Intro to Metabolism

METABOLISM

Metabolism all of an organism’s chemical reactions

Metabolic reactions use enzymes to facilitate the creation of a product

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.

Catabolic pathways break down food molecules into useful forms of energy and heat, or smaller building blocks for biosynthesis. Anabolic pathways combine the building blocks or useful forms of energy into the many molecules that form the cell using an intake of energy

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

Anabolic reactions use energy and small molecules to build larger molecules, and catabolic reactions break down larger molecules into energy and smaller molecules

Pathways Quiz
Release energy? catabolic

  1. Store energy? anabolic

  2. Build larger molecules? anabolic

  3. Break down molecules? catabolic

  4. Downhill? catabolic

  5. Uphill? anabolic

  6. What type of rxn is cellular respiration? catabolic

  7. What type of rxn is photosynthesis? anabolic

  8. 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 is stored energy that could become kinetic energy, the energy of motion

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

more potential energy equals more potential to do more work

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 

Photosynthesis is an endergonic reaction because it uses  energy to build sugar and O2 out of CO2 and H2O. Respiration is an exergonic reaction because it releases free energy in the breakdown of sugar and O2 into CO2 and H2O

EXERGONIC REACTIONS

Exergonic Rxns

  • Net release of free energy

  • Spontaneous

  • Greactants > Gproducts

  • -∆G


Exergonic reactions release energy; meaning the reactants have a higher free energy than the products; which is a negative ∆G

ENDERGONIC REACTIONS

Endergonic Rxns

  • net input of free energy

  • Never spontaneous

  • Greactants < Gproducts

  • + ∆G

endergonic reactions use energy; meaning the reactants have a lower amount of energy than the products; meaning there is a positive ∆GExergonic reactions release energy (-∆G) and the products have lower energy. Endergonic reactions consume energy (+∆G) and the products have higher energy

3 MAIN TYPES OF WORK

  1. Chemical Work -- the pushing of endergonic reactions that would not occur spontaneously  (ex: dehydration synthesis)

Dehydration reactions join monomers into a polymer by removing water; a type of chemical work

2. Transport Work -- pumping of substances across membranes/requires input of energy (ex: active transport of hydrogen ions in electron transport chains)

Active transport moves ions across the concentration gradient, a type of transport work

3. Mechanical Work -- physical movement (ex: movement of chromosomes during mitosis)

Chromosomes align themselves to divide during mitosis, a type of mechanical work

ATP: STRUCTURE 

ATP consists of three phosphate groups, ribose, and adenine

ATP CYCLE

catabolism releases energy from ATP (transforming it to ADP) and anabolism adds energy to ADP (transforming it to ATP)

ENZYMES

Enzymes 

  • Act as a  catalyst -- a chemical agent that speeds up a reaction 

Catalysts increase the rate of 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 aid the reactants through the reactionEnzymes lower the activation energy of the reaction

ENZYMES LOWER E

an uncatalyzed reaction requires a higher activation energy than does a catalyzed reaction, there is no difference in free energy between catalyzed and uncatalyzed reactions

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

the substrate binds to the active site, creating an enzyme substrate complex. the bonds in the substrate are weakened to produce productsthe transition state is where bonds are broken on the substrate

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

initiation: reactants bind to the active site in a specific orientation, forming an enzyme-substrate complex. 
Transition state facilitation: interactions between enzyme and substrate lower the activation energy required
termination: products have lower affinity for the active site and are released. enzyme is unchanged after the reaction

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). 


  1. Proper Orientation for a rxn to occur between the substrates

  2. Bond Contortion: the enzymes may stretch, stress, distort, and bend the critical bonds bringing them to their transition state 

  3. Microenvironment: Active site provides a microenvironment that is more conducive to a particular type of rxn

  4. 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


when all enzymes are at capacity, increasing concentration of substrate does not affect the reaction rate

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 

Competitive inhibitors bind at the active site, preventing the substrate from binding. noncompetitive inhibitors bind at an allosteric site, causing the enzyme to change shape and no longer be able to bind to substrate

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 

noncompetitive inhibition changes the active site so that the substrate cannot bind

ALLOSTERIC REGULATION

Allosteric regulation 

  • Changes between 2 different shapes: active and inactive

  • Can be inhibition or activation 

  • It is a non-competitive interaction

allosteric activation changes the active site when the inhibitor binds to an allosteric site, allowing substrate to bind to the enzyme

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

in feedback inhibition, the end product of a metabolic pathway binds to the allosteric site, preventing a reaction from continuing