TEM1 Class Antibiotic Resistance Proteins: Difference between revisions
From Proteopedia
Jump to navigationJump to search
No edit summary |
No edit summary |
||
| Line 14: | Line 14: | ||
== Background and History == | == 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. | 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). | Many antibiotics such as penicillin, their derivatives (penams), and cephalosporins (cephams) possess a β-lactam ring (Figure 1). | ||
[[Image:Beta-Lactam-Ring.png]] | [[Image:Beta-Lactam-Ring.png]] | ||
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) | 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. | 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. | |||
[[Image:Figure2.jpg]] | |||
Figure 2. Bacteria are capable of becoming antibiotic resistant by catalyzing the hydrolysis of the β-lactam ring. | Figure 2. Bacteria are capable of becoming antibiotic resistant by catalyzing the hydrolysis of the β-lactam ring. | ||
Revision as of 22:47, 13 April 2016
Your Heading Here (maybe something like 'Structure')
| ||||||||||||
References
Proteopedia Page Contributors and Editors (what is this?)
Ryan Hunter Wilson, Matt O'Malley, Kenna Salvatore, Riley Culhane, Michal Harel

