In which of the following environmental conditions would digestive enzyme Y be unable to bring its substrate(s) to the transition state? a. At any temperature below optimum b. At any pH where the rate of reaction is not maximum c. At any pH lower than 5.5 d. At any temperature higher than \(37^{\circ} \mathrm{C}\)

Short Answer

Expert verified
The condition that would stop the enzyme Y from bringing its substrates to the transition state is any temperature higher than \(37^{\circ} \mathrm{C}\).

Step by step solution

01

Understanding Enzyme Function

Enzymes are biological catalysts that enhance the rate of biochemical reactions. They work by reducing the activation energy necessary for chemical reactions to progress. The transition state refers to the condition where the bonds in the reactant molecules (substrates) are strained and ready to be turned into products. This transition state is achieved more easily with the help of enzymes.
02

Effects of Temperature and pH on Enzyme Activity

Enzymes have optimal conditions under which they function best. This includes an optimal temperature and pH. If the temperature or pH departs from the optimum, the enzyme's ability to bind to the substrate and facilitate the reaction is reduced.
03

Analyzing the Answer Options

a) If the temperature is below optimum, enzyme activity is reduced but not completely eliminated. Therefore, the enzyme can still bring substrates to the transition state. b) The rate of enzyme-catalysed reactions can vary with changes in pH. However, as in the case with temperature below the optimum, the reaction rate decreases but doesn't necessarily drop to zero. c) The pH value of 5.5 doesn't indicate whether this is above or below the enzyme's optimum pH. Hence, we can't determine its effect on the enzyme's function. d) Too high a temperature can denature an enzyme, causing it to lose its specific shape and thus its ability to bind to the substrate. Thus, it would fail to bring its substrates to the transition state.

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Most popular questions from this chapter

An enzyme-substrate complex can form when the substrate \((\mathrm{s})\) bind (s) to the active site of the enzyme. Which environmental condition might alter the conformation of an enzyme to the extent that its substrate is unable to bind? a. Enzyme \(A\) at \(40^{\circ} \mathrm{C}\) b. Enzyme \(B\) at pH 2 c. Enzyme \(X\) at \(p H 4\) d. Enzyme \(Y\) at \(37^{\circ} \mathrm{C}\)

Tosyl-L-phenylalanine chloromethyl ketone (TPCK) specifically inhibits chymotrypsin by covalently labeling His \(^{57}\). Tosyl-L-phenylalanine chloromethyl ketone (TPCK) a. Propose a mechanism for the inactivation reaction, indicating the structure of the product(s). b. State why this inhibitor is specific for chymotrypsin. c. Propose a reagent based on the structure of TPCK that might be an effective inhibitor of trypsin.

The \(k_{\text {cat }}\) for alkaline phosphatase-catalyzed hydrolysis of methylphosphate is approximately \(14 / \sec\) at \(\mathrm{pH} 8\) and \(25^{\circ} \mathrm{C}\). The rate constant for the uncatalyzed hydrolysis of methylphosphate under the same conditions is approximately \(10^{-15} /\) sec. What is the difference in the free energies of activation of these two reactions?

At \(35^{\circ} \mathrm{C},\) the rate of the reaction catalyzed by enzyme \(\mathrm{A}\) begins to level off. Which hypothesis best explains this observation? a. The temperature is too far below optimum. b. The enzyme has become saturated with substrate. c. Both \(A\) and \(B\). d. Neither A nor B.

Another consequence of tight binding (problem 9 ) is the free energy change for the binding process. Calculate \(\Delta G^{\circ}\) ' for an equilibrium with a \(K_{\mathrm{D}}\) of \(10^{-27} M .\) Compare this value to the free energies of the noncovalent and covalent bonds with which you are familiar. What are the implications of this number, in terms of the nature of the binding of a transition state to an enzyme active site?

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