Sandbox 130
From Proteopedia
(Difference between revisions)
| Line 1: | Line 1: | ||
| - | <Structure load='4eyl' size='350' frame='true' align='right' caption='Insert caption here' scene='NDN1' /> | + | ==New Delhi Metallo-Beta-Lactamase== |
| + | <Structure load='4eyl' size='350' frame='true' align='right' caption='Insert caption here' scene='NDN1' /> | ||
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 18:04, 18 July 2016
New Delhi Metallo-Beta-Lactamase
|
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.
