Biochem - PCC Word Scramble
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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 |
Created by:
LrB
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