Enzymes II: kinetics الفريق الطبي األكاديمي. Done By: - AHMAD ALSAHELE. Corrected By:-Bushra saleem
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1 Enzymes II: kinetics الفريق الطبي األكاديمي Done By: - AHMAD ALSAHELE Corrected By:-Bushra saleem لكية الطب البرشي البلقاء التطبيقية / املركز و من أحياها /
2 و من أحياها Specific aims: 1. Know what is kinetics; 2. Understand the concepts of Michaelis-Menten Kinetics and its conditions 3. Define Velocity (initial velocity V0) and how it is determined 4. Understand how the experiment of initial velocity V0 versus substrate concentration [S ] is achieved 5. 5.Define steady state kinetics,( M-M kinetics: E and ES changes very small) 6. 6.Define Pre-steady State Kinetics and its importance: 7. Understand the concept of Vmax, and Km 8. Understand Michaelis-Menten Equation 9. Compare Michaelis-Menten kinetics enzymes with enzymes that do not follow M-M kinetics (allosteric enzymes) 10. Describe Perfect enzymes, 11. Understand the concept of Kcat/Km 12. Know how Line weaver Burk blot is established 13. Interpret data from Line weaver Burk blot Slide 1: E+S >=< ES >=< ES* >=< EP >=< E+P this equation explain that :- substrate bind to enzyme=> to make enzyme-substrate complex=> which form transitional state=> which give you enzyme and products=> then enzyme release products you should differentiate between ES & ES* ES ==> enzyme-substrate complex (just binding) ES* ==> the middle of the reaction (transitional state) Michaelis-Menten kinetics Slide 2: E+S >=< ES >=< ES* >=< EP >=< E+P Page 1
3 rate of formation mean how much product produced per the unit of time on another words the velocity of the reaction Slide 3+4+5: Important Page 2
4 enzyme kinetics is very important in pharmacology and what applied to enzyme kinetics applied to the drug kinetics How experimenters got these data in the plot 1? we know that by this experiment which is done in different tubes in the first tube we add 0 substrates and in the last tube we add the highest amount of substrate and the rest we add vary amounts of substrate then we add a considered amount of enzyme in all tubes and then we measure at different concentration of substrate how many products (usually in micromole) are produced per second when we add the enzyme to the tubes at this moment [S] decrease, [P] increase, [E] decrease, [ES] increase these processes take place in millisecond dramatic changes in the beginning of the reaction make measuring of velocity of the reaction very difficult because the change in [E] & [ES] is very sharp we can measure the velocity of the reaction when the changes is minimal this happen after about 1 minute measuring [P] is more important than measuring [E] or [ES]... at the beginning of the reaction (time zero) enzyme is not added yet (the reaction is not catalyzed by an enzyme) at time zero [S] => high, [E] => high, [ES] => low, [P] => low [ES] is very low at time zero because enzyme is not added to the reaction yet Page 3
5 ... pre-steady state: the state in which enzyme concentration drop rapidly this state is not important in study of reaction velocity because [E] & [ES] varying widely steady state: we interest with this state because the study of reaction velocity in this state is possible because [E] & [ES] relatively constant equilibrium state: it is the state after the steady state in which the products will accumulated and the reversible reactions go back and the reaction reach equilibrium at this period we cannot measure the velocity of reaction because the change in [S] & [P] is very little Slide 6: This instrument is used to study Pre-steady State Kinetics reaction mechanism, rate of ES formation Can give info on Kinetic Considerations Slide 7: Page 4
6 Increase in substrate concentration Low substrate Moderate substrate High substrate [S] Little Good Excess [E] Excess Enough Little Reaction rate The reaction will be very small because the enzyme are waiting to have substrate but there is no Reaction rate is good There is saturation so that no more product is produced per unit of time Slide 7: Page 5
7 و من أحياها this plot explain what mentioned in the previous slide V 0 don't mean 0 time put mean steady state when the [S] increase, V 0 increase until we reach the point of saturation at this point V0 become constant because all enzymes are busy and no more products are produced at the unit of time Slide 8: 1 2 the most important parameters in Michaelis-Menten kinetics are:- V max => maximal velocity K m => michaelis constant line 1 represent the V max which is at very high concentration of substrate V max depend on the amount of enzyme we have V max is a variable for the enzymes represent enzyme availability example: if we have two enzymes with V max 50 & 100 respectively it is not necessary E2 stronger than E1 because [E] has an effect in V max at point 2 all enzymes are busy and the velocity of reaction is constant K m => the concentration of substrate at 50% of V max K m tells the substrate affinity of the enzyme substrate affinity (or enzyme strength) is inversely related with K m the lowest [S] taken to reach 1/2 V max the stronger the enzyme Page 6
8 we called this curve hyperbolic curve and it represent all enzymes that follow Michaelis-Menten kinetics Slide 9: Michaelis-Menten equation:- Enzymes That Don t Follow Michaelis-Menten Kinetics Include Those That Bind Substrate Cooperatively - Binding of One Substrate Affects Binding of Others Michaelis-Menten equation is the equation that relate between V max & K m & [S] we can calculate V0 at specific [S] if we know V max & K m The unit of V max Mole/size. time the unit of K m Mole/size allosteric enzyme don't have hyperbolic plot instead sigmoidal Slide 10: Page 7
9 و من أحياها allosteric enzymes:- have a sigmoidal curve because of cooperativity cooperativity mean if a substrate bind to one subunit this favor bind to the second subunit cooperativity must occur in multi subunit enzyme Page 8
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