Title : Different Conformations Revealed by NMR Underlie Resistance to Ceftazidime/Avibactam and Susceptibility to Meropenem and Imipenem among D179Y Variants of KPC β-Lactamase.

Pub. Date : 2022 Apr 19

PMID : 35311523






4 Functional Relationships(s)
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1 Using timed mass spectrometry, the D179Y variant formed prolonged acyl-enzyme complexes with imipenem (IMI) and meropenem (MEM) in KPC-2 and KPC-3, which could be detected up to 24 h, suggesting that IMI and MEM act as covalent beta-lactamase inhibitors more than as substrates for D179Y KPC-2 and -3. Imipenem carbapenem-hydrolyzing beta-lactamase KPC-2 Klebsiella pneumoniae
2 Using timed mass spectrometry, the D179Y variant formed prolonged acyl-enzyme complexes with imipenem (IMI) and meropenem (MEM) in KPC-2 and KPC-3, which could be detected up to 24 h, suggesting that IMI and MEM act as covalent beta-lactamase inhibitors more than as substrates for D179Y KPC-2 and -3. Imipenem carbapenem-hydrolyzing beta-lactamase KPC-2 Klebsiella pneumoniae
3 Using timed mass spectrometry, the D179Y variant formed prolonged acyl-enzyme complexes with imipenem (IMI) and meropenem (MEM) in KPC-2 and KPC-3, which could be detected up to 24 h, suggesting that IMI and MEM act as covalent beta-lactamase inhibitors more than as substrates for D179Y KPC-2 and -3. Imipenem carbapenem-hydrolyzing beta-lactamase KPC-2 Klebsiella pneumoniae
4 Using timed mass spectrometry, the D179Y variant formed prolonged acyl-enzyme complexes with imipenem (IMI) and meropenem (MEM) in KPC-2 and KPC-3, which could be detected up to 24 h, suggesting that IMI and MEM act as covalent beta-lactamase inhibitors more than as substrates for D179Y KPC-2 and -3. Imipenem carbapenem-hydrolyzing beta-lactamase KPC-2 Klebsiella pneumoniae