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What is an active site? a. the location in an enzyme where substrates bind and react b. the place where a molecule or ion binds to an inactive protein to induce a shape change c. the portion of a motor protein involved in moving cargo in a cell d. the site on an antibody where it binds to bacterial cells or viruses

Short Answer

Expert verified
The correct answer is \(a. \) the location in an enzyme where substrates bind and react.

Step by step solution

01

Active Site Definition

An active site is a region on an enzyme where substrates bind, and the biochemical reaction occurs within the catalytic process. It is usually a small, specific pocket or groove on the enzyme's surface that fits the substrate. Now, let's look at the options and choose the one that fits this definition. a. the location in an enzyme where substrates bind and react b. the place where a molecule or ion binds to an inactive protein to induce a shape change c. the portion of a motor protein involved in moving cargo in a cell d. the site on an antibody where it binds to bacterial cells or viruses
02

Compare Definitions and Options

Comparing the definition of an active site to the given options, we can see that option (a) fits the definition perfectly. a. the location in an enzyme where substrates bind and react
03

Answer

Therefore, the correct answer is: \(a. \) the location in an enzyme where substrates bind and react.

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Key Concepts

These are the key concepts you need to understand to accurately answer the question.

Enzyme Catalysis
Enzyme catalysis is a process where enzymes accelerate chemical reactions by lowering the activation energy needed for the reaction to occur. This is akin to a helper reducing the effort you need to push a heavy object uphill. An enzyme's active site plays a crucial role in this process. It's where the magic happens—substrates, which are the molecules the enzyme acts upon, snugly fit into the active site like a key in a lock. This precise fit is necessary for the enzyme to work efficiently.

Once the substrate is in place, the enzyme might stress certain bonds, which makes them easier to break, or bring substrate molecules close together to encourage a reaction. After the reaction, the products are released, and the enzyme is ready to assist in another reaction, often thousands of times over. It's like a tiny, highly efficient assembly line worker, tirelessly performing its task.
Substrate Binding
Substrate binding is the interaction between an enzyme and the molecules it acts upon, the substrates. This interaction is highly specific; an enzyme typically recognizes its substrate with a precision that's been likened to a lock and key fit. This specificity is due to the unique three-dimensional shape of the enzyme's active site.

Substrates will bind to the active site through various types of bonds—hydrogen bonds, ionic bonds, or transient covalent bonds. This interaction can result in a change in the enzyme's shape, known as induced fit, which can help catalyze the reaction further. Fundamentally, understanding substrate binding is critical because it establishes the foundation for everything enzymes do in catalyzing biological reactions.
Biochemical Reactions
Biochemical reactions are transformations that occur within living organisms to sustain life. These reactions are often complex and must occur with the perfect balance and speed to maintain homeostasis. Enzymes are the catalysts that make these reactions work at speeds necessary for life.

Biochemical reactions can include processes like breaking down nutrients for energy, synthesizing new cellular components, and responding to environmental changes. The active site of an enzyme is where specific substrates are transformed into products through biochemical reactions. Without enzymes to speed up these reactions, most would progress at imperceptibly slow rates, and life as we know it would not exist.

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Most popular questions from this chapter

Make a concept map (see BioSkills 12 ) that relates the four levels of protein structure and shows how they can contribute to the formation of hemoglobin. Your map should include the following boxed terms: Primary structure, Secondary structure, Tertiary structure, Quaternary structure, Active site, Amino acid sequence, R-groups, \(\alpha\) -Helices.

Explain how molecular chaperones facilitate protein folding in many different polypeptides, each with their own specific shape.

Gluten is a mixture of proteins abundant in wheat, barley, and rye. Although these grains are staples in the Western diet, almost 1 percent of Americans have celiac disease- a disorder of the intestines caused by an abnormal immune response after eating gluten. This immune response damages the fingerlike villi of the small intestine, which can lead to intestinal upset and malnourishment. Currently, the only treatment is to maintain a strict gluten- free diet. When you eat gluten, enzymes present in your stomach and intestines digest all but a few short peptides. How do enzymes accomplish this activity? a. The active site of an enzyme binds to a gluten protein and facilitates the hydrolysis reaction that breaks apart peptide bonds. b. An enzyme binds to the active site of a gluten protein and speeds up the condensation reaction that breaks apart peptide bonds. c. The active site of an enzyme binds to a gluten protein and reacts with it to break apart hydrogen bonds. d. An enzyme binds to the active site of a gluten protein and catalyzes the reactions that break apart hydrogen bonds.

If proteins could fold only into rigid, inflexible structures, how might this affect the cell's ability to regulate their function?

Gluten is a mixture of proteins abundant in wheat, barley, and rye. Although these grains are staples in the Western diet, almost 1 percent of Americans have celiac disease- a disorder of the intestines caused by an abnormal immune response after eating gluten. This immune response damages the fingerlike villi of the small intestine, which can lead to intestinal upset and malnourishment. Currently, the only treatment is to maintain a strict gluten- free diet. One of the peptides that can be recovered after gluten digestion is 33 residues long; 13 of the 33 residues are proline. How many times would you expect proline to appear in this peptide if it were made up of a completely random assortment of the 20 most common amino acids?

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