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Chapter 8- An Introduction to Metabolism

metabolism- includes all the chemical reactions in an organism

  • these chemical reactions are ordered into metabolic pathways

    • sequence of steps, each controlled by an enzyme

      • products of one step become the reactants of the next step

  • enzymes help regulate the rate (or speed) of metabolic pathways

two types of metabolic pathways

  • catabolic

    • breakdown pathways

    • complex molecule to simpler compound

    • spontaneous

    • exergonic

    • release energy (kinetic)

    • downhill reactions

    • examples:

      • cellular respiration and hydrolysis of starch into glucose

  • anabolic

    • synthesis pathways

    • simple compound to complex molecule

    • non-spontaneous

    • endergonic

    • consume (absorb) energy (potential)

    • uphill reaction

    • examples

      • photosynthesis and synthesis of protein from amino acids

  • the energy released from catabolic pathways drives the anabolic pathways in a cell

laws of thermodynamics (energy transformations)

  • an organisms metabolism transforms matter and energy

    • subject to the laws of thermodynamics

  • in an open system, energy and matter may be exchanged between the system and its surroundings (organism and environment)

  • 1st law of thermodynamics

    • principle of conservation of energy

      • energy can be neither created or destroyed

      • total energy of the universe is constant

  • 2nd law of thermodynamics

    • entropy (disorder)

      • every energy transformation or transfer results in increasing entropy (disorder)

      • as energy is transferred or transformed more energy is wasted (unavailable for work)

        • some energy converted to heat in all chemical reactions

free energy and metabolism

  • free energy (G)- the portion of a systems energy available to perform work when the systems temperature and pressure are uniform

  • free energy equation- see in powerpoint notes

exergonic reactions (energy outward)

  • spontaneous reaction in which there is a net release of free energy

    • see powerpoint/BILL for graphic

endergonic reactions (energy inward)

  • non spontaneous reactions in which free energy is absorbed from the surroundings

    • see powerpoint/BILL for graphic

equilibrium and metabolism

  • reactions in an isolated system will naturally move toward equilibrium

    • not the same as homeostasis

  • cells are never at equilibrium because of the constant flow of materials in and out of the cell

    • steady supply of reactants

    • constant flow of energy

  • living organisms do not work in isolation

  • living organisms are open systems

  • a cell at equilibrium is a dead cell

hydrolysis of ATP to ADP

  • ATP is the energy source used to drive most types of cellular work

    • chemical, transport, and mechanical

  • the bond between the final two phosphate groups is broken by hydrolysis

  • the breaking of the final phosphate bond produces ADP, inorganic phosphate, and energy

    • because hydrolysis of ATP to ADP releases energy considered exergonic

regeneration of ATP from ADP and Pi

  • cells regenerates ATP very quickly through the process of cellular respiration

    • human muscle cell @ 10 million molecules per second per cell

enzymes that are biological catalysts

  • catalyst- a substance that can change the rate of a reaction without being altered in the process

  • enzyme- a protein catalyst that changes the rate of a reactions without being consumed

    • speeds up rate of metabolic reactions but are unchanged by the actions

activation energy

  • in chemical reactions- bonds are broken and bonds are formed

    • AB+CD to AC+BD

    • reactants must absorb energy from their surroundings for their bonds to break and energy is released when new bonds are formed to make products

  • activation energy (EA)- energy needed initially to reach transition state, in which bonds can be broken and from which the reaction can proceed

    • activation energy is often supplied in the form of heat (in chemistry)

    • (in biology) high temps denature proteins and kill cells

    • heat would speed up all reactions not just those that are needed

    • instead of heat organisms use enzymes to catalyze metabolic reactions

how do enzymes speed up a reactions?

  • enzymes lower the activation energy

    • allow reaction to begin sooner

    • allow reaction to proceed more quickly

  • enzymes do not change the G for a reactions

  • enzymes only change the rate at which a reaction occurs

  • enzymes are not consumed in a reactions (enzymes are reused)

enzyme structure and specificity

  • protein enzymes are macromolecules with characteristic three dimensional shapes

    • result in their being very specific- each enzymes works on one specific reaction

  • substrate- the reactant that an enzyme acts on

  • active site- region on an enzyme where the substrate binds

    • pocket or groove found on surface of enzyme that has a shape compatible to that of the substrate

    • forms enzyme-substrate complex

  • the enzyme works by binding itself to the substrate

  • biochemists have discovered and named more than 4000 different enzymes in various species

enzyme reaction rates

  • one enzyme can act on 1000 substrate molecules per second

  • rate at which an enzyme works depends on initial concentration of substrate

    • the more substrate molecules there are, the more frequently they will bind to the active site of available enzyme (higher rate of reaction)

  • when the concentration of substrate is high enough that all of the enzymes active sites are engaged the enzyme is said to be saturated

    • when enzymes are saturated the only way to increase the reaction rate would be to add more enzyme

effects of local conditions on enzyme activity

  1. temperature- each enzyme has an optimal termperature at which its reaction rate is the fastest

    • what happens to the enzyme as the temperature moves beyond the optimal temperature?

