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An Introduction to Metabolism and Enzymes

An Introduction to Metabolism and Enzymes. Metabolism. is the sum total of an organism ’ s chemical reactions. Metabolism- e.g. oxidation of sugar. Catalase. Facts to be explained. Enzymes are proteins Enzymes are required in minute quantities

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An Introduction to Metabolism and Enzymes

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  1. An Introduction to Metabolism and Enzymes

  2. Metabolism • is the sum total of an organism’s chemical reactions

  3. Metabolism- e.g. oxidation of sugar

  4. Catalase

  5. Facts to be explained • Enzymes are proteins • Enzymes are required in minute quantities • Enzymes show striking specificity. They catalyze specific reactions involving specific substrates • Enzymes increase the speed of a chemical reaction - Both forward and backward reaction • The action of enzyme is greatly affected by temperatures. • Enzymatic activity is affected by H+ ions concentration (pH) • The rate of reaction is affected by substrate and enzymeconcentration • Enzyme itself is not used up in the reaction it catalyzes so it can be used over again and again

  6. Specificity-lock and key hypothesis

  7. Induced Fit model of enzyme action

  8. 3D / tertiary structure of an enzyme

  9. Binding sites of an enzyme

  10. Mechanism of enzyme reaction • The substrate • is the reactant an enzyme acts on • The enzyme • binds to its substrate, forming an enzyme-substrate complex

  11. 1Substrates enter active site; enzyme changes shape so its active site embraces the substrates (induced fit). 2Substrates held in active site by weak interactions, such as hydrogen bonds and ionic bonds. Substrates Enzyme-substrate complex 3Active site (and R groups of its amino acids) can lower EA and speed up a reaction by • provide correct substrate orientation, • stress the substrate bonds • stabilize the transition state, • provide a favorable microenvironment, 6Active site Is available for two new substrate Mole. Enzyme 5Products are Released. 4Substrates are Converted into Products. Products The catalytic cycle of an enzyme

  12. Interaction between Active site and substrate fitting of a substrate brings chemical groups of the active site into positions that enhance their ability to catalyze the chemical reaction

  13. Activation energy-barrier to reaction

  14. Activation energy

  15. The active site can lower an EA • The active site can lower an EA barrier by • Orienting substrates correctly • Straining substrate bonds • Stabilizing transition state • Providing a favorable microenvironment

  16. Reaction pathway

  17. Effect of Enzyme concentration

  18. Effect of Substrate concentration

  19. Effect of temperature on rate of chemical reaction

  20. Chemical reaction takes place only if the particles collide at the right orientation and with sufficient energy (activation energy) Effect of temperature on rate of chemical reaction: http://www.absorblearning.com/media/attachment.action?quick=w2&att=2298

  21. Effect of temperature on rate of chemical reactions

  22. Effect of temperature

  23. Are all enzymes equally susceptible to denaturation by high temperature ? Some bacteria survive in hot spring at the yellow stone national park US) at ~ 70°C

  24. Some bacteria survive in deep sea hydrothermal vent at > 110°C

  25. Enzyme application_thermophilic

  26. Optimal temperature for typical human enzyme Optimal temperature for enzyme of thermophilic (heat-tolerant) bacteria Rate of reaction 80 0 20 100 40 Temperature (Cº) (a) Optimal temperature for two enzymes Effects of Temperature • Each enzyme • Has an optimal temperature in which it can function best

  27. pH – a measure of the conc of H+

  28. Optimal pH for different enzymes Optimal pH for pepsin (stomach enzyme) Optimal pH for trypsin (intestinal enzyme) Rate of reaction 5 6 7 8 9 3 4 0 2 1 (b) Optimal pH for two enzymes

  29. Effect of pH on enzyme / protein

  30. Effect of pH on enzyme / protein

  31. Effect of pH on enzyme

  32. Coenzymes-- Non-protein molecules that are enzyme helpers • Some enzymes work only in the presence of other molecules E.g. NAD+ in dehydrogenation • Some vitamins are important because they are co-enzymes e.g. Vitamin B groups

  33. Co-enzyme e.g. NAD+ NAD+ helps the enzyme dehydrogenase accepting H removed from substrates

  34. Denaturation and renaturation of enzyme

  35. Denaturation of enzyme

  36. It is the loss of the specific tertiary structure of a protein molecule. Lose its normal biological function. The change may be temporary or permanent, but the amino acid sequence (primary structure) of the protein could remain un________ --- renaturation, though rare, might occurs and restore the enzyme function. Denaturation of enzyme

  37. Factors causing protein denaturation

  38. Factors causing protein denaturation

  39. Enzyme Inhibitor_types

  40. Competitive inhibition

  41. Competitive inhibition

  42. Competitive inhibition–e.g. sulphonamide

  43. Non competitive inhibition

  44. Com vs non comp inhibition

  45. End product inhibition –helps regulate enzyme activities

  46. End product inhibition

  47. End product_cellular respiration

  48. Mitochondria, sites of cellular respiraion 1 µm Specific Localization of Enzymes • Within the cell, enzymes may be • Grouped into complexes • Incorporated into membranes • Contained inside organelles

  49. Is 37 degree Celcius the optimum temperature for human enzyme? • Why then our body temperature is 37 degree Celcius?

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