Draw two reaction coordinate diagrams (DG vs reaction coordinate) that compare the uncatalyzed process of lipid flipping (lipid out à lipid in ) from outer to inner leaflet to the flippase-catalyzed process.
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- Figure 27.3 illustrates the response of R (ATP-regenerating) and U (ATP-utilizing) enzymes to energy charge. a. Would hexokinase be an R enzyme or a U enzyme? Would glutamine: PRPP amidotransferase, the second enzyme in purine biosynthesis, be an R enzyme or a U enzyme? b. If energy charge = 0.5: Is the activity of hexokinase high or low? Is ribose-5-P pyrophosphokinase activity high or low? c. If energy charge = 0.95: Is the activity of hexokinase high or low? Is ribose-5-P pyrophosphokinase activity high or low?5) Consider the hypothetical biochemical pathway shown below. Assume that each letter (A, B, C, etc) represents a molecule and each number over an arrow (1, 2, 3, etc) represents an enzyme that catalyzes that reaction (so enzyme 2 catalyzes the conversion of B to C). Indicate all the probable feedback inhibition interactions that would be expected to regulate the activity of enzymes in this pathway. please indicate each interaction in the format example: "X will inhibit enzyme 27".The protein catalase catalyzes the reaction 2H,O,(aq) — 2H,O(l) + O,(g) and has a Michaelis-Menten constant of KM = 25 mM and a turnover number of 4.0 × 107 s¯¹. The total enzyme concentration is 0.010 µM and the initial substrate concentration is 4.83 µM. Catalase has a single active site. Calculate the value of Rmax (often written as Vmax) for this enzyme. Rmax Calculate the initial rate, R (often written as V), of this reaction. R = ×10 mM.s-1 mM-s-1
- The catalytic efficiency of many enzymes depends on pH. Chymotrypsin, which has a well-known catalytic mechanism, shows a maximum value of kcat/Km at pH 8.0. A) Draw a pH curve of chymotrypsin activity over the pH range of 5 to 10 and briefly explain the rationale within the context of catalysis for your depiction. In particular, note how kcat and Km may change over this pH range. B) Enzymes of the a-amylase family catalyze a reaction by forming a covalent intermediate analogous to chymotrypsin, but to a conserved aspartate residue. Illustrate a catalytic mechanism containing a tetrahedral intermediate for a glycogen debranching enzyme based upon its potential membership in the a-amylase family. (don’t need to draw a whole glycogen)Creatine is a popular dietary supplement. What is the biochemical rationale for the use of creatine? It would serve as an electron donor to support reductive biosyntheses required to sustain cellular function. It would promote the movement of ions through ion channels and thus power the synthesis of ATP during exercise. It would be converted into creatine phosphate and thus serve as a rapid means of replenishing ATP during muscle contraction. O It would directly serve as an electron carrier to support the oxidation of fuel molecules and thus energy production. What type of exercise would benefit most from creatine supplementation? O a long-distance run a leisurely walk yoga O sprinting. The optimal conditions for salivary lysozyme (hydrolyzing glycoproteins of bacterial wall) are 37 C - temperature and pH is 5.2. Explain the decrease in this enzyme activity if the temperature will rise up to 60 °C and pH will be changed to 8.0. To answer the question: a) draw the graph of the velocity dependency on temperature and pH; b) calculate the relative enzyme activity if 10 mg of lysozyme catalyzes the formation of 5 uM of the product per 2 minutes. Concidor NH3: 5.
- You are working on an enzyme that obeys standard Michaelis-Menten kinetics. What variable is the V, dependant on if the concentration of the substrate is substantially higher than the concentration of the enzyme? [S] [E] [ES] O [P] O not enough information provideda particular enzyme catalyzes a single reactant S to a single product P, following michaelis-menten kinetics rp=(VmaxCs) / (Km + Cs) 1. A reaction with this enzyme is carried out at very low substrate concentrations. Draw and label a curve on the plot that describes the reaction kinetics under those conditions.Sketch the complete reaction free energy diagram for an enzyme-catalyzed conversion of a single substrate (S) into product (P), where the reaction is spontaneous in the forward direction Overlay the free energy diagram for the uncatalyzed reaction and indicate delta delta G〒 on your sketch: Chemical step is rate limiting
- the kinetics of an enzyme were analyzed in the absence of inhibitors, as well as in the presence of inhibitor A and inhibitor B. Using the given data below, construct or calculate the following (make sure the label graphs with appropriate axes and equations, and circle final answers) plot 1[S] as abscissa and 1/v as ordinate for both catalyzed reaction and reaction with inhibitor. Use the same graph for both plots Calculate the; Km of enzyme in the reaction without inhibitor Km of the enzyme in the reaction with inhibitor (A dnB) Vmax of the uninhibited reaction Vmax of the inhibited reaction (A and B) What kind of inhibitor (A and B) was added to the enzyme-catalyzed reaction? Explain in terms of changes in Km and Vmax24. Consider the figure below, which is an alternate way to depict the energy changes occurring during a reaction from Substrate (S) to Product (P), when uncatalyzed (curve A) and when catalyzed by an enzyme (curve B). Note that curve B is not the same way we modeled an enzyme-catalyzed reaction in class; this model is a different, perhaps slightly more realistic, way of conceptualizing the energy changes over the course of a reaction than what we did in class. S and ES represent the transition states for reaction of the free substrate (S) or the enzyme-substrate complex (ES). T T activation energy for uncatalyzed reaction EST S edhosob nohtum od bluo woH abiow yedio 2 wwolaixa-y odi no vaigin oroda dapng odt ni o nfog) r gibadhoa P B ES EP progress of reaction activation energy for catalyzed reaction a) Explain briefly why, in curve B, the energy state of the enzyme-substrate complex is less than the energy state of the substrate alone. b) Suppose the enzyme in the diagram was mutated…The following diagram shows reaction curves for aspartate transcarbamoylase (ATCase) with carbamoylphosphate and different concentrations of aspartate, in the absence of ATP (curve 1) and presence of ATP (curve 2). What do the shapes of the curves tell us about the ATCase enzyme? 2 جر [aspartate] It binds substrate through a sequential mechanism. It binds substte cooperatively. It obeys Michaelis-Menten kinetics. It binds substrate through a concerted mechanism.