7.6 enzymes
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7.6 enzymes Presentation Transcript

  • 1. 7.6 Enzymes Topic 7 Nucleic Acids & Proteins
  • 2. 7.6.1 State that metabolic pathways consist of chains and cycles of enzyme-catalysed reactions. 7.6.2 Describe the induced-fit model. (This is an extension of the lock-and-key model. Its importance in accounting for the ability of some enzymes to bind to several substrates should be mentioned) 7.6.3 Explain that enzymes lower the activation energy of the chemical reactions that they catalyse. (Only exothermic reactions should be considered)
  • 3. 7.6.4 Explain the difference between competitive and non- competitive inhibition, with reference to one example of each. Competitive inhibition is the situation when an inhibiting molecule that is structurally similar to the substrate molecule binds to the active site, preventing substrate binding. (Limit non-competitive inhibition to an inhibitor binding to an enzyme (not to its active site) that causes a conformational change in its active site, resulting in a decrease in activity) Reversible inhibition, as compared to irreversible inhibition, is not required. 7.6.5 Explain the control of metabolic pathways by end-product inhibition, including the role of allosteric sites.
  • 4. Metabolic Pathways  Metabolic pathways have these features:  They consist of many chemical reactions that are carried out in a particular sequence.  An enzyme catalyses each reaction.  All the reactions occur inside cells.  Some pathways build up organic compounds (Anabolic).  Some pathways break down organic compounds (Catabolic).  Some metabolic pathways consist of chains of reactions  eg: glycolysis  a chain of 10 enzyme controlled reactions  Some metabolic pathways consist of cycles of reactions:  eg: the Krebs Cycle
  • 5. Metabolic Pathways Ref: Biology for the IB Diploma, Allott
  • 6. Induced Fit Model  Scientists have discovered the lock and key model of enzyme action does not fully explain bind of substrates and active sites.  A modification of the lock and key model is the Induced Fit Model.  This model proposes that the active site does not fit the substrate precisely until the substrate binds.  As the substrate binds to the active site, the active site changes shape to better fit the substrate.  This weakens the bonds in the substrate, thus reducing the activation energy required for the reaction.
  • 7. Induced Fit Model Ref: Biology for the IB Diploma, Allott
  • 8. Induced Fit Model  Some enzymes have quite a broad specificity:  eg: some proteases  The induced fit model explains this better than the lock and key.  If the shape of the active site changes when the substrate binds, several different, but similar substrates could bind successfully to it and be catalysed.
  • 9. Activation Energy  For reactions to occur, the reactants must meet with sufficient energy.  This energy is called the Activation Energy.  Enzymes work by lowering the activation energy.  When the enzyme-substrate complex is formed the bonds of the substrate are stressed/weakened.  This means that less energy is required to break them.
  • 10. Exergonic & Endergonic Reactions  Chemical reactions can be either:  Exergonic:  This is where energy is released.  The products have less energy than the reactants.  Endergonic:  This is where energy is taken in from the surroundings.  The products have more energy than the reactants.
  • 11. Ref: Biology for the IB Diploma, Allott
  • 12. Ref: Biology for the IB Diploma, Allott
  • 13. Inhibition of Enzymes  Some substances reduce the activity of enzymes or even prevent it completely.  These substances are called Enzyme Inhibitors.  There are two main classes of inhibitors:  Competitive:  Non-competitive:
  • 14. Competitive Inhibitors  Competitive inhibitors are where:  The inhibitor and the substrate are structurally very similar.  The inhibitor binds to the active site preventing the substrate from binding.  An example is the inhibition of folic acid synthesis in bacteria by sulfonamide Prontosil™ (an antibiotic)
  • 15. Competitive Inhibitors Ref: Biology Levels of Life, Lecornu
  • 16. Non-competitive Inhibitors  Non-competitive inhibitors are where:  The inhibitor and substrate are not structurally similar.  The inhibitor binds to the enzyme at another site, other than the active site.  This changes the shape of the active site and prevents the substrate from binding.  An example is cyanide inhibition of cytochrome oxidase (an important enzyme in cellular respiration).  The cyanide binds to the –SH groups in an enzyme and breaks the disulphide bridges, changing the shape and function of the enzyme.
  • 17. Non-competitive Inhibitors Ref: Biology Levels of Life, Lecornu
  • 18. Graphical Representation of Inhibition Ref: IB Biology, OSC
  • 19. Allostery & Metabolic Pathways  A special kind of non-competitive inhibition is Allostery.  In many metabolic pathways, the product of the last reaction inhibits the enzyme that catalyses the first reaction.  This is called end-product inhibition.  This is also an example of negative feedback.  The site where the end-product inhibitor binds is called the allosteric site.
  • 20. Allostery & Metabolic Pathways Ref: Biology for the IB Diploma, Allott
  • 21. Allostery & Metabolic Pathways  The advantage of this method is that if there is an excess of the end-product, the whole pathway can be switched off and intermediates do not build up.  If the levels of end-product are low, more and more of the enzymes that catalyse the first reaction will start to work and the whole pathway will become activated.
  • 22. 7.6.1 State that metabolic pathways consist of chains and cycles of enzyme-catalysed reactions. 7.6.2 Describe the induced-fit model. (This is an extension of the lock-and-key model. Its importance in accounting for the ability of some enzymes to bind to several substrates should be mentioned) 7.6.3 Explain that enzymes lower the activation energy of the chemical reactions that they catalyse. (Only exothermic reactions should be considered)
  • 23. 7.6.4 Explain the difference between competitive and non- competitive inhibition, with reference to one example of each. Competitive inhibition is the situation when an inhibiting molecule that is structurally similar to the substrate molecule binds to the active site, preventing substrate binding. (Limit non-competitive inhibition to an inhibitor binding to an enzyme (not to its active site) that causes a conformational change in its active site, resulting in a decrease in activity) Reversible inhibition, as compared to irreversible inhibition, is not required. 7.6.5 Explain the control of metabolic pathways by end-product inhibition, including the role of allosteric sites.