Sandbox Reserved 992: Difference between revisions
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[[Image:Beta lactamase mechaism.jpg|1000px|thumb|center|Class C β-lactamase general mechanism, showing covalently bound β-lactam antibiotic in intermidiate state.]] | [[Image:Beta lactamase mechaism.jpg|1000px|thumb|center|Class C β-lactamase general mechanism, showing covalently bound β-lactam antibiotic in intermidiate state.]] | ||
Class C β-lactamases, among many other enzyme types, also contain a structural component known as an oxyanion hole. This pocket of hydrophilic residues directly stabilizes the high-energy tetrahedral intermediate, lowering the activation energy and promoting a faster overall reaction.<ref>Albert Lehninger et al. (2008). Principles of Biochemistry (5th ed.). Macmillan. p. 207.</ref><ref>Livermore, David. β-Lactamase mediated resistance and opportunities for its control. J. Antimicrob. Chemother. (1998) 41 (suppl 4): 25-41.</ref> | Class C β-lactamases, among many other enzyme types, also contain a structural component known as an [http://en.m.wikipedia.org/wiki/Oxyanion_hole oxyanion hole]. This pocket of [http://en.m.wikipedia.org/wiki/Hydrophile hydrophilic] residues directly stabilizes the high-energy [http://en.m.wikipedia.org/wiki/Tetrahedral_carbonyl_addition_compound tetrahedral intermediate], lowering the activation energy and promoting a faster overall reaction.<ref>Albert Lehninger et al. (2008). Principles of Biochemistry (5th ed.). Macmillan. p. 207.</ref><ref>Livermore, David. β-Lactamase mediated resistance and opportunities for its control. J. Antimicrob. Chemother. (1998) 41 (suppl 4): 25-41.</ref> | ||
== Clinical Significance == | == Clinical Significance == | ||
