BIOCHEMISTRY (LOOSELEAF)-W/ACCESS
9th Edition
ISBN: 9781319425784
Author: BERG
Publisher: Macmillan Higher Education
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Question
Chapter 8, Problem 41P
Interpretation Introduction
Interpretation:
Among the given three families of curves, the family of three curves that is expected to be obtained is to be stated.
Concept introduction:
The Michaelis-Menten equation relates the concentration of substrate with the velocity of the reaction. A constant which expresses the substrate’s concentration if the velocity of reaction equals to the half of the maximum velocity of the reaction is known as Michaelis-Menten constant. It is denoted by
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Modified TRUE or FALSE. Write the word TRUE if the statement is correct. If the statement is false, write the incorrect underlined word/s and indicate the correct word/s to make the statement true.
The Michaelis-Menten Constant (Km) of an enzyme is equal to the enzyme concentration at which the initial velocity of the reaction is one half of maximum velocity (Vmax).
Crohn’s disease. Omega-3 fatty acids have been tested asa means to prevent relapse of Crohn’s disease. Two large,randomized, placebo-controlled studies have shown nosuch benefit from omega-3 fatty acids. Suppose you areasked to design an experiment to further study this claim.Imagine that you have collected data on Crohn’s relapsesin subjects who have used these omega-3 fatty acids and
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6-25
substrate-band enzyme concentrations. The the
turnover number is equal to umax-
b)
V=Umax •57(Km+S)
anstont
For an enzyme that displays Michaelis-Menten kinetics, what is
the reaction velocity, V (as a percentage of Vmax), observed at
the following values?
a)
[S] = KM
C)
d)
e)
[S] = 0.5KM
[S] = = 0.1KM
[S] = 2KM
[S] = 10KM
w
reactores
-maximumrate of reaction
boteles conc.
Would you expect the structure of a competitive inhibitor of a
given enzyme to be similar to that of its substrate?
Chapter 8 Solutions
BIOCHEMISTRY (LOOSELEAF)-W/ACCESS
Ch. 8 - Prob. 1PCh. 8 - Prob. 2PCh. 8 - Prob. 3PCh. 8 - Prob. 4PCh. 8 - Prob. 5PCh. 8 - Prob. 6PCh. 8 - Prob. 7PCh. 8 - Prob. 8PCh. 8 - Prob. 9PCh. 8 - Prob. 10P
Ch. 8 - Prob. 11PCh. 8 - Prob. 12PCh. 8 - Prob. 13PCh. 8 - Prob. 14PCh. 8 - Prob. 15PCh. 8 - Prob. 16PCh. 8 - Prob. 17PCh. 8 - Prob. 18PCh. 8 - Prob. 19PCh. 8 - Prob. 20PCh. 8 - Prob. 21PCh. 8 - Prob. 22PCh. 8 - Prob. 23PCh. 8 - Prob. 24PCh. 8 - Prob. 25PCh. 8 - Prob. 26PCh. 8 - Prob. 27PCh. 8 - Prob. 28PCh. 8 - Prob. 29PCh. 8 - Prob. 30PCh. 8 - Prob. 31PCh. 8 - Prob. 32PCh. 8 - Prob. 33PCh. 8 - Prob. 34PCh. 8 - Prob. 35PCh. 8 - Prob. 36PCh. 8 - Prob. 37PCh. 8 - Prob. 38PCh. 8 - Prob. 39PCh. 8 - Prob. 40PCh. 8 - Prob. 41PCh. 8 - Prob. 42PCh. 8 - Prob. 43PCh. 8 - Prob. 44PCh. 8 - Prob. 45PCh. 8 - Prob. 46PCh. 8 - Prob. 47PCh. 8 - Prob. 48PCh. 8 - Prob. 49P
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Similar questions
- not 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_forwardan inorganic ion. Such as metal ion, that improves the fit of an enzyme with its substrate is a(n)?arrow_forwardIn full details. Define 'activation energy' of an enzyme catalysed single substrate reaction and mention the effects of an enzyme on this energy.arrow_forward
- . Recall your study of equilibria and kinetics from general chemistry. You used equations with upper case Kand lower case k during the study of equilibria and kinetics respectively. What do the upper and lower case letters refer to?arrow_forwardX Incorrect. Suppose that an uncatalyzed reaction is spontaneous because AG has a value of -10 kcal/mol. An enzyme that catalyzes the reaction is identified. What effect will the enzyme have on the rate of the reaction? Choose all that are correct. The enzyme increases the AG value. The enzyme increases the rate of reaction. The enzyme decreases the rate of reaction. The enzyme decreases the AG value. The enzyme raises the activation energy. The enzyme lowers the activation energy.arrow_forwardEnteric bacteria .lactic acid, and propionic bacteria have distinctive metabolic traits that can be used to characterized and identify these organisms .Describe the metabolic characteristics of these organisms name a genus that belong to each group, initiated in what way these organisms can be differentiated.arrow_forward
- Select 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_forwardATP yield. Each of the following molecules is processed by glycolysis to lactate. How much ATP is generated from each molecule?arrow_forwardLess energetic electrons. Why are electrons carried by FADH 2 not as energy rich as those carried by NADH? What is the consequence of this difference?arrow_forward
- Less energetic electrons. Why are electrons carried by FADH2FADH2 not as energy rich as those carried by NADH? What is the consequence of this difference?arrow_forwardEnzymes catalyze chemical reactions. What constitutes the active site of an enzyme? What are the turnover number (kcat), the Michaelis constant (Km), and the maximal velocity (Vmax) of an enzyme? The kcat (catalytic rate constant) for carbonic anhydrase is 5 × 105 molecules per second. This is a “rate constant,” but not a “rate.” What is the difference? By what oncentration would you multiply this rate constant in order to determine an actual rate of prod- uct formation (V)? Under what circumstances would this rate become equal to the maximal velocity (Vmax) of the enzyme?arrow_forwardTrue or False. Write the word “reducing” if the statement is correct, otherwise write “non-reducing”.arrow_forward
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