Sandbox Reserved 988: Difference between revisions

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One of the main causes of [http://en.wikipedia.org/wiki/Antimicrobial_resistance resistance] to β-lactam antibiotics is caused by β-lactamase enzymes. Chemically, β-lactamases and PBPs bind to β-lactam antibiotics in similar mechanisms. The catalytic serine of both enzymes performs a nucleophilic attack on to the carbonyl group in the β-lactam functional group of the antibiotic. ~~However~~, β-lactamases are ~~then~~ able to undergo [http://en.m.wikipedia.org/wiki/Acetylation deacylation]. This process cleaves the β-lactam ring, ridding the β-lactam antibiotic of its antimicrobial activity. <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> The cleaved β-lactam antibiotic is ~~rendered incapable of inhibiting~~ 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 antibiotics is caused by β-lactamase enzymes. Chemically, β-lactamases and PBPs bind to β-lactam antibiotics in similar mechanisms. The catalytic serine of both enzymes performs a nucleophilic attack on to the carbonyl group in the β-lactam functional group of the antibiotic. Unlike PBPs, where the β-lactam antibiotics bind irreversibly, β-lactamases are able to undergo [http://en.m.wikipedia.org/wiki/Acetylation deacylation] in order to regenerate their active site. This process cleaves the β-lactam ring, ridding the β-lactam antibiotic of its antimicrobial activity. <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> The cleaved β-lactam antibiotic is unable to inhibit PBPs, allowing cross-linking to occur for adequate cell wall formation.

Sandbox Reserved 988: Difference between revisions

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Revision as of 20:01, 14 December 2015 view source Paul Thomas Morse (talk \| contribs) 81 edits No edit summary ← Older edit		Latest revision as of 20:08, 14 December 2015 view source Paul Thomas Morse (talk \| contribs) 81 edits No edit summary
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	One of the main causes of [http://en.wikipedia.org/wiki/Antimicrobial_resistance resistance] to β-lactam antibiotics is caused by β-lactamase enzymes. Chemically, β-lactamases and PBPs bind to β-lactam antibiotics in similar mechanisms. The catalytic serine of both enzymes performs a nucleophilic attack on to the carbonyl group in the β-lactam functional group of the antibiotic. ~~However~~, β-lactamases are ~~then~~ able to undergo [http://en.m.wikipedia.org/wiki/Acetylation deacylation]. This process cleaves the β-lactam ring, ridding the β-lactam antibiotic of its antimicrobial activity. <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> The cleaved β-lactam antibiotic is ~~rendered incapable of inhibiting~~ 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 antibiotics is caused by β-lactamase enzymes. Chemically, β-lactamases and PBPs bind to β-lactam antibiotics in similar mechanisms. The catalytic serine of both enzymes performs a nucleophilic attack on to the carbonyl group in the β-lactam functional group of the antibiotic. Unlike PBPs, where the β-lactam antibiotics bind irreversibly, β-lactamases are able to undergo [http://en.m.wikipedia.org/wiki/Acetylation deacylation] in order to regenerate their active site. This process cleaves the β-lactam ring, ridding the β-lactam antibiotic of its antimicrobial activity. <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> The cleaved β-lactam antibiotic is unable to inhibit PBPs, allowing cross-linking to occur for adequate cell wall formation.