Enzymes are kinetically important for many of the complex reactions necessary for plant and animal life to exist. However, only a tiny amount of any particular enzyme is required for these complex reactions to occur. Explain.

Short Answer

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Enzymes, as biological catalysts, enable complex reactions in plant and animal life by lowering activation energy and increasing reaction rates. Their high catalytic efficiency, turnover number, and enzyme-substrate specificity allow enzymes to rapidly convert many substrate molecules into products, making only a small amount necessary for reactions. Additionally, enzyme activity is regulated by factors such as allosteric effectors and covalent modifications, ensuring optimal reaction rates and preventing wastage. Thus, even tiny amounts of enzymes efficiently carry out vital life processes.

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01

Introduction to Enzymes

Enzymes are biological catalysts, which are essential for carrying out complex chemical reactions in plant and animal cells. They function by lowering the activation energy of a reaction, increasing the reaction rate, and ensuring that the reaction proceeds efficiently. Since enzymes are not consumed or changed during the reaction, only a small amount of enzyme is needed to catalyze the reaction.
02

Turnover Number

The turnover number of an enzyme is a measure of its catalytic activity, defined as the number of substrate molecules converted into product per unit time by a single enzyme molecule. With a high turnover number, an enzyme can rapidly convert many substrate molecules into product, which allows a small amount of enzyme to be sufficient for a reaction.
03

Catalytic Efficiency

Enzymes exhibit high catalytic efficiency, which means they can accelerate reactions by several orders of magnitude, often increasing the reaction rate by factors of 10^6 to 10^12. This enhanced reaction rate ensures that even in the presence of trace amounts of enzyme, the necessary reactions can proceed at an adequate pace for the plant or animal cells.
04

Enzyme-Substrate Binding

One of the reasons enzymes are able to function with only a tiny amount is that they bind to their specific substrate with high specificity and affinity. This means that each enzyme molecule can bind and process multiple substrate molecules in a short period of time, ensuring a quick conversion to the required products. Additionally, the enzyme-substrate complex undergoes a series of conformational changes to form an enzyme-product complex, which then releases the product and frees the enzyme to bind with another substrate molecule, allowing the enzyme to be reused repeatedly.
05

Regulation of Enzymatic Activity

In addition to their intrinsic efficiency, enzymes in biological systems are regulated by various factors such as allosteric effectors, covalent modifications, and the presence of other proteins or molecules. This allows the cell to control the rate and extent of enzyme activity, ensuring that a specific reaction occurs only as required and not indiscriminately, preventing wastage of the enzyme and maintaining an optimal reaction rate. In conclusion, the tiny amount of enzyme required for complex reactions in plant and animal life can be attributed to the high catalytic efficiency, turnover number, enzyme-substrate binding, and regulated enzymatic activity. These factors together ensure that even small amounts of enzymes are sufficient to carry out the necessary reactions for life processes.

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Most popular questions from this chapter

The decomposition of hydrogen iodide on finely divided gold at \(150^{\circ} \mathrm{C}\) is zero order with respect to HI. The rate defined below is constant at \(1.20 \times 10^{-4} \mathrm{~mol} / \mathrm{L} \cdot \mathrm{s}\) $$ \begin{array}{r} 2 \mathrm{HI}(g) \stackrel{\mathrm{Au}}{\longrightarrow} \mathrm{H}_{2}(g)+\mathrm{I}_{2}(g) \\ \text { Rate }=-\frac{\Delta[\mathrm{HI}]}{\Delta t}=k=1.20 \times 10^{-4} \mathrm{~mol} / \mathrm{L} \cdot \mathrm{s} \end{array} $$ a. If the initial HI concentration was \(0.250 \mathrm{~mol} / \mathrm{L}\), calculate the concentration of HI at 25 minutes after the start of the reaction. b. How long will it take for all of the \(0.250 M\) HI to decompose?

The type of rate law for a reaction, either the differential rate law or the integrated rate law, is usually determined by which data is easiest to collect. Explain.

Assuming that the mechanism for the hydrogenation of \(\mathrm{C}_{2} \mathrm{H}_{4}\) given in Section \(12.7\) is correct, would you predict that the product of the reaction of \(\mathrm{C}_{2} \mathrm{H}_{4}\) with \(\mathrm{D}_{2}\) would be \(\mathrm{CH}_{2} \mathrm{D}-\mathrm{CH}_{2} \mathrm{D}\) or \(\mathrm{CHD}_{2}-\mathrm{CH}_{3} ?\) How could the reaction of \(\mathrm{C}_{2} \mathrm{H}_{4}\) with \(\mathrm{D}_{2}\) be used to confirm the mechanism for the hydrogenation of \(\mathrm{C}_{2} \mathrm{H}_{4}\) given in Section \(12.7\) ?

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The initial rate of a reaction doubles as the concentration of one of the reactants is quadrupled. What is the order of this reactant? If a reactant has a \(-1\) order, what happens to the initial rate when the concentration of that reactant increases by a factor of two?

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