Enzymes

2. Chemical reactions  Chemical reactions need an initial input of energy = THE ACTIVATION ENERGY  During this part of the reaction the molecules are said to be in a transition state. © 2007 Paul Billiet ODWS

4. Making reactions go faster  Increasing the temperature make molecules move faster  Biological systems are very sensitive to temperature changes.  Enzymes can increase the rate of reactions without increasing the temperature.  They do this by lowering the activation energy.  They create a new reaction pathway “a short cut” © 2007 Paul Billiet ODWS

7. The active site  One part of an enzyme, the active site, is particularly important  The shape and the chemical environment inside the active site permits a chemical reaction to proceed © H.PELLETIER, M.R.SAWAYA ProNuC Database more easily © 2007 Paul Billiet ODWS

8. Cofactors  An additional non-protein molecule that is needed by some enzymes to help the reaction  Tightly bound cofactors are called prosthetic groups  Cofactors that are bound and released easily are called coenzymes  Many vitamins are coenzymes Nitrogenase enzyme with Fe, Mo and ADP cofactors Jmol from a RCSB PDB file © 2007 Steve Cook H.SCHINDELIN, C.KISKER, J.L.SCHLESSMAN, J.B.HOWARD, D.C.REES STRUCTURE OF ADP X ALF4(-)-STABILIZED NITROGENASE COMPLEX AND ITS IMPLICATIONS FOR SIGNAL TRANSDUCTION; NATURE 387:370 (1997) © 2007 Paul Billiet ODWS

9. The substrate  The substrate of an enzyme are the reactants that are activated by the enzyme  Enzymes are specific to their substrates  The specificity is determined by the active site © 2007 Paul Billiet ODWS

10. The Lock and Key Hypothesis  Fit between the substrate and the active site of the enzyme is exact  Like a key fits into a lock very precisely  The key is analogous to the enzyme and the substrate analogous to the lock.  Temporary structure called the enzyme-substrate complex formed  Products have a different shape from the substrate  Once formed, they are released from the active site  Leaving it free to become attached to another substrate © 2007 Paul Billiet ODWS

13. The Induced Fit Hypothesis  Some proteins can change their shape (conformation)  When a substrate combines with an enzyme, it induces a change in the enzyme’s conformation  The active site is then moulded into a precise conformation  Making the chemical environment suitable for the reaction  The bonds of the substrate are stretched to make the reaction easier (lowers activation energy) © 2007 Paul Billiet ODWS

14. The Induced Fit Hypothesis Hexokinase (a) without (b) with glucose substrate http://www.biochem.arizona.edu/classes/bioc462/462a/NOTES/ENZYMES/enzyme_mechanism.html  This explains the enzymes that can react with a range of substrates of similar types © 2007 Paul Billiet ODWS

17. Substrate concentration: Enzymic reactions Reaction velocity  Faster reaction but it reaches a saturation point when all the enzyme molecules are occupied.  If you alter the concentration of the enzyme then Vmax will change too. Substrate concentration Vmax © 2007 Paul Billiet ODWS

19. The effect of pH  Extreme pH levels will produce denaturation  The structure of the enzyme is changed  The active site is distorted and the substrate molecules will no longer fit in it  At pH values slightly different from the enzyme’s optimum value, small changes in the charges of the enzyme and it’s substrate molecules will occur  This change in ionisation will affect the binding of the substrate with the active site. © 2007 Paul Billiet ODWS

20. The effect of temperature  Q10 (the temperature coefficient) = the increase in reaction rate with a 10°C rise in temperature.  For chemical reactions the Q10 = 2 to 3 (the rate of the reaction doubles or triples with every 10°C rise in temperature)  Enzyme-controlled reactions follow this rule as they are chemical reactions  BUT at high temperatures proteins denature  The optimum temperature for an enzyme controlled reaction will be a balance between the Q10 and denaturation. © 2007 Paul Billiet ODWS

22. The effect of temperature  For most enzymes the optimum temperature is about 30°C  Many are a lot lower, cold water fish will die at 30°C because their enzymes denature  A few bacteria have enzymes that can withstand very high temperatures up to 100°C  Most enzymes however are fully denatured at 70°C © 2007 Paul Billiet ODWS

23. Inhibitors  Inhibitors are chemicals that reduce the rate of enzymic reactions.  The are usually specific and they work at low concentrations.  They block the enzyme but they do not usually destroy it.  Many drugs and poisons are inhibitors of enzymes in the nervous system. © 2007 Paul Billiet ODWS

24. The effect of enzyme inhibition  Irreversible inhibitors: Combine with the functional groups of the amino acids in the active site, irreversibly. Examples: nerve gases and pesticides, containing organophosphorus, combine with serine residues in the enzyme acetylcholine esterase. © 2007 Paul Billiet ODWS

26. The effect of enzyme inhibition 1. Competitive: These compete with the substrate molecules for the active site. The inhibitor’s action is proportional to its concentration. Resembles the substrate’s structure closely. E + I EI Enzyme inhibitor complex Reversible reaction © 2007 Paul Billiet ODWS

28. The effect of enzyme inhibition 2. Non-competitive: These are not influenced by the concentration of the substrate. It inhibits by binding irreversibly to the enzyme but not at the active site. Examples  Cyanide combines with the Iron in the enzymes cytochrome oxidase.  Heavy metals, Ag or Hg, combine with –SH groups. These can be removed by using a chelating agent such as EDTA. © 2007 Paul Billiet ODWS

29. Applications of inhibitors  Negative feedback: end point or end product inhibition  Poisons snake bite, plant alkaloids and nerve gases.  Medicine antibiotics, sulphonamides, sedatives and stimulants © 2007 Paul Billiet ODWS

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