      • the heat breaks bonds in the enzyme, denaturing it and causing it to be inactive

  2. pH- enzymes have a specific pH in which they are most active

    • the optimal pH for most enzymes is between 6 and 8

    • what happens to the enzyme when the pH drops below or goes above the optimal pH?

      • the enzyme is denatured

cofactors and coenzymes

  • many enzymes are not able to work unless they have the help of another molecule

  • cofactors- any non-protein molecule that is required for the proper functioning of an enzyme

    • example: minerals such as iron or zinc

  • if a cofactor is an organic molecule, it is more specifically called a coenzyme

    • example: vitamins

regulation of enzyme activity

  • the cells metabolic pathways cannot all operate simultaneously (overload)

  • to regulate metabolic pathways the cell

    • switches on and off the genes that encode the specific enzymes (genetics) or

    • regulates the activity of enzymes once they are made

enzyme inhibitors

  • competitive inhibitors- molecules that resemble the normal substrate and compete to bind to the active site

    • resembles/mimics normal substrate

    • competitive inhibitors bind directly to the active site

    • overcome by increasing concentration of substrate

  • noncompetitive inhibitors- inhibitors that bind to the other part of the enzyme causing it to change shape so the substrate can’t bind the the active site

    • active site becomes non-functional

    • also called allosteric inhibitors

    • inhibitor binds to allosteric site

feedback inhibition

  • another way in which metabolic pathways are regulated

  • end product shuts down pathways by binding to allosteric site

    • prevents wasting of chemical resources

    • increases efficiency of cell

  • ATP can act as a feedback inhibitor

MJ

Chapter 8- An Introduction to Metabolism

metabolism- includes all the chemical reactions in an organism

  • these chemical reactions are ordered into metabolic pathways

    • sequence of steps, each controlled by an enzyme

      • products of one step become the reactants of the next step

  • enzymes help regulate the rate (or speed) of metabolic pathways

two types of metabolic pathways

  • catabolic

    • breakdown pathways

    • complex molecule to simpler compound

    • spontaneous

    • exergonic

    • release energy (kinetic)

    • downhill reactions

    • examples:

      • cellular respiration and hydrolysis of starch into glucose

  • anabolic

    • synthesis pathways

    • simple compound to complex molecule

    • non-spontaneous

    • endergonic

    • consume (absorb) energy (potential)

    • uphill reaction

    • examples

      • photosynthesis and synthesis of protein from amino acids

  • the energy released from catabolic pathways drives the anabolic pathways in a cell

laws of thermodynamics (energy transformations)

  • an organisms metabolism transforms matter and energy

    • subject to the laws of thermodynamics

  • in an open system, energy and matter may be exchanged between the system and its surroundings (organism and environment)

  • 1st law of thermodynamics

    • principle of conservation of energy

      • energy can be neither created or destroyed

      • total energy of the universe is constant

  • 2nd law of thermodynamics

    • entropy (disorder)

      • every energy transformation or transfer results in increasing entropy (disorder)

      • as energy is transferred or transformed more energy is wasted (unavailable for work)

        • some energy converted to heat in all chemical reactions

free energy and metabolism

  • free energy (G)- the portion of a systems energy available to perform work when the systems temperature and pressure are uniform

  • free energy equation- see in powerpoint notes

exergonic reactions (energy outward)

  • spontaneous reaction in which there is a net release of free energy

    • see powerpoint/BILL for graphic

endergonic reactions (energy inward)

  • non spontaneous reactions in which free energy is absorbed from the surroundings

    • see powerpoint/BILL for graphic

equilibrium and metabolism

  • reactions in an isolated system will naturally move toward equilibrium

    • not the same as homeostasis

  • cells are never at equilibrium because of the constant flow of materials in and out of the cell

