KMID : 1234520120070020089
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Korean Journal of Urogenital Tract Infection Inflammation 2012 Volume.7 No. 2 p.89 ~ p.98
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The Mechanism of Extended Spectrum ¥â-Lactamase
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Kim Ki-Ho
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Abstract
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¥â-lactamases are the most widespread cause of bacterial resistance to ¥â-lactam antibiotics, such as the penicillins and cephalosporins, and the mechanisms of these enzymes are intensely studied. The first ¥â-lactamase was identified in an isolate of Escherichia coli in 1940. Many of the gram-negative bacteria possess a naturally occurring, chromosomally mediated ¥â-lactamase, which probably assists the bacteria in finding a niche when faced with competition from other bacteria that naturally produce ¥â-lactams. ¥â-lactamases are classified into two major types on the basis of the main component of the active site: serine¥â-lactamases and metallo-¥â-lactamases. Serine¥â-lactamases are further classified into three classes: class A, C, and D; i.e., metallo¥â-lactamase is classified into class B. As is well known, the catalytic mechanism of serine¥â -lactamases involves acylation and deacylation. In this paper, we have investigated the mechanisms of class A ¥â-lactamase, most of which have extended spectrum ¥â-lactamases belonging to that of the other classes B, C, and D ¥â-lactamase.
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KEYWORD
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¥â-Lactamases, Mechanism of action
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