(a)
To determine: The reaction for the phosphorylation of glucose by the transfer of phosphate group from ATP, along with
Introduction: In a system, multiple
(b)
To determine: The reaction for the transfer of phosphate from phosphocreatine to ADP to generate creatine and ATP, and
Introduction: In a system, multiple chemical reactions can take place at same time. Each of the proceeding reactions has their own thermodynamic parameters such as enthalpy, free energy and others. If these reactions take place in a sequential manner and are a part of a bigger chemical process, then the total free energy for the complete system can be calculated using the free energies of the individual reactions.
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Becker's World of the Cell (9th Edition)
- ENZYME KINETICS ANALYSIS of 6 Xanthine oxidase (XO) is the enzyme that catalyzes the synthesis of uric acid, which in excess causes gouty arthritis. The inhibition of this enzyme is therefore critical in its treatment. A student researcher is investigating the inhibitory effects of kaempferol (Kmp) and chlorogenic acid (Cha) on XO which uses xanthine (Xan) as substrate. Table 1 below shows the enzyme kinetic data. Construct the Lineweaver-Burk plot complete with the linear regression analvsis. Fill in the needed information on Table 2 and paste a copy of your Lineweaver-Burk plot. submit the picture of your output in PNG or JPG format. Table 1. Enzyme Kinetic Data Velocity, mM/s [S], mM Хan Kmp Cha 0.492 0.0678 0.0351 0.0615 0.211 0.0531 0.0261 0.0451 0.087 0.0298 0.0157 0.0211 0.048 0.0195 0.0091 0.0142 0.029 0.0127 0.0067 0.0081 Table 2. Enzyme Kinetic Parameters Xanthine Kaempferol Chlorogenic acid Parameters Vmax Км Type of Inhibition Mode of Binding NA NA Lineweaver-Burk Plotarrow_forwardHigh potential. What is the equilibrium ratio of phosphoenolpyruvate to pyruvate under standard conditions when [ATP ]/[ ADP ]=10? [ATP]/[ADP] = 10?arrow_forwardHi, can someone help please. Thank you!arrow_forward
- . Pyruvate can be processed under anaerobic conditions to ethanol (in yeast) or to lactate (in mammals), as shown. Explain the primary purpose of these reactions. Describe the major biochemical features of each reactionarrow_forwardEnzyme Kinetics and Inhibition, Part 1 (worksheet for laboratory exercise 5) Suppose that you have isolated the enzyme sucrase (able to hydrolyze sucrose into glucose and fructose), and you wish to determine the nature of inhibitor A for this enzyme. You have prepared five different concentrations of substrate (sucrose), and five different concentrations of inhibitor A (plus the control, with zero mM of inhibitor A). The following Table lists the inhibitor A concentrations [I], substrate concentrations [S], and resulting enzyme velocities (V.) for all six of these experiments: 1/ V. (1) 0 mM O mM 0 mM 0 mM 0 mM [S] 0.1 mM 0.2 mM Vo 0.3333 0.50 1/[S] 33333 mM per minute 0.3 mM 0.4 mM 0.5 mM 0.60 0.666666666667 0.714285714286 0.1 mM 0.1 mM 0.20 0.2 mM 0.3 mM 0.1 mM 0.333333333333 0.428571428571 0.50 0.1 mM 0.1 mM 0.4 mM 0.5 mM 0.1 mM 0.1 mM 0.555555555556 0.20 mM 0.20 mM 0.20 mM 0.20 mM 0.20 mM 0.3 mM 0.142857142857 0.25 0.2 mM 0.3 mM 0.333333333333 0.40 0.454545454545 0.111111111111…arrow_forwardSelect all that apply. What is true about the conformational aspects of coupling? O The proton gradient is involved in the release of bound ATP from the synthase as a result of conformational change. O The conformational states interconvert as a result of proton flux through the synthase. There are two sites for substrate on the synthase and two possible conformational states: open (0) and tight-binding (T). Dinitrophenol binds to and inhibits ATP synthase conformational changes, thus inhibiting ATP synthesis. The Fo portion of ATP synthase acts as a rotary motor.arrow_forward
- Hand written solutions are strictly prohibited.arrow_forwardPhysiology Michaelis Menten relationsarrow_forwardnot true about the Michaelis-Menten equation? The equation that gives the rate, v, of an the substrate concentration [S] is the Michaelis-Menten equation = Vmax[S]/(Km + [S]), where V, enzyme-catalyzed reaction for all values of max and Km are constants. Which of the following is a) for [S] << Km, V = Vmax applies to most enzymes, but allosteric enzymes have different kinetics when [S] = Km, then v = Vmax/2 gives the rate when the enzyme concentration, temperature, pH, and ionic strength are constant for very high values of [S], v approaches Vmax e) Which is correct about the constant Km in the Michaelis-Menten equation? also called the catalytic constant or turnover number equal to the number of product molecules produced per unit time when the enzyme is saturated with substrate it is the constant in the first order rate equation v = k[A] it is the constant in the second order rate equation v = equal to the substrate concentration at which the velocity or rate of a reaction is ½ the…arrow_forward
- BiochemistryBiochemistryISBN:9781305577206Author:Reginald H. Garrett, Charles M. GrishamPublisher:Cengage Learning