Hydrolytic mechanism of OXA-58 enzyme, a carbapenem-hydrolyzing class D β-lactamase from Acinetobacter baumannii.
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Crystal Structure of OXA-58 with the Substrate-Binding Cleft in a Closed State: Insights into the Mobility and Stability of the OXA-58 StructureCrystal Structure of Carbapenemase OXA-58 from Acinetobacter baumanniiStructural basis for carbapenem-hydrolyzing mechanisms of carbapenemases conferring antibiotic resistanceClass D β-lactamases: a reappraisal after five decadesDetection of OXA-48-type carbapenemase-producing Enterobacteriaceae in diagnostic laboratories can be enhanced by addition of bicarbonates to cultivation media or reaction buffers.Class D β-lactamases do exist in Gram-positive bacteria.Bacterial cell-wall recycling.OXA β-lactamases.Acquired Class D β-Lactamases.β-Lactamases: A Focus on Current Challenges.Class D β-lactamases: are they all carbapenemases?Activity of the β-Lactamase inhibitor LN-1-255 against carbapenem-hydrolyzing class D β-lactamases from Acinetobacter baumannii.Active-Site Plasticity Is Essential to Carbapenem Hydrolysis by OXA-58 Class D β-Lactamase of Acinetobacter baumannii.13C-Carbamylation as a mechanistic probe for the inhibition of class D β-lactamases by avibactam and halide ions.
P2860
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P2860
Hydrolytic mechanism of OXA-58 enzyme, a carbapenem-hydrolyzing class D β-lactamase from Acinetobacter baumannii.
description
2011 nî lūn-bûn
@nan
2011年の論文
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2011年論文
@yue
2011年論文
@zh-hant
2011年論文
@zh-hk
2011年論文
@zh-mo
2011年論文
@zh-tw
2011年论文
@wuu
2011年论文
@zh
2011年论文
@zh-cn
name
Hydrolytic mechanism of OXA-58 ...... from Acinetobacter baumannii.
@en
type
label
Hydrolytic mechanism of OXA-58 ...... from Acinetobacter baumannii.
@en
prefLabel
Hydrolytic mechanism of OXA-58 ...... from Acinetobacter baumannii.
@en
P2093
P2860
P356
P1476
Hydrolytic mechanism of OXA-58 ...... from Acinetobacter baumannii.
@en
P2093
Dasantila Golemi-Kotra
Jerome Liu
Kaveh Amini
Lakshmi P Kotra
Naresh Balachandran
Sebastian A Testero
Siobhan Stynes
Tharseekan Monoharan
Vidhu Verma
William Wei
P2860
P304
37292-37303
P356
10.1074/JBC.M111.280115
P407
P577
2011-08-31T00:00:00Z