| Question |
Answer |
| What are enzymes primary function |
They speed up reactions without being consumed |
| True or False: Enzymes do not shift the equilibrium, they just reach it faster? |
True |
| What macronutrient are enzymes? |
Proteins |
| Cofactor |
Inorganic component (minerals) needed to make the reaction work |
| Coenzyme |
Organic component (vitamins) needed to make the reaction work |
| Holoenzyme |
Complete enzyme: functional enzyme |
| Apoenzyme |
Enzyme missing cofactor or coenzyme |
| Zymogen |
Enzyme precursor: Must be converted to active form |
| Name the classes of enzymes |
Oxidoreductase, transferase, hydrolase, lyase, isomerase, ligase |
| Oxydoreductase |
Transfer e- from donnor to acceptor for redox reaction. NAD or FAD |
| Transferase |
Transfer a functional group. Breaking the bond on one molecule and putting it on another. |
| Hydrolase |
Water is a reactant...digestion! |
| Lyase |
Adds water, CO2 or ammonia to doubble bond or removes them from double bond |
| Isomerase |
Rearranges functional groups |
| Ligase |
Joins bond between C and a O, S or N... has a Pi in results and uses ATP |
| Induced fit model |
Most common active site model... not lock and key |
| When [s] = km, them Vo = ? |
1\2 Vmax |
| When Vo = 1|2 Vmax then [s] = ? |
Km |
| If the concentration of substrate [s] is smaller than Km, what is the reaction dependant on? |
Substrate |
| When the concentration of substrate is bigger than Km, what is the reaction dependant on? |
Enzymes |
| Name 4 factors effecting enzyme activity |
1. Environmental 2. Enzyme and substrate concentration 3. cofactors and coenzymes 4. Effector |
| 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. |
| Environmental effect on enzymes: pH |
Each enzyme has an optimum pH which depends on pK |
| [e] and [s] effects |
Excess of substrate = velocity of rxn depends on [e] |
| Cofactor and coenzymes |
Vitamin and mineral deficiencies will decrease enzyme activity |
| Effectors |
Activators = increase activity Inhibitors = decrease activity |
| Competitive Inhibitor |
Vmax does not change but Km will change because you have "competition" for the binding site of the enzyme |
| 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 |
| Ternary Complex |
|
| Enzyme Regulation |
1. Covalent Modification 2. Modulation of Allosteric Enzymes 3. Increase [E] by induction |
| Covalent Modification |
Primary was to regulate cellular enzymes. Adding or removing a phosphate group. Dependant on enzyme...can turn it on or off. |
| Phosphorylation of glycogen phosphorylase ____ activity |
Increases |
| Phosphorylation of glycogen synthase ____ activity |
Decreases |
| 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. |
| 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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