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Some bacteria produce the enzyme \(\beta\) -lactamase, which cleaves and opens lactam rings. How would the presence of \(\beta\) -lactamase affect bacterial sensitivity to penicillin?

Short Answer

Expert verified
The presence of \\(\beta\\)-lactamase makes bacteria resistant to penicillin.

Step by step solution

01

Understanding \\(\beta\\)-lactamase Function

The enzyme \(\beta\)-lactamase breaks open the lactam rings, a critical structure in penicillin and similar antibiotics. This action deactivates the antibiotic, preventing it from inhibiting bacterial cell wall synthesis.
02

Effect on Penicillin's Action

Penicillin works by disrupting the synthesis of bacterial cell walls, leading to cell lysis and death. Without intact lactam rings, penicillin cannot bind to its target enzymes effectively.
03

Assessing Sensitivity Changes

With \(\beta\)-lactamase present, penicillin becomes ineffective as it can no longer compromise the bacterial cell wall structure. This leads to reduced sensitivity or resistance of the bacteria to penicillin.

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Key Concepts

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

β-lactamase
β-lactamase is an enzyme produced by some bacteria that is a key player in antibiotic resistance. It targets antibiotics with a β-lactam structure, such as penicillin. These antibiotics have a crucial four-membered lactam ring that is essential for their antimicrobial action. This enzyme works by cleaving or breaking down this ring structure.

Once the β-lactam ring is broken, the antibiotic is rendered ineffective because it can no longer bind to the bacterial enzymes responsible for cell wall construction. This action thus protects bacteria from being destroyed by the antibiotic, allowing them to survive even in the presence of drugs designed to kill them.
  • Breaks the β-lactam ring in penicillin.
  • Makes antibiotics ineffective.
  • Provides a survival advantage to bacteria.
Understanding β-lactamase is crucial for grasping how antibiotic resistance arises and why certain bacterial infections are difficult to treat with conventional antibiotics.
Penicillin mechanism
Penicillin is a widely used antibiotic known for its ability to combat various bacterial infections. It works by interfering with the cell wall synthesis of bacteria. Bacterial cell walls are vital for maintaining structural integrity and protecting the cell from bursting due to internal pressure.

Penicillin specifically targets the penicillin-binding proteins (PBPs) involved in the last steps of cell wall synthesis. It binds to these proteins and inhibits their activity, which disrupts the formation of peptidoglycan, an essential component of the bacterial cell wall.
  • Targets the bacterial cell wall.
  • Inhibits penicillin-binding proteins.
  • Causes cell lysis and bacterial death.
This mechanism is highly effective against actively growing bacteria, which is why penicillin and similar antibiotics are essential in treating infections caused by bacterial pathogens.
Antibiotic resistance
Antibiotic resistance is a growing concern in the medical field. It occurs when bacteria evolve mechanisms to withstand the effects of antibiotics. The presence of β-lactamase is a common example of such resistance. When bacteria produce this enzyme, they can deactivate antibiotics like penicillin, making standard treatments ineffective.

Resistance can result from spontaneous mutations or be acquired through horizontal gene transfer, where bacteria share resistance genes. This sharing can happen through plasmids, small DNA molecules independent of chromosomal DNA.
  • Deactivates antibiotics like penicillin.
  • Results from genetic mutations or gene transfer.
  • Leads to ineffective standard treatments.
Addressing antibiotic resistance involves developing new drugs and strategies to minimize its spread, such as using antibiotics judiciously and enhancing infection control measures.
Cell wall synthesis
The bacterial cell wall is a vital component that provides structural support and protection. It consists mainly of peptidoglycan, a network of sugars and amino acids that forms a mesh-like layer outside the bacterial cell membrane.

Cell wall synthesis is a multi-step process that involves several enzymes, including transpeptidases, which help cross-link the peptidoglycan molecules. Penicillin targets and inactivates these enzymes, disrupting the cell wall's construction and leading to bacterial lysis.
  • Essential for bacterial integrity and survival.
  • Composed of peptidoglycan.
  • Targeted by penicillin to cause bacterial death.
A thorough understanding of cell wall synthesis is key to developing new antibiotics, as each step in the process presents a potential target for drug development, especially in overcoming resistance mechanisms.

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Most popular questions from this chapter

The effect of \(\mathrm{pH}\) on the activity of an enzyme was examined. At its active site, the enzyme has an ionizable group that must be negatively charged in order for substrate binding and catalysis to take place. The ionizable group has a \(\mathrm{p} K_{\mathrm{a}}\) of \(6.0 .\) The substrate is positively charged throughout the \(\mathrm{pH}\) range of the experiment. (EQUATION CAN'T COPY) (a) Draw the \(V_{0}\) -versus-pH curve when the substrate concentration is much greater than the \(K_{M}\) of the enzyme. (b) Draw the \(V_{0}\) -versus-pH curve when the substrate concentration is much less than the \(K_{M}\) of the enzyme. (c) At which \(\mathrm{pH}\) will the velocity equal one-half of the maximal velocity attainable under the conditions described in (b)?

Match the term with the description or compound. (a) Competitive inhibition_____ (b) Uncompetitive inhibition_____ (c) Noncompetitive inhibition_____ 1\. Inhibitor and substrate can bind simultaneously 2\. \(V_{\text {max }}\) remains the same but the \(K_{\mathrm{M}}^{\text {app }}\) increases 3\. Sulfanilamide 4\. Binds to the enzymesubstrate complex only 5\. Lowers \(V_{\max }\) and \(K_{M}^{\text {app }}\) 6\. Roundup 7\. \(K_{M}\) remains unchanged but \(V_{\text {max }}\) is lower 8\. Doxycycline 9\. Inhibitor binds at the active site

Succinylcholine is a fast-acting, short-duration muscle relaxant that is used when a tube is inserted into a patient's trachea or when a bronchoscope is used to examine the trachea and bronchi for signs of cancer. Within seconds of the administration of succinylcholine, the patient experiences muscle paralysis and is placed on a respirator while the examination proceeds. Succinylcholine is a competitive inhibitor of acetylcholinesterase, a nervous system enzyme, and this inhibition causes paralysis. However, succinylcholine is hydrolyzed by blood-serum cholinesterase, which shows broader substrate specificity than does the nervous system enzyme. Paralysis lasts until the succinylcholine is hydrolyzed by the serum cholinesterase, usually several minutes later. (a) As a safety measure, serum cholinesterase is measured before the examination takes place. Explain why this measurement is good idea. (b) What would happen to the patient if the serum cholinesterase activity were only 10 units of activity per liter rather than the normal activity of about 80 units? (c) Some patients have a mutant form of the serum cholinesterase that displays a \(K_{M}\) of \(10 \mathrm{mM},\) rather than the normal 1.4 mM. What will be the effect of this mutation on the patient?

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