TEM1 Class Antibiotic Resistance Proteins
From Proteopedia
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== 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). |
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[[Image:Beta-Lactam-Ring.png]] | [[Image:Beta-Lactam-Ring.png]] | ||
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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]] | ||
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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')
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References
- ↑ Hanson, R. M., Prilusky, J., Renjian, Z., Nakane, T. and Sussman, J. L. (2013), JSmol and the Next-Generation Web-Based Representation of 3D Molecular Structure as Applied to Proteopedia. Isr. J. Chem., 53:207-216. doi:http://dx.doi.org/10.1002/ijch.201300024
- ↑ Herraez A. Biomolecules in the computer: Jmol to the rescue. Biochem Mol Biol Educ. 2006 Jul;34(4):255-61. doi: 10.1002/bmb.2006.494034042644. PMID:21638687 doi:10.1002/bmb.2006.494034042644
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