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Biochem - PCC

Enzymes

QuestionAnswer
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 on 2009-04-03



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