METABOLISM
Metabolism all of an organism’s chemical reactions
CATABOLIC PATHWAY
Catabolic Rxn
Releases energy/ “down”
breaks down complex molecules to simpler molecules.
Released energy becomes available to do the work of the cell.
ANABOLIC PATHWAY
Anabolic Rxn
Net input of energy/ “uphill”
Builds more complex molecules from simpler ones.
Energy released from catabolic pathways can be stored for later use
Pathways Quiz
Release energy? catabolic
Store energy? anabolic
Build larger molecules? anabolic
Break down molecules? catabolic
Downhill? catabolic
Uphill? anabolic
What type of rxn is cellular respiration? catabolic
What type of rxn is photosynthesis? anabolic
Require enzymes? anabolic and catabolic
ENERGY -- THE CAPACITY TO CAUSE CHANGE
Kinetic Energy
Energy of Motion
Heat -- associated with the random movement of atoms or molecules
Light -- can be harnessed to perform work
Potential Energy
Due to location, position or structure
chemical energy -- stored in chemical bonds because of the arrangement of atoms
Standing on top of a hill possesses PE because of its altitude above sea level
THERMODYNAMICS
1st Law: the energy of the universe is constant; it can be transferred and transformed, but it cannot be created nor destroyed.
2nd Law: every energy transfer or transformation increases the entropy of the universe (some energy is lost as heat)
Entropy is the measure of disorder or randomness of matter.
Spontaneous Process -- process is energetically favorable (can be quick or slow)
FREE ENERGY
Free energy: energy that can perform work
Represent this with a ∆G.
Free energy change: ∆G = Gfinal - Ginitial
EXERGONIC REACTIONS
Exergonic Rxns
Net release of free energy
Spontaneous
Greactants > Gproducts
-∆G
ENDERGONIC REACTIONS
Endergonic Rxns
net input of free energy
Never spontaneous
Greactants < Gproducts
+ ∆G
3 MAIN TYPES OF WORK
Chemical Work -- the pushing of endergonic reactions that would not occur spontaneously (ex: dehydration synthesis)
2. Transport Work -- pumping of substances across membranes/requires input of energy (ex: active transport of hydrogen ions in electron transport chains)
3. Mechanical Work -- physical movement (ex: movement of chromosomes during mitosis)
ATP: STRUCTURE
ATP CYCLE
ENZYMES
Enzymes
Act as a catalyst -- a chemical agent that speeds up a reaction
Enzymes speed up reactions by lowering the activation energy
activation energy (EA) -- the initial investment of energy for starting a reaction
the energy required to contort the reactant molecules so the bonds can break.
transition state = when the molecules have absorbed enough energy for the bonds to break
ENZYMES LOWER EA
ENZYME-SUBSTRATE
Substrate - the reactant an enzyme acts on
the catalytic action of the enzyme converts the substrate to the product
Reaction catalyzed by each enzyme is very specific = results from its shape -- shape of the active site and substrate is a compatible fit.
Active site - typically a pocket or groove on the surface of the enzyme where catalysis occurs
INDUCED FIT
As the substrate enters the active site, the enzyme slightly changes shape
This shape change makes the active site fit more snugly around the substrate
This enhances their ability to catalyze chemical reactions= induced fit
4 MECHANISMS TO LOWER EA
These 4 mechanisms reduce the amount of energy that must be absorbed to reach the transition state(EA is proportional to difficulty breaking the bonds).
Proper Orientation for a rxn to occur between the substrates
Bond Contortion: the enzymes may stretch, stress, distort, and bend the critical bonds bringing them to their transition state
Microenvironment: Active site provides a microenvironment that is more conducive to a particular type of rxn
Direct Participation: Active site may participate directly in the rxn.
CONVERSION RATE
Conversion rate
more substrate available = more frequently they access the active sites
At saturation
all enzyme molecules have their active sites engaged
as soon as product exits, another substrate enters
rate is determined by how fast the active site converts substrate to product
can only increase speed by adding more enzyme
OPTIMAL CONDITIONS
Temperature -- faster molecular motion allows for more frequent collisions between substrates and active sites.
lower temperature means fewer collisions
too high? disrupts weak interactions in protein structure = denature
Each enzyme has its own optimal temperature (usually around body temperature)
pH -- most fall in the 6-8 range
denature when out of the optimal pH
COFACTORS
Cofactors -- Nonprotein helpers for catalytic activity
can be inorganic (zinc, iron, and copper)
coenzymes = organic cofactor (vitamins)
COMPETITIVE INHIBITOR
Competitive Inhibition
Inhibitor binds to the active site
Blocks the substrate from entering the active site
active site becomes less effective
NONCOMPETITIVE INHIBITOR
Noncompetitive Inhibition
Inhibitor does not bind to active site (“non- competitive” for active site)
The binding of the inhibitor changes the shape of the protein
active site becomes less effective
ALLOSTERIC REGULATION
Allosteric regulation
Changes between 2 different shapes: active and inactive
Can be inhibition or activation
It is a non-competitive interaction
ALLOSTERIC INHIBITION
An inhibitor binds to the regulatory site and stabilizes the inactive form of the enzyme
Binding of one inhibitor will affect the active sites of all subunits.
ALLOSTERIC ACTIVATION
An activator binds to the regulatory site and stabilizes the active form of the enzyme
Binding of one activator will affect the active sites of all subunits.
FEEDBACK INHIBITION
Metabolic pathway is switched off by the binding of its end product to an enzyme that acts early in the pathway.
End product acts as the inhibitor
Prevents the cell from wasting chemical resources by making more than is necessary