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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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Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

Wayne Decatur, Student, Meng Han Liu, Allison Granberry