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Chapter 5: Problem 1

Why would you want to design a drug that is an enzyme inhibitor?

Short Answer

Expert verified
Drugs are designed as enzyme inhibitors to treat diseases where certain enzymes play a crucial role. By inhibiting the action of these enzymes, these drugs can control or prevent disease progression. This is especially beneficial in diseases like HIV, where enzyme inhibitors prevent the virus replication, thus halting disease progression.

Step by step solution

01

Understanding Enzymes

Enzymes are proteins that act as catalysts inside the body, speeding up the rate of specific biochemical reactions. They play essential roles in various bodily functions including digestion and metabolism. Their function is dependent on their structure and they usually have a specific place called an active site where the chemical reactions occur.
02

The Role of Enzymes in Diseases

While enzymes are necessary for normal bodily functions, they can also contribute to disease conditions. Some diseases are due to the overactivity or underactivity of certain enzymes. For example, HIV, a deadly virus that causes AIDS, uses a specific enzyme to replicate itself.
03

Understanding Enzyme Inhibitors

Enzyme inhibitors are molecules that bind to enzymes and decrease their activity. They are often used in medicines to diminish the action of enzymes and alleviate disease symptoms. They work by binding to the active site of an enzyme, thus preventing it from fulfilling its role.
04

Importance of Enzyme Inhibitors in Drug Design

Designing a drug that acts as an enzyme inhibitor can be especially beneficial in treating diseases where specific enzymes play a crucial role. By blocking these enzymes, it's possible to control or stop the progression of the disease. For instance, many of the drugs used to treat HIV are enzyme inhibitors that block the action of the enzyme the virus uses to replicate itself, thus halting the progression of the disease.

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Most popular questions from this chapter

S-Adenosylmethionine (SAM) is biosynthesized from methionine and ATP, catalyzed by methionine adenosyl transferase. The mechanism is shown below. a. Design a competitive reversible inhibitor for this enzyme. b. Design a multi-substrate analogue inhibitor, and show the basis for your design.

If you wanted to inhibit an enzyme in a microorganism that is also in humans, what approaches would you take in your research?

GABA aminotransferase catalyzes a PLP-dependent conversion of GABA to succinic semialdehyde (see Section 5.3.3.3.1). a. Draw a mechanism for how 6 inactivates this enzyme. b. A hypothetical anticonvulsant drug that inhibits GABA aminotransferase was given to a patient in overdose quantities. Not only did the patient stop convulsing, but he went into a coma. If the problem was that the GABA concentration became too high, mention two possible solutions to the problem.

What advantage does a slow, tight-binding inhibitor have over a simple reversible inhibitor?

a. Two isoforms of an enzyme were discovered; isoform-1 produces a hormone that causes muscle spasms and isoform-2 makes another hormone from the same substrate that lowers cholesterol levels. What would you do to prevent muscle spasms without raising cholesterol levels? b. If the active sites of isoform-1 and \(-2\) are the same except isoform-1 has a cysteine residue and isoform-2 has a phenylalanine residue at that same position, what two approaches would you take for a muscle spasm drug without a cholesterol level increase side effect?
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