Sandbox 130
From Proteopedia
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The New Delhi metallo-β-lactamase (<scene name='37/372730/Asymmetrical_4eyl/2'>NMD-1</scene>) in complex with meropenem demonstrates the mechanism in which the active site binds and hydrolyzed the a carbapenem, in this case meropenem. | The New Delhi metallo-β-lactamase (<scene name='37/372730/Asymmetrical_4eyl/2'>NMD-1</scene>) in complex with meropenem demonstrates the mechanism in which the active site binds and hydrolyzed the a carbapenem, in this case meropenem. | ||
Zn1 (coordinated by three histidine residues), acts as a major constituent of oxyanion hole to stabilize tetrahedral intermediate. It also acts as a Lewis acid for interaction with lactam carbonyl in Michaelis complex and acts to suppress the pKa of the hyrdolytic water to (~5-6) to facilitate it's nucleophilic role. | Zn1 (coordinated by three histidine residues), acts as a major constituent of oxyanion hole to stabilize tetrahedral intermediate. It also acts as a Lewis acid for interaction with lactam carbonyl in Michaelis complex and acts to suppress the pKa of the hyrdolytic water to (~5-6) to facilitate it's nucleophilic role. | ||
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Revision as of 17:31, 19 July 2016
New Delhi Metallo-β-Lactamase
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The New Delhi metallo-β-lactamase () in complex with meropenem demonstrates the mechanism in which the active site binds and hydrolyzed the a carbapenem, in this case meropenem. Zn1 (coordinated by three histidine residues), acts as a major constituent of oxyanion hole to stabilize tetrahedral intermediate. It also acts as a Lewis acid for interaction with lactam carbonyl in Michaelis complex and acts to suppress the pKa of the hyrdolytic water to (~5-6) to facilitate it's nucleophilic role.
β β β β
