Question
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D. Competitive inhibitor E. Enzyme-substrate complex 7) The area of an encyme into which a substrate comes into the enzyme is called the A Catalyst B. Product C. Active site D. Binding site E. Activated complex 8) The tertiary structure of an enzyme is A. Its helical orientation in space B. Its three-dimensional shape C. The particular sequence of amino acids D. The arrangement of several proteins to create a functional unit 9) A reaction catalyzed by a human enzyme was carried out at 20°C. If there is an excess of substrate, which of the following would cause the greatest increase in the rate of the reaction? A. Lowering the temperature to 10°C B. Adding more enzyme and raising the temperature to 30 C C. Adding more substrate and raising the temperature to 30°C D. Adding more enzyme and lowering the temperature to 10°C 10) Which of the following statements about initial rate enzyme inhibition kinetics is TRUE? A. Competitive inhibition permanently lowers the maximum velocity of the enzyme B. Non-competitive inhibitors resemble the substrate C. You cannot perform kinetics in the presence of inhibitors since the enzyme is no longer active D. Whenever Vmx decreases as a result of the presence of inhibitors, Km decreases also E. A competitive inhibitor is a structural analogue of the enzyme's substrate II) What decreases the activity of an enzyme by binding to a site different than the catalytic site? A. Non-competitive inhibitor B. Allosteric inhibitor C. Stereospecific agent D. Competitive inhibitor E. Transition-state analog 12) When measuring the enzyme activity, which of the following parameters will change the initial rates you measure? A. Buffer B. Temperature C. Presence of cofactor D. Substrate concentration E. Enzyme concentration 13) Which of the following statements is FALSE? A. A chemical reaction may not occur at a detectable rate even though it has a favorable equilibrium B. At the end of an enzyme-catalyzed reaction, the functional enzyme becomes available to catalyze the reaction again C. Substrate binds to an enzyme's active site D. For conversion of A to B, an enzyme shifts the reaction equilibrium to the right E. Lowering the temperature of a reaction will lower the reaction rate 14) In a plot of the rate of enzyme activity versus substrate concentration, why does the curve asymptote at high substrate concentrations?
Explanation / Answer
7. Ans- C. active site
Explanation:
The area where enzymes bind to the substrate is called active site.
8. Ans-B. is three-dimensional shape
Explanation:
The tertiary structure of an enzyme is the three-dimensional structure of the entire polypeptide chain.
9. Ans-B. adding more enzyme and raising the temp to 300 C
The rate of an enzyme-catalyzed reaction increases in the presence of increasing concentration of an enzyme. In this reaction, the substrate binds to the enzyme and produce an enzyme-substrate complex. Increases in substrate concentration cannot increase the rate and for most chemical reactions, a temperature rise of 10°C approximately when the reaction takes place.
10. Ans-E. a competitive inhibitor is a structural analog of the enzyme’s substrate
Explanation:
The competitive inhibitor resembles the substrate. They bind to the active site of the enzyme and increases Km and does not affect the Vmax. Non-competitive inhibitor decreases the Vmax and Km.
A competitive inhibitor is a structural analog of the enzyme’s substrate that reversibly binds to the active site of the enzyme which is similar to the binding site of the substrate.
