Chapter 7 - Enzyme Mechanisms Flashcards
Enzyme
Alters reaction rates without changing product/substrate ratio at equilibrium
Cofactors
Aid in catalytic reactions at the active site
Catalyst 1
Lowers activation energy by stabilizing transition state
Catalyst 2
Alternate pathway for product formation
Catalyst 3
Reduces entropy by orienting the substrates
Active Site
Portion of the cell surface that the enzyme binds to
Lock Key Model
Substrates bind to a portion of the enzyme with a complementary shape
Induced Fit Model
Substrate binds induce conformation change for a complementary fit
Kinetics
Quantitative study of chemical reaction rates of an enzyme
Reversible Inhibition
Noncovalent bonding of small biomolecules to enzyme subunit
Irreversible Inhibition
Forms covalent bond with a catalytic group at enzyme active site
Competitive Inhibition
Inhibits substrate binding at active site
Uncompetitive Inhibition
Binds to enzyme-substrate complex and alters active site conformation
Mixed Inhibition
Binds to another site but distorts active site
Suicide Inhibition
Reacts with an enzyme but fails reaction and becomes permanently attached to that enzyme
Isomerization
Doesn’t change the molecular formula of product compared to substrate
Condensation
Combines two substrates to form a larger molecule
Hydrolysis/Dehydration
Involves addition/removal of water