Enzyme Inhibition

Allosteric enzymes display a _______ curve in contrast to the hyperbolic curve displayed by Michaelis-Menten Enzymes.

Most allosteric enzymes contain multiple sub-units which can affect each other when the substrate binds to the _______.

Inhibition can affect either K0.5, which is the substrate concentration for _______-saturation, Vmax or both.

Allosteric enzymes have two states: a low-affinity state dubbed the “T” state and the high-affinity “R” state. Inhibitors work by preferentially binding to the ___ state of an allosteric enzyme.

Phosphorylation provides another mechanism by which enzymes can be _______.

Enzymes can also be secreted in an inactive state, known as _______.

Enzymes catalyse a reaction by reducing the activation energy needed for the reaction to occur. However, enzymes need to be tightly regulated to ensure that levels of the product do not rise to ______ levels.

Types of Inhibition: Reversible and irreversible inhibitors are chemicals which bind to an enzyme to suppress its activity. One method to accomplish this is to almost permanently bind to an enzyme. These types of inhibitors are called ______.

Reversible inhibitors either bind to an active site (competitive inhibitors), or to another site on the enzyme (non-competitive inhibitors). Competitive inhibitors compete with the substrate at the active site and therefore increase ______ (the Michaelis-Menten constant).

However, Vmax is unchanged because, with enough substrate concentration, the reaction can still ______.

The graph plot of enzyme activity against substrate concentration would be shifted to the right due to the increase of the Km, whilst the Lineweaver-Burke plot would be ______ when compared with no inhibitor.

Non-competitive inhibitors bind to another location on the enzyme and as such decrease ______.