TY - JOUR
T1 - Extended-spectrum AmpC cephalosporinase in Acinetobacter baumannii
T2 - ADC-56 confers resistance to cefepime
AU - Tian, Guo Bao
AU - Adams-Haduch, Jennifer M.
AU - Taracila, Magdalena
AU - Bonomo, Robert A.
AU - Wang, Hong Ning
AU - Doi, Yohei
PY - 2011/10
Y1 - 2011/10
N2 - 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.
AB - 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.
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UR - http://www.scopus.com/inward/citedby.url?scp=80052863427&partnerID=8YFLogxK
U2 - 10.1128/AAC.00704-11
DO - 10.1128/AAC.00704-11
M3 - Article
C2 - 21788456
AN - SCOPUS:80052863427
SN - 0066-4804
VL - 55
SP - 4922
EP - 4925
JO - Antimicrobial agents and chemotherapy
JF - Antimicrobial agents and chemotherapy
IS - 10
ER -
