Enzymes
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| What are enzymes primary function | They speed up reactions without being consumed
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| True or False: Enzymes do not shift the equilibrium, they just reach it faster? | True
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| What macronutrient are enzymes? | Proteins
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| Cofactor | Inorganic component (minerals) needed to make the reaction work
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| Coenzyme | Organic component (vitamins) needed to make the reaction work
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| Holoenzyme | Complete enzyme: functional enzyme
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| Apoenzyme | Enzyme missing cofactor or coenzyme
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| Zymogen | Enzyme precursor: Must be converted to active form
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| Name the classes of enzymes | Oxidoreductase, transferase, hydrolase, lyase, isomerase, ligase
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| Oxydoreductase | Transfer e- from donnor to acceptor for redox reaction. NAD or FAD
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| Transferase | Transfer a functional group. Breaking the bond on one molecule and putting it on another.
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| Hydrolase | Water is a reactant...digestion!
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| Lyase | Adds water, CO2 or ammonia to doubble bond or removes them from double bond
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| Isomerase | Rearranges functional groups
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| Ligase | Joins bond between C and a O, S or N... has a Pi in results and uses ATP
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| Induced fit model | Most common active site model... not lock and key
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| When [s] = km, them Vo = ? | 1\2 Vmax
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| When Vo = 1|2 Vmax then [s] = ? | Km
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| If the concentration of substrate [s] is smaller than Km, what is the reaction dependant on? | Substrate
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| When the concentration of substrate is bigger than Km, what is the reaction dependant on? | Enzymes
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| Name 4 factors effecting enzyme activity | 1. Environmental 2. Enzyme and substrate concentration 3. cofactors and coenzymes 4. Effector
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| Environmental effect on enzymes: temperature | Heating up an enzyme will make the reaction go faster. However, when you heat up an enzyme, it will eventually become denatured.
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| Environmental effect on enzymes: pH | Each enzyme has an optimum pH which depends on pK
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| [e] and [s] effects | Excess of substrate = velocity of rxn depends on [e]
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| Cofactor and coenzymes | Vitamin and mineral deficiencies will decrease enzyme activity
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| Effectors | Activators = increase activity Inhibitors = decrease activity
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| Competitive Inhibitor | Vmax does not change but Km will change because you have "competition" for the binding site of the enzyme
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| Noncompetitive Inhibitor | Km will stay the same but Vmax will change because you have no competition for the binding site but the inhibitor is making the molecule harder to bind with the substrate
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| Ternary Complex |
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| Enzyme Regulation | 1. Covalent Modification 2. Modulation of Allosteric Enzymes 3. Increase [E] by induction
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| Covalent Modification | Primary was to regulate cellular enzymes. Adding or removing a phosphate group. Dependant on enzyme...can turn it on or off.
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| Phosphorylation of glycogen phosphorylase ____ activity | Increases
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| Phosphorylation of glycogen synthase ____ activity | Decreases
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| Allosteric Enzymes | Regulatory enzymes in a cascade (rate limiting). Activator or inmhibitor binds to an allosteric site on the enzyme. Feedback inhibition. Tells the enzyme to speed up or slow down. Act like a noncompetitive inhibitor.
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| Enzyme Induction | Slowest of all regulations . Cells can regulate the amount of E by induction. Inductions occur from hormones and diet. Ex. Insulin
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Created by:
LrB
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