کد مقاله | کد نشریه | سال انتشار | مقاله انگلیسی | نسخه تمام متن |
---|---|---|---|---|
1391749 | 983632 | 2013 | 9 صفحه PDF | دانلود رایگان |

• OXA-23 is the major carbapenemase in Acinetobacter
• Antibiotic susceptibility and enzyme kinetics of OXA-23 have been determined
• The crystal structure of OXA-23 has been solved by X-ray crystallography
• The structure of a wild-type CHDL complexed with a carbapenem substrate is presented
SummaryDissemination of Acinetobacter baumannii strains harboring class D β-lactamases producing resistance to carbapenem antibiotics severely limits our ability to treat deadly Acinetobacter infections. Susceptibility determination in the A. baumannii background and kinetic studies with a homogeneous preparation of OXA-23 β-lactamase, the major carbapenemase present in A. baumannii, document the ability of this enzyme to manifest resistance to last-resort carbapenem antibiotics. We also report three X-ray structures of OXA-23: apo OXA-23 at two different pH values, and wild-type OXA-23 in complex with meropenem, a carbapenem substrate. The structures and dynamics simulations reveal an important role for Leu166, whose motion regulates the access of a hydrolytic water molecule to the acyl-enzyme species in imparting carbapenemase activity.
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Journal: - Volume 20, Issue 9, 19 September 2013, Pages 1107–1115