Class C beta-lactamase
From Proteopedia
(Difference between revisions)
| Line 5: | Line 5: | ||
== Background and beta-lactam antibiotics == | == Background and beta-lactam antibiotics == | ||
<StructureSection load='1stp' size='340' side='right' caption='Caption for this structure' scene=''> | <StructureSection load='1stp' size='340' side='right' caption='Caption for this structure' scene=''> | ||
| - | Since the discovery of penicillin in the late 1920s, β-lactam antibiotics, characterized by their central chemical structure, the β-lactam ring, have played an important role in human health (Fig 1). Unfortunately, extensive use, and often misuse, of such drugs has led to an increased resistance in many species of bacterium resulting in major clinical treatment dilemmas. Each year in the United States alone, a minimum of 2 million people are infected with drug-resistant bacteria and of those 2 million, at least 23,000 infections result in fatality. | + | Since the discovery of penicillin in the late 1920s, β-lactam antibiotics, characterized by their central chemical structure, the β-lactam ring, have played an important role in human health (Fig 1). Unfortunately, extensive use, and often misuse, of such drugs has led to an increased resistance in many species of bacterium resulting in major clinical treatment dilemmas. Each year in the United States alone, a minimum of 2 million people are infected with drug-resistant bacteria and of those 2 million, at least 23,000 infections result in <ref>fatality.<ref/> |
[[Image:Beta-lactam.jpg]] | [[Image:Beta-lactam.jpg]] | ||
| Line 11: | Line 11: | ||
The β-lactam ring covalently attaches to PBPs, inhibiting them from executing their role in properly synthesizing the cell wall peptidoglycan layer, via nucleophilic attack of the carbonyl carbon (Fig 3). The β-lactam cannot be removed and thus permanently renders the PBP incapable of its catalytic function in cross-linking. Ultimately, this results in death of bacterial cells from osmotic instability or autolysis | The β-lactam ring covalently attaches to PBPs, inhibiting them from executing their role in properly synthesizing the cell wall peptidoglycan layer, via nucleophilic attack of the carbonyl carbon (Fig 3). The β-lactam cannot be removed and thus permanently renders the PBP incapable of its catalytic function in cross-linking. Ultimately, this results in death of bacterial cells from osmotic instability or autolysis | ||
| + | |||
| + | ==References== | ||
| + | <references/> | ||
Revision as of 19:58, 22 February 2015
Beta-lactamases are awesome
|
Background and beta-lactam antibiotics
| |||||||||||
