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An Introduction to Metabolism

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Title: Work, Energy and Enzymes Author: Ruth Gleicher Last modified by: THS District 211 Created Date: 8/19/1999 4:23:39 PM Document presentation format – PowerPoint PPT presentation

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Title: An Introduction to Metabolism


1
An Introduction to Metabolism
  • Chapter 8

2
Metabolism
  • What is metabolism?
  • The sum total of all chemical reactions in an
    organism
  • How do catabolic and anabolic pathways differ?
  • Catabolism - breaks down complex molecules
  • Anabolism - builds complex molecules

3
Energy
  • Energy is the capacity to cause change or do work
  • Kinetic Energy
  • Associated with the relative motion of objects
  • Heat or thermal energy is kinetic energy
    associated with the random movement of atoms
  • Potential Energy
  • Chemical energy is potential energy available for
    release in a chemical reaction

4
The Laws of Thermodynamics
  • The first Law Energy can be transformed, but is
    never lost, or created
  • The second law With every energy transfer,
    entropy is increased
  • Entropy is a measure of disorder

5
  • How does a cell maintain its high level of order
    if with every energy transfer entropy is
    increased?
  • Life demands a constant input of energy

6
What is free energy?
  • Free energy is the portion of a systems energy
    that is available to perform work
  • The term free does not mean that there is no cost
    to using this energy
  • It means that the energy is available

7
How Do Reactions Occur?
  • Spontaneous reactions may occur very slowly
  • All reactions require free energy of activation
    (EA)
  • Uphill portion represents the EA required to
    start the reaction
  • Downhill portion represents the loss of free
    energy by the molecules in the reaction
  • DG is the difference in free energy of products
    and reactants

8
Exergonic and Endergonic Reactions
  • Exergonic
  • Endergonic
  • Less free energy in products than reactants
  • Energetically downhill
  • DG is negative
  • More free energy in products than reactants
  • Energetically uphill
  • DG is positive

Give an example of the coupling of exergonic and
endergonic reactions in living organisms
9
Is this reaction exergonic or endergonic?
10
How can the EA barrier be overcome?
  • Temperature
  • Temperatures that are too high denature organic
    molecules, so what else is there?
  • ENZYMES
  • Enzymes lower the EA barrier so that reactions
    can occur at lower temperatures

11
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12
What are Enzymes?
  • Catalysts change the rate of the reaction without
    being altered themselves
  • Enzymes are biological catalysts
  • Enzymes are proteins, whose three dimensional
    shape allows for their ability to react
    specifically

13
Enzyme / Substrate Relationship
  • What is the substrate?
  • It is the reactant upon which an enzyme reacts
  • Enzymes are substrate specific
  • Only the active site of the enzyme actually binds
    the substrate

14
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15
The Active Site
  • The active site is where the enzyme-substrate
    interaction occurs
  • Most enzyme-substrate interactions are the result
    of weak bonds
  • The active site may cause the enzyme to hold onto
    the substrate in a very specific way
  • The active site may provide a micro-environment
    (e.g. low pH) which enhances a reaction

16
Enzyme Activity
  • Temperature
  • pH
  • Enzyme Concentration
  • Substrate Concentration

17
Cofactors
  • Non-protein molecules that help enzymes function
  • Bind to active site to enhance enzymatic
    reactions
  • Cofactors may be inorganic metals such as zinc,
    iron, or copper
  • Coenzymes are organic cofactors (e.g. vitamins)

18
Enzyme Inhibition
  • Competitive inhibitors - mimic the substrate and
    compete for the active site
  • Non-competitive inhibitors bind to the enzyme
    away from the active site, and indirectly cause a
    change in the active site

19
Competitive and Noncompetitive Inhibition
20
Allosteric Regulation
  • Regulatory molecules that bind to the enzymes
    allosteric site changing the shape of the enzyme
  • Allosterically regulated enzymes have a
    quaternary protein structure
  • Each subunit of the enzyme has an active site and
    an allosteric site
  • Allosteric activators stabilizes the active site
  • Allosteric inhibitors deactivates the active site

21
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22
Feedback Inhibition
23
Cooperativity
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