    • steady supply of reactants

    • constant flow of energy

  • living organisms do not work in isolation

  • living organisms are open systems

  • a cell at equilibrium is a dead cell

hydrolysis of ATP to ADP

  • ATP is the energy source used to drive most types of cellular work

    • chemical, transport, and mechanical

  • the bond between the final two phosphate groups is broken by hydrolysis

  • the breaking of the final phosphate bond produces ADP, inorganic phosphate, and energy

    • because hydrolysis of ATP to ADP releases energy considered exergonic

regeneration of ATP from ADP and Pi

  • cells regenerates ATP very quickly through the process of cellular respiration

    • human muscle cell @ 10 million molecules per second per cell

enzymes that are biological catalysts

  • catalyst- a substance that can change the rate of a reaction without being altered in the process

  • enzyme- a protein catalyst that changes the rate of a reactions without being consumed

    • speeds up rate of metabolic reactions but are unchanged by the actions

activation energy

  • in chemical reactions- bonds are broken and bonds are formed

    • AB+CD to AC+BD

    • reactants must absorb energy from their surroundings for their bonds to break and energy is released when new bonds are formed to make products

  • activation energy (EA)- energy needed initially to reach transition state, in which bonds can be broken and from which the reaction can proceed

    • activation energy is often supplied in the form of heat (in chemistry)

    • (in biology) high temps denature proteins and kill cells

    • heat would speed up all reactions not just those that are needed

    • instead of heat organisms use enzymes to catalyze metabolic reactions

how do enzymes speed up a reactions?

  • enzymes lower the activation energy

    • allow reaction to begin sooner

    • allow reaction to proceed more quickly

  • enzymes do not change the G for a reactions

  • enzymes only change the rate at which a reaction occurs

  • enzymes are not consumed in a reactions (enzymes are reused)

enzyme structure and specificity

  • protein enzymes are macromolecules with characteristic three dimensional shapes

    • result in their being very specific- each enzymes works on one specific reaction

  • substrate- the reactant that an enzyme acts on

  • active site- region on an enzyme where the substrate binds

    • pocket or groove found on surface of enzyme that has a shape compatible to that of the substrate

    • forms enzyme-substrate complex

  • the enzyme works by binding itself to the substrate

  • biochemists have discovered and named more than 4000 different enzymes in various species

enzyme reaction rates

  • one enzyme can act on 1000 substrate molecules per second

  • rate at which an enzyme works depends on initial concentration of substrate

    • the more substrate molecules there are, the more frequently they will bind to the active site of available enzyme (higher rate of reaction)

  • when the concentration of substrate is high enough that all of the enzymes active sites are engaged the enzyme is said to be saturated

    • when enzymes are saturated the only way to increase the reaction rate would be to add more enzyme

effects of local conditions on enzyme activity

  1. temperature- each enzyme has an optimal termperature at which its reaction rate is the fastest

    • what happens to the enzyme as the temperature moves beyond the optimal temperature?

      • the heat breaks bonds in the enzyme, denaturing it and causing it to be inactive

  2. pH- enzymes have a specific pH in which they are most active

    • the optimal pH for most enzymes is between 6 and 8

    • what happens to the enzyme when the pH drops below or goes above the optimal pH?

      • the enzyme is denatured

cofactors and coenzymes

  • many enzymes are not able to work unless they have the help of another molecule

  • cofactors- any non-protein molecule that is required for the proper functioning of an enzyme

    • example: minerals such as iron or zinc

  • if a cofactor is an organic molecule, it is more specifically called a coenzyme

    • example: vitamins

regulation of enzyme activity

  • the cells metabolic pathways cannot all operate simultaneously (overload)

  • to regulate metabolic pathways the cell

    • switches on and off the genes that encode the specific enzymes (genetics) or

    • regulates the activity of enzymes once they are made

enzyme inhibitors

  • competitive inhibitors- molecules that resemble the normal substrate and compete to bind to the active site

    • resembles/mimics normal substrate

    • competitive inhibitors bind directly to the active site

    • overcome by increasing concentration of substrate

  • noncompetitive inhibitors- inhibitors that bind to the other part of the enzyme causing it to change shape so the substrate can’t bind the the active site

    • active site becomes non-functional

    • also called allosteric inhibitors

    • inhibitor binds to allosteric site

feedback inhibition

  • another way in which metabolic pathways are regulated

  • end product shuts down pathways by binding to allosteric site

    • prevents wasting of chemical resources

    • increases efficiency of cell

  • ATP can act as a feedback inhibitor

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