AP Biology Enzymes

University:
Winston-Salem Forsyth County Schools
Course:
AP Biology
Academic year:

2023
Views:

211

Pages:

1
Author:

Cory Singh

Enzymes ● The active site of enzymes specifically interact with specific substrate molecules ○ Can be used to break a polymer into 2 monomers (catabolic & exergonic) ○ Can be used to join 2 monomers into a polymer (anabolic & endergonic) ● The charge of the substrate & enzyme must be compatible ● They are catalysts: speed up reactions by lowering the activation energy ● Change in the molecular structure of an enzyme may change its function/efficiency ○ Denaturing: The protein structure of an enzyme is disrupted & it can’t catalyze reactions ■ Caused by: Temperatures & pH outside of the optimal range ● Rate of Reactions ○ Increase in concentrations of substrates & enzymes can increase the rate of the reactions ○ Increases as temperature increases (within optimal range) since molecules will collide more often (molecules are faster) ● As the amount of product increases, feedback inhibition can occur (to maintain homeostasis) ○ Inhibitors can reversibly (once removed, the enzyme can be used again)/irreversibly prevent substrates from binding to an enzyme’s active site ○ Competitive inhibition: Binds to the active site, competes with substrate ○ Non-Competitive Inhibition: Does not bind to the active site (binds to allosteric sites), but changes the shape of the active site and prevents the binding of the substrate ○ Negative feedback inhibition is required to maintain homeostasis ● Enzymes need to be activated through non-protein cofactors & coenzymes ○ Cofactors: Small inorganic compounds/ions that are bound within the enzyme molecule ○ Coenzymes: Organic molecules that bind loosely to the active site of an enzyme & aid in substrate recruitment (vitamins)