Abstract
ADC-56, a novel extended-spectrum AmpC (ESAC) β-lactamase, was identified in an Acinetobacter baumannii clinical isolate. ADC-56 possessed an R148Q change compared with its putative progenitor, ADC-30, which enabled it to hydrolyze cefepime. Molecular modeling suggested that R148 interacted with Q267, E272, and I291 through a hydrogen bond network which constrained the H-10 helix. This permitted cefepime to undergo conformational changes in the active site, with the carboxyl interacting with R340, likely allowing for better binding and turnover.
| Original language | English |
|---|---|
| Pages (from-to) | 4922-4925 |
| Number of pages | 4 |
| Journal | Antimicrobial agents and chemotherapy |
| Volume | 55 |
| Issue number | 10 |
| DOIs | |
| Publication status | Published - 10-2011 |
| Externally published | Yes |
UN SDGs
This output contributes to the following UN Sustainable Development Goals (SDGs)
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SDG 3 Good Health and Well-being
All Science Journal Classification (ASJC) codes
- Pharmacology
- Pharmacology (medical)
- Infectious Diseases
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