3.2 - Environmental Impacts on Enzyme Function

Enzyme Denaturation

Change in 3D shape of the enzyme caused by temperature or pH changes.

Optimal Temperature

Temperature range where enzyme activity is the fastest.

Denaturation

Typically irreversible change in enzyme structure resulting in loss of catalytic ability.

Competitive Inhibitors

Inhibitors that bind to the active site of an enzyme and compete with the substrate.

Noncompetitive Inhibitors

Inhibitors that bind to an allosteric site and do not compete with the substrate.

pH

Hydrogen ion concentration in a solution, measured on a log scale.

Substrate Concentration

Increased concentration leads to an increased reaction rate up to substrate saturation.

Product Concentration

More products leads to fewer chances for enzyme-substrate collisions.

Active Site

Region on the enzyme where substrate binds.

Tertiary Structure

Unique 3D shape of an enzyme crucial for its function.

Irreversible Inhibitors

Inhibitors that permanently prevent enzyme function.

Reversible Inhibitors

Inhibitors that allow the enzyme to regain function upon detaching.

Catalytic Activity

The ability of an enzyme to facilitate a chemical reaction.

Temperature Effects

Changes in temperature can increase or decrease enzyme activity.

Hydrogen Bonds

Bonds that can be disrupted by changes in hydrogen ion concentration affecting enzyme structure.

Denatured Enzyme

An enzyme that has lost its functional shape and ability to catalyze reactions.

Saturation Levels

Point at which adding more substrate does not increase reaction rate.

Allosteric Site

Site on an enzyme where noncompetitive inhibitors bind.

Increased Temperature

Leads to faster molecular movement but can cause denaturation.

Decreased Temperature

Leads to slower molecular movement without denaturation.