Sandbox 130
From Proteopedia
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==New Delhi Metallo-Beta-Lactamase== | ==New Delhi Metallo-Beta-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-beta-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. | ||
| - | <scene name='37/372730/Asymmetrical_4eyl/2'>'''Asymmetrical Structure NMD1'''</scene> | ||
Revision as of 18:40, 18 July 2016
New Delhi Metallo-Beta-Lactamase
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The New Delhi metallo-beta-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.
