Sandbox 130
From Proteopedia
(Difference between revisions)
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| - | ==New Delhi Metallo- | + | ==New Delhi Metallo-β-Lactamase== |
<Structure load='4eyl' size='350' frame='true' align='right' caption='Insert caption here' scene='Insert optional scene name here NDN1' /> | <Structure load='4eyl' size='350' frame='true' align='right' caption='Insert caption here' scene='Insert optional scene name here NDN1' /> | ||
| - | The New Delhi metallo- | + | 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. | ||
Revision as of 17:27, 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.
