期刊
ANTIMICROBIAL AGENTS AND CHEMOTHERAPY
卷 55, 期 10, 页码 4922-4925出版社
AMER SOC MICROBIOLOGY
DOI: 10.1128/AAC.00704-11
关键词
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资金
- National Institute of Health [K22AI080584, R03AI079296]
- China Scholarship Council (CSC)
- Pennsylvania Department of Health [4100047864]
- Veterans Affairs Merit Review Program
- Geriatric Research Education and Clinical Care (GRECC)
- National Institutes of Health [R01 AI072219]
ADC-56, a novel extended-spectrum AmpC (ESAC) beta-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.
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