MODEL 10.2. Tagyngene Perim Carlady Lia N aid Pari NADPI ATP And Inda. ATP Caul NAD Cea NADI derpni ATP ATT ATT NADMI NADI Pre lnd Enerpp proa Tatywid N lu Figure 10.2.1 Catabolism (left) vs. Anabolism (right) (Taken from page 518 of Biochemistry by Garrett and Grisham 4th Edition) The w ing bi tyl
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- An enzyme contains an active site aspartic acid with a pKa = 5.0, whichacts as a general acid catalyst. On the accompanying template, draw thecurve of enzyme activity (reaction rate) versus pH for the enzyme (assumethat the protein is stably folded between pH 2–12 and that the active siteAsp is the only ionizable residue involved in catalysis). Briefly explain theshape of your curve.12. Explain why those biological reactions that have their equilibria shifted towards theproducts have negative values for ΔGo of reactions. Explain how equilibria relates toGibbs free energy.The table presents the rates of reaction at specific substrateconcentrations for an enzyme that displays classicalMichaelis-Menten kinetics. Two sets of inhibitor data arealso included. Determine the Km and Vmax for the uninhibitedenzyme.
- Q1. We plan a farge scale purification of enzyme using a packed colum of polyacrylamide beads. We obtain the following data, in a bed. of volume. 201t Volume Eiuted (iters) ‘Concentration (Arbitrary Units] 126 00073 40 00162 (maximum) Find the yieid at 150 lites eluted.1. Which medium would you consider to be “complex” and which “defi ned”? Which is “rich” and which is “minimal”? Explain your answers. 2. Given that polyurethane is a huge polymer (MW >>100,000 Daltons), why is it important that thepolyurethanase is a secreted enzyme? If we assume that the polyurethane is the source of energy for the organism, how can material (carbon atoms) from it fi nd its way into the central metabolic pathways ofthis microbe? What is the “entry point”? What happens after its entry into the metabolic pathway?a. Describe in your own words, 5 assumptions that must be made in order to apply a Michaelis-Menten kinetic model to an enzymatic reaction. providing a mathematical expression or inequivalent (">" or "
- pls explainWhy was absorbance measured at 420 nm in the enzyme kinetics experiment? To monitor thea. decrease in catechol concentrationb. increase in quinone concentrationc. decrease in polyphenol oxidase concentrationd. polyphenol oxidase-catechol complex concentrationLineweaver-Burk plot is the most used linearization method of the MichaelisMenten equation, but the main drawback is a/an:a. overemphasis to low substrate concentration and less emphasis to high substrate concentration.b. overemphasis to high substrate concentration and less emphasis to low substrate concentration.c. exaggeration to both ends of the reciprocal of the substrate concentration.d. lack of independent variables to x- and y- coordinatesA catalyst like lactase that assists in the metabolism od milk is best described as Group of answer choices homogeneous heterogeneous enzymatic non-truseable 7, What graph will demonstrate that experimental concentration data fit a second-order reaction? Group of answer choices ln[reactant] vs. time ln(k) vs. 1/T 1/[reactant] vs. time [reactant] vs. time ln(k) vs. EaIf an enzyme catalyzed reaction has a KM of 5mM and a Vmax of 60 nm/sec, the substrate concentration at 30 nM/sec is? Thank you.
- 9:34 AM You sent Help me with this one Select true if the statement is CORRECT and false if OTHERWISE 1. Enzymes are catalysts and increase the speed of a chemical reaction without themselves undergoing any permanent chemical change. 2. Catalysis is defined as the acceleration of a chemical reaction 3. if the amount of the enzyme is kept constant and the substrate concentration is then gradually increased, the reaction velocity will decrease. 4. In the Induced-fit Model, if a dissimilar substance which does not fit the site is present, the enzyme rejects it 5. The Michaelis constant Vo is defined as the substrate concentration at 1/2 the maximum velocity. 6. A prosthetic group - an organic substance which is dialyzable and thermostable which is firmly attached to the protein or apoenzyme portion. 7. The rate of an enzyme-catalyzed reaction increases as the temperature is raised beyond optimum temperature. 8. Enzymes can be classified by the kind of chemical…Blue numbers (3, 10, 11, 14, 16, 17) refer to a biochemical molecule Orange numbers (1, 2, 5, 6, 7, 8, 9, 12, 15) refer to reaction(s) in the pathway/process.Black numbers (4, 13 ) refer to an entire pathwayEach arrow may indicate multiple biochemical reactions required Match the description of lipid metabolism to the number on the figure (1-17): Inhibits b-hydroxy-b-methylglutaryl reductase Produced during the oxidation of malate to pyruvate…Pls help ASAP, thank you! "Regulation of metabolic pathways most typically occurs at enzyme steps that are"