Biochem Chapter 6
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| What are some characterisitics of enzymes? | Specificity/ function under mild conditions such of temperature and pH/ and accelerate chemical reactions
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| Cofactor | Inorganic Ion (ex. Ca2+)
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| Coenzyme | Organic or Metalloorganic molecule
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| Prosthetic Group | Conenzyme or metal ion tightly bound to a enzyme protien
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| Holoenzyme | Catalytically active enzyme together with cofactor/coenzyme
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| Apoprotein | Protien part of the holoenzyme
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| Active Site | Where substrate binds and reaction occurs
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| Substrate | Molecule bound to the active site and worked upon
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| Simple Enzymatic Reaction Equation | E + S -> ES -> EP -> E + P
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| Ground State | The starting point for either the forward or reverse reaction
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| Standard Conditions | 1 atm/ 298K/ 1 M
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| Standard Energy Change in Biochemical Reactions | pH 7.0
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| Transition State | The point at which the decay to Substrate or Product is equally possible
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| Activation Energy | Difference in energy between ground state and transition state
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| Rate of Reaction and Ea relationship | Higher Ea = Slower Reaction/ Lower Ea = Faster Reaction
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| Catalysts | Lower Ea
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| Role of Enzymes | Speed up conversion of S -> P and Eq is not affected. Reaction reaches EQ when the rate of reaction speeds up
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| Reaction Intermediates | Transient Chemical Species
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| How is rate determined? | By the rate limiting step (one with the highest Ea)
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| Reaction rates are linked to? | Ea
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| Reaction equilibria is linked to? | Gibbs Free Energy (G)
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| Values of G | Negative = Favorable/ Positive = Not
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| How do enzymes speed up reactions? | Covalent Bond formation between substrate and enzymes functional groups/ non-covalent interactions that form release small amounts of energy that help stabalize interactions . Weak interactions are optimized in the transition state because enzyme site is
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| Binding Energy | Energy dervied from enzyme substrate interaction. Major source of free energy used to lower the Ea of reactions
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| What kind of interactions are the main driving force for enzyme catalysis? | Weak binding interactions (mostly formed in the transition state make the largest contribution)
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| Where does specificty in an enzyme come from? | The binding energy
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| What is specificty dervied from? | Many weak interactions between the enzyme and the substrate
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| Things that need to occur for a reaction to take place | Reduction in entropy/ removal of solvation shell/ distortion of substrates/ proper alignment of catalytic groups on the enzyme
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| How does binding energy overcome the factors needed for a reaction to take place? | Hold substrate in place/ Enzyme-substrate interactions replace most the bonds with water/ Change in conformation induced by weak interactions
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| Induced Fit | Bring specific functional groups into position on the enzyme and allows for more weak interactions to occur as conformational change occurs
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| Catalytic Mechanisms | General Acid-Base/ Covalent/ Metal Ion
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| General Acid-Base Catalysis | Proton transfer mediatedd by other classes of molecules
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| Covalent Catalysis | Transient covalent bond is formed between enzyme and the substrate. An enzyme with a nucleophilic group is used an helps alter the reaction pathway with a lower energy
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| Metal Ion Catalysis | Help orient the substrate for reaction or stabalize a charged reaction transition states and mediate redox reaction
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| Chymotrypsin Catalysis Methods | Covalent Catalysis (Cleavage of Bond and formation of a bond between Ser residue on enzyme and part of the substrate)/ General Acid-Base Catalysis
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| Initial Rate (Vo) | When S is much greater than E in concentration
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| Vmax | Region where substrate increases will not increase the initial rate (essentially when all the enzyme has been saturated with the substrate (ES form))
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| Pre-Steady State | Period in which ES concentration builds up
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| Steady State | ES remains constant over time
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| Steady-state Kinetics | Analysis of Initial Rates
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| Steady-State Assumption | Rate of formation is equal to rate of breakdown
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| Find Vo | Vo = 1/2Vmax
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| Michaelis Menton Graph | Vo = Y/ S = X
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| Double Reciprocal Plot | 1/Vo = Km/vmax[s] + 1/vmax; Slope = Km/Vmax; Y-intercept = 1/vmax (1/vo = Y; 1/S = X)
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| Reversible Enzyme Inhibition | Competitive inhibitor competes with substrate for the active site of an enzyme. Inhibitor occupies active site of enzyme.
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| Uncompetitive Inhibitor | Binds at a different site than the active site
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| Mixed Inhibitor | Binds to both ES or E
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| pH and Enzyme Activity | Can shift how bonds are formed with the substrate or eliminate bonds that are necessary
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| Function of Chymotrypsin | Cuts bonds adjacent to aromatic amino acids/ Trp/ Phe/ Tyr
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| Zymogen | Inactive Precursor which must be cleaved
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| Methods of Enzyme Regulation | Proteolytic Cleavage/ Phosphorylation/ Proenzymes
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| Proenzymes | Must be cleaved
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