Sandbox Reserved 992: Difference between revisions
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{{Sandbox_gvsu_chm463}}<!-- PLEASE ADD YOUR CONTENT BELOW HERE --> | {{Sandbox_gvsu_chm463}}<!-- PLEASE ADD YOUR CONTENT BELOW HERE --> | ||
'''Class C β-lactamases''' are a subcategory of β-lactamase enzymes. These enzymes are produced by some bacteria and result in their resistance to a variety of β-lactam antibiotics. β-lactam antibiotics are classified based on their chemical structure which contains a four membered, amide containing ring known as the β-lactam ring. <scene name='69/691534/Class_c_beta-lactamase/1'>Class C β-lactamases</scene> specifically target [http://en.m.wikipedia.org/wiki/Cephalosporin cephalosporin] antibiotics and deactivate their antimicrobial activity by hydrolyzing the [http://en.m.wikipedia.org/wiki/Β-lactam β-lactam ring]. | '''Class C β-lactamases''' are a subcategory of β-lactamase enzymes. These enzymes are produced by some bacteria and result in their resistance to a variety of β-lactam antibiotics. β-lactam antibiotics are classified based on their chemical structure which contains a four membered, amide containing ring known as the β-lactam ring. <scene name='69/691534/Class_c_beta-lactamase/1'>Class C β-lactamases</scene><ref>Powers, Rachel, Hollister C. Swanson, Magdalena A. Taracila, Nicholas W. Florek, Chiara Romagnoli, Emilia Caselli, Fabio Prati, Robert A. Bonomo, and Bradley J. Wallar. Biochemical and Structural Analysis of Inhibitors Targeting the ADC-7 Cephalosporinase of Acinetobacter baumannii. Biochemistry, 2014, 53 (48), 7670-7679.</ref> specifically target [http://en.m.wikipedia.org/wiki/Cephalosporin cephalosporin] antibiotics and deactivate their antimicrobial activity by hydrolyzing the [http://en.m.wikipedia.org/wiki/Β-lactam β-lactam ring]. | ||
<Structure load='1ke4' size='400' frame='true' color='white' align='right' caption='Class C Beta-lactamase' /> | <Structure load='1ke4' size='400' frame='true' color='white' align='right' caption='Class C Beta-lactamase' /> | ||
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</ref> | </ref> | ||
One of the main causes of [http://en.wikipedia.org/wiki/Antimicrobial_resistance resistance] to β-lactam drugs is caused by β-lactamases. Chemically, β-lactamases bind to β-lactams the same way β-lactams bind to PBPs. However, the β-lactamases are then able to deactivate the antimicrobial activity of the β-lactams by cleaving the β-lactam bound in the active site through a molecular process called [http://en.m.wikipedia.org/wiki/Acetylation deacylation], rendering it incapable of inhibiting the PBPs and ultimately, allowing cross-linking to occur for adequate cell wall formation. | One of the main causes of [http://en.wikipedia.org/wiki/Antimicrobial_resistance resistance] to β-lactam drugs is caused by β-lactamases. Chemically, β-lactamases bind to β-lactams the same way β-lactams bind to PBPs. However, the β-lactamases are then able to deactivate the antimicrobial activity of the β-lactams by cleaving the β-lactam bound in the <scene name='69/691534/Class_c_beta-lactamase_as/2'>active site</scene><ref>Powers, Rachel, Hollister C. Swanson, Magdalena A. Taracila, Nicholas W. Florek, Chiara Romagnoli, Emilia Caselli, Fabio Prati, Robert A. Bonomo, and Bradley J. Wallar. Biochemical and Structural Analysis of Inhibitors Targeting the ADC-7 Cephalosporinase of Acinetobacter baumannii. Biochemistry, 2014, 53 (48), 7670-7679.</ref> through a molecular process called [http://en.m.wikipedia.org/wiki/Acetylation deacylation], rendering it incapable of inhibiting the PBPs and ultimately, allowing cross-linking to occur for adequate cell wall formation. | ||
[[Image:Beta-lactam inhibition.png|500px|thumb|center|Image showing mechanism performed by β-lactam antibiotic within PBP [http://en.m.wikipedia.org/wiki/Active_site active site].]] | [[Image:Beta-lactam inhibition.png|500px|thumb|center|Image showing mechanism performed by β-lactam antibiotic within PBP [http://en.m.wikipedia.org/wiki/Active_site active site].]] | ||