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Lecture 10 Cell Structure - Enzymes - Lecture 10 Cell...

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Lecture 10 Cell Structure – Enzymes A. Protein Catalysts - Proteins that speed up the rate of the reaction - Never used up unless it is destroyed C 6 H 12 O 6 + 6O 2 + 6H 2 O <-> 6CO 2 + 2H 2 O + energy (ATP) o Breakdown of glucose o Killing enzymes requires heat (50-55 o C), acid Don’t have to use extreme conditions, can be selective B. Activation Energy (fig. 6-10) - Breakdown of glucose requires activation en ergy o Very few m olecules are already at a high enough en ergy that they can break down o Using a hotplat e to break down glucose a dds en ergy We h ave e nzym es that reduce the a m ount of en ergy ne ed ed to react C. Enzym e-Substrat e Complex - E + S (S) <-> ES (S) <-> E + P (S) Enzymes forms a complex with the substrate(s), this is a temporary complex. The substrate turns into the product(s), then the enzyme can be reused Lowers activation energy at ES stage D. Active Sites - Proteins h ave 3D sh ap es - Glucose + fructose <- > sucrose These would h ave to fit into the active site E. Lock a nd Key Model - One way of describing the substrat e-active site - The enzym e is the lock - The substrat e is the key
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Should have one or very few substrates that will fit F. Induced Fit Model (fig. 7-11) - A more expanded version of the lock and key model - Not an exact fit - The active site is bigger than it’s supposed to be, stretches the chemical bonds on th   substrate Enzymes and substrate are both stretched - Reasons an enzyme lowers the activation energy: 1. It puts the substrate in close proximity (L&K) 2. It puts them in the correct orientation (L&K) 3. It puts strain on the bonds (I.F.) G. Naming - Has –ase on the end Sucrose   Glucose +  Fructose =  sucrase Urea   Ammonia +  CO 2  = urease Beta-Galactosidase breaks down beta-galactosides such as lactose Lipase = lipids H. Efficiency -
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