Which of the following is incorrect? a. The ratio "catalyzed rate/uncatalyzed rate" is known as catalytic power Ob. Most enzymes exhibit a higher degree of specificity than non-biologic catalysts Most enzymes are proteins; but a few are RNA molecules Od. Most enzymes exhibit a higher catalytic power than non-biologic catalysts O c.
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- Which of the following is incorrect? a. The ratio "catalyzed rate/uncatalyzed rate" is known as catalytic power b. Most enzymes exhibit a higher degree of specificity than non-biologic catalysts O c. Most enzymes are proteins; but a few are RNA molecules Od. Most enzymes exhibit a higher catalytic power than non-biologic catalystsWhich of the following best explains why enzyme catalysis is affected by a change in pH? A. Change in pH alters ionization states of serine in the active site involved in nucleophilic catalysis B. The ionization states of his, asp and glu involved in acid/base catalysis are altered with change in pH C. Change in pH alters ionization states of contact amino acids in the active site D. All enzymes have optimum pHSelect the correct option a.A holoenzyme is a catalytically inactive enzyme in the absence of its cofactor b.An enzyme cofactor is the amino acid side group in the enzyme active site c.Each of the option listed here is true d.An apoenzymes is catalytically active RNA molecule e.A co-substrate is a detachable enzyme cofactor required with another substrate for an enzyme reaction
- is when one substrate molecule primes an enzyme to act on additional substrate molecules more readily a. Catalysis b. Cooperativity c. Feedback inhibition d. Activation energy e. CatabolismA biochemist wants to determine the effect of inhibitor A to enzyme B which catlyzes the conversion of C to D. The effect of A to the rate of formation of D is shown below: 1. The Km (report to the nearest whole number) for the enzyme-catalyzed reaction in the absence of inhibitor A is _____ mM. 2. The Km for the enzyme catalyzed reaction in the presence of inhibitor A is ____mM. 3. The Vmax for the enzyme catalyzed reaction in the absence of inhibitor A is ____ mM/min 4. The Vmax for the enzyme catalyzed reaction in the presence of inhibitor A is ____mM/min 5. Inhibitor A is a/an ________ inhibitor of enzyme BAlthough we have introduced catalytic strategies separately, an enzyme typically employs more than one during a reaction. The catalytic strategies employed by serine protease include: Select one or more: O a. reduction of ASt b. transition state stabilization Oc. metal-assisted catalysis O d. acid/base catalysis O e. covalent catalysis
- An enzyme catalyzes the reaction A --> B. The enzyme is present at a concentration of 2 nM, and the Vmax is 10 uM/s. The Km for substrate A is 10mM Calculate the catalytic efficiency of this enzymeWhich of the following is incorrect about chymotrypsin? It uses acid-base catalysis b. It has three essential amino acid residues (called the catalytic triad) at the active site It does not use metal catalysis d. It does not use covalent catalysis a. O c.Which of the following is incorrect about an enzyme-catalyzed reaction? a. Its progress can be monitored as the disappearance of substrate Ob. Its progress can be monitored as the formation of product OC. The reaction rate can be expressed as the change in [enzyme] with time d. None; all the other choices are correct
- pse A red blood cell is placed in a solution that is .85% solute. O a It depends upon the temperature b. Salt will leave the cell c. The cell crenates Od. There is no net change in the cell e The cell lyses QUESTION 4 If a reaction has a Delta G of -61: a. The reaction is non-spontaneous b The reaction is energy requiring Oc The reaction is spontaneous C. Od The reaction is exergonic Ge The reaction is endergonicAn allosteric enzyme that follows the concerted mechanism has a T/R ratio of 500 in the absence of substrate. Suppose that a mutation reversed the ratio. How would this mutation affect the relation between the rate of the reaction and substrate concentration? The mutant enzyme would behave like an enzyme that obeys Michaelis Menton kinetics. The mutant enzyme would have a smaller vmax There would be no difference in the mutant enzyme in terms of substrate binding and catalysis. More than one answer is correct. The mutant enzyme would display cooperativity more than the wild type. MacBook Air 888 F5 F4 F3 F2 %23 2$ %The key catalytic amino acids of the lysozyme active site in the free enzyme are Glu 35 with a protonated side chain and Asp 52 with a deprotonated side chain. From this observation, lysozyme requires for effective catalysis. O A. an Asp in a nonpolar environment O B. a Glu that functions as an acid catalyst O C.a Glu functions as a covalent catalyst O D. All of the above