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Free Energy
(G) depends on the energy available to do work & the disorderedness (entropy) of the system
First Law of Thermodynamics
Energy cannot be created or destroyed, only transformed.
Second Law of Thermodynamics
Systems trend from order to disorder.
Entropy
disorderedness/randomness
Metabolism
the sum of all chemical reactions that occur in living organisms to sustain life
Exergonic Reaction
Reactions that release energy (-ΔG); they reduce the usable free energy in the system
Endergonic Reaction
Reactions that require energy (+ΔG); they increase the usable free energy in the system
Activation energy
the amount of energy required for a reaction to proceed
Enzyme
biological catalysts that decrease the activation energy of a reaction (but do not alter ΔG)
Active Site
region of the enzyme where a substrate molecule binds and undergoes a chemical reaction
Substrate
a molecule that an enzyme acts upon during a biochemical reaction
Lock and Key Model
illustrates that the active site has a shape that only allows the substrate to fit
Induced Fit Model
describes a small conformational change that occurs when substrate binds active site; more accurate model
Conformation
shape of something
Cofactor
inorganic molecules (like metals or ions) that help enzymes function
Coenzyme
carbon-based molecules that help enzymes function
Denaturation
unfolding of a protein; loss of biological function
Renaturation
refolding of a protein; regain biological activity
Enzyme saturation
enzymes are fully occupied = maximum rate of reaction
Inhibitor
molecules that block enzyme function
Reversible Inhibition
inhibitor can be removed from the enzyme
Irreversible Inhibition
inhibitor cannot be removed from the enzyme (covalently bound)
Competitive Inhibition
Molecule “competes” directly with substrate; fits in active site
Non-competitive/allosteric inhibition
Molecule binds to the enzyme NOT in the active site
Allosteric site
site on the enzyme where allosteric inhibitors bind to the enzyme and cause a shape change