Sandbox 122
From Proteopedia
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==New Delhi Metallo-Beta-Lactamase== | ==New Delhi Metallo-Beta-Lactamase== | ||
| + | The New Delhi metallo-beta-lactamse <scene name='37/372723/Asymmetrical_4eyl/5'>(NDM-1)</scene> in complex with meropenem demonstrates the mechanism in which the active site binds and hydrolyzes the 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. Zn1 also acts to suppress the pka of the hydrolytic water to (~5-6) to facilitate it's nucleophillic 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. Zn1 also acts to suppress the pka of the hydrolytic water to (~5-6) to facilitate it's nucleophillic role. | ||
<Structure load='4eyl' size='350' frame='true' align='right' caption='Insert caption here' scene='Insert optional scene NDM1' /> | <Structure load='4eyl' size='350' frame='true' align='right' caption='Insert caption here' scene='Insert optional scene NDM1' /> | ||
Revision as of 18:46, 18 July 2016
New Delhi Metallo-Beta-Lactamase
The New Delhi metallo-beta-lactamse in complex with meropenem demonstrates the mechanism in which the active site binds and hydrolyzes the 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. Zn1 also acts to suppress the pka of the hydrolytic water to (~5-6) to facilitate it's nucleophillic role.
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