Enzymes and Their Properties

<p>Temperature and pH levels (C)</p> Signup and view all the answers

<p>It illustrates the specificity of enzymes for their substrates. (A)</p> Signup and view all the answers

<p>They exhibit variation in tissue distribution and properties. (D)</p> Signup and view all the answers

<p>A change in the enzyme's conformation to form a stable complex. (C)</p> Signup and view all the answers

<p>Transferases (D)</p> Signup and view all the answers

<p>They are organic molecules often derived from vitamins. (A)</p> Signup and view all the answers

<p>The three-dimensional arrangement of amino acids in the enzyme. (A)</p> Signup and view all the answers

<p>Apoenzyme (B)</p> Signup and view all the answers

<p>Activation energy (C)</p> Signup and view all the answers

<p>It decreases the reaction velocity. (D)</p> Signup and view all the answers

<p>Temperature of the reaction (C)</p> Signup and view all the answers

<p>By changing the pH of the enzyme environment to inhibit activity. (C)</p> Signup and view all the answers

<p>It is reached when all active sites of the enzyme are saturated. (C)</p> Signup and view all the answers

<p>The rate increases until it reaches Vmax. (D)</p> Signup and view all the answers

<p>At steady state. (C)</p> Signup and view all the answers

<p>Velocity increases to a peak before decreasing with higher temperatures. (C)</p> Signup and view all the answers

<p>pH affects the ionization of active site groups and can lead to denaturation. (A)</p> Signup and view all the answers

<p>The plateau phase of the velocity curve. (B)</p> Signup and view all the answers

<p>The substrate concentration at which reaction velocity equals 50% of Vmax. (B)</p> Signup and view all the answers

<p>The enzyme activity plateaus and cannot increase further. (A)</p> Signup and view all the answers

<p>They can lead to temperature-induced denaturation of the enzyme. (A)</p> Signup and view all the answers

Biologically active proteins that accelerate chemical reactions within living organisms.

Enzymes are not consumed or changed during the reaction they catalyze. They can be used repeatedly.

A specific region on an enzyme where the substrate binds to initiate the catalytic reaction.

A model that describes the enzyme's active site as a rigid structure that perfectly fits the substrate.

The active site of the enzyme changes shape slightly to accommodate the substrate, facilitating the reaction.

The molecule that an enzyme acts upon, the 'ingredient' that's processed.

Enzymes that catalyze the same reaction but have different amino acid sequences and properties.

A non-protein component that assists in the catalytic activity of some enzymes.

The active site of an enzyme is not rigid but flexible, allowing the enzyme to adjust its shape to fit the substrate and create a stable complex.

Cofactors are non-protein molecules that assist in the function of enzymes. They can bind temporarily or permanently.

An enzyme with its cofactor bound to it is called a holoenzyme. Without the cofactor, it's known as an apoenzyme.

The process of converting a substrate into a product often goes through an intermediate form known as the transition state. The transition state has higher energy than the substrate.

The energy needed to initiate a chemical reaction is called Activation Energy (ΔG). Higher activation energy means the reaction is slower.

The rate at which a reaction occurs, measured by the amount of substrate converted to product per time unit.

The rate of a reaction is affected by factors such as substrate concentration, pH, temperature, and presence of inhibitors.

The maximum rate at which an enzyme can catalyze a reaction. It is reached when all enzyme active sites are saturated with substrate.

The substrate concentration at which the reaction velocity is half of Vmax. It is a measure of an enzyme's affinity for its substrate.

The state where an enzyme is working at its maximum activity, with all active sites bound to substrate.

The increase in reaction velocity as temperature increases up to a certain point. This happens because the molecules have more energy and collide more frequently.

The decrease in reaction velocity as temperature rises above its optimal point. This occurs because the enzyme starts to denature (lose its shape) and loses its ability to function.

Changes in pH can alter the ionization state of amino acids in the active site, affecting enzyme-substrate interactions and ultimately the reaction rate.

Extreme pH values can cause the enzyme to denature, meaning it loses its structure and function. This is similar to how high temperature can denature enzymes.

The relationship between the reaction velocity of an enzyme-catalyzed reaction and the substrate concentration. It is typically represented as a hyperbolic curve.