Biochem Chapter 6
Quiz yourself by thinking what should be in
each of the black spaces below before clicking
on it to display the answer.
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| show | Specificity/ function under mild conditions such of temperature and pH/ and accelerate chemical reactions
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| Cofactor | show 🗑
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| Coenzyme | show 🗑
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| show | Conenzyme or metal ion tightly bound to a enzyme protien
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| show | Catalytically active enzyme together with cofactor/coenzyme
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| Apoprotein | show 🗑
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| show | Where substrate binds and reaction occurs
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| Substrate | show 🗑
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| Simple Enzymatic Reaction Equation | show 🗑
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| show | The starting point for either the forward or reverse reaction
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| Standard Conditions | show 🗑
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| show | pH 7.0
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| Transition State | show 🗑
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| show | Difference in energy between ground state and transition state
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| show | Higher Ea = Slower Reaction/ Lower Ea = Faster Reaction
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| show | Lower Ea
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| show | 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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| show | Transient Chemical Species
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| How is rate determined? | show 🗑
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| show | Ea
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| Reaction equilibria is linked to? | show 🗑
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| Values of G | show 🗑
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| show | 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 | show 🗑
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| show | 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? | show 🗑
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| What is specificty dervied from? | show 🗑
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| show | Reduction in entropy/ removal of solvation shell/ distortion of substrates/ proper alignment of catalytic groups on the enzyme
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| show | Hold substrate in place/ Enzyme-substrate interactions replace most the bonds with water/ Change in conformation induced by weak interactions
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| show | 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 | show 🗑
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| show | Proton transfer mediatedd by other classes of molecules
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| show | 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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| show | Help orient the substrate for reaction or stabalize a charged reaction transition states and mediate redox reaction
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| show | 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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| show | When S is much greater than E in concentration
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| Vmax | show 🗑
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| show | Period in which ES concentration builds up
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| Steady State | show 🗑
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| Steady-state Kinetics | show 🗑
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| show | Rate of formation is equal to rate of breakdown
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| show | Vo = 1/2Vmax
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| Michaelis Menton Graph | show 🗑
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| Double Reciprocal Plot | show 🗑
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| Reversible Enzyme Inhibition | show 🗑
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| Uncompetitive Inhibitor | show 🗑
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| show | Binds to both ES or E
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| pH and Enzyme Activity | show 🗑
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| show | Cuts bonds adjacent to aromatic amino acids/ Trp/ Phe/ Tyr
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| Zymogen | show 🗑
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| Methods of Enzyme Regulation | show 🗑
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| Proenzymes | show 🗑
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