered by adding more substrate.

An allosteric site on the enzyme, only when the substrate is already bound to the active site

The active site of the enzyme before the substrate has a chance to bind

An allosteric site on the enzyme only when the substrate has not yet bound to the active site

An allosteric site on the enzyme, regardless of whether or not the substrate is already bound to the active site

The active site of the enzyme at the same time as the substrate

decreases

increases

remains unchanged

remains unchanged

increases