TEM1 Class Antibiotic Resistance Proteins

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Structural highlights

Background and History

Antibiotics have long been the primary line of defense against many infections. The advent of penicillin in the 1930s brought an end to an era of uncertainty: diseases once considered fatal became treatable. Unfortunately, natural selection stops for no species. Resistance to some form of antibiotic now has become standard for many infections.[A] Moreover, their liberal usage have resulted in “superbugs”, which are resistant to multiple antibiotics.[B] These strains are capable of secreting enzymes capable of deactivating the antibiotic or modifying their cell walls to render the antibiotic ineffective. Many antibiotics such as penicillin, their derivatives (penams), and cephalosporins (cephams) possess a β-lactam ring (Figure 1). Figure 1. The beta-lactam ring is highlighted in red. Beta-lactamases function in hydrolyzing the amide bond within the ring, rendering the antibiotic ineffective. (Image Credit: Wikipedia)

β-Lactamases function by hydrolyzing the β-lactam ring within the antibiotic (Figure 2). This prevents the interaction between the cell wall and the antibiotic.

Image:Figure2.jpeg Figure 2. Bacteria are capable of becoming antibiotic resistant by catalyzing the hydrolysis of the β-lactam ring.

The TEM-1 subclass is one of the most common of all β-Lactamases.[3] Their prevalence began when bacteria started exhibiting penicillin resistance on a mass scale. Since the TEM-1 subclass has been prevalent for many years, many inhibitors have either been discovered or synthesized to prevent their catalytic function.

Function

Disease

Relevance

Structural highlights

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