
NMR Backbone Assignment of VIM-2 and Identification of the …
Jan 28, 2022 · Verona-integron encoded metallo-β-lactamase 2 (VIM-2) is a bacterial enzyme that has been reported from multidrug-resistant nosocomial isolates of Pseudomonas aeruginosa and other Gram-negative pathogens. As it hydrolyzes most β-lactams efficiently, including carbapenems, it is a major threat to current antimicrobial chemotherapies.
Characterization of VIM-2, a Carbapenem-Hydrolyzing Metallo-β …
VIM-2 is the second carbapenem-hydrolyzing metalloenzyme characterized from a P. aeruginosa isolate outside Japan. Among the class B metalloenzymes, two carbapenem-hydrolyzing β-lactamases have been genetically characterized in Pseudomonas aeruginosa: IMP-1 …
VIM-2–producing Multidrug-Resistant Pseudomonas aeruginosa …
Carbapenem resistance among Pseudomonas aeruginosa strains from India: evidence for nationwide endemicity of multiple metallo-beta-lactamase clones (VIM-2, −5, −6, and −11 and the newly characterized VIM-18).
Exploiting the fitness cost of metallo-β-lactamase expression can ...
Jan 2, 2025 · Using a systemic murine infection model, we showed azithromycin’s therapeutic potential against VIM-2-expressing pathogens. In all, our findings provide a framework to exploit the fitness...
RCSB PDB - 1KO3: VIM-2, a Zn-beta-lactamase from …
Dec 20, 2001 · The crystal structures of the universally widespread metallo-beta-lactamase (MBL) Verona integron-encoded MBL (VIM)-2 from Pseudomonas aeruginosa have been solved in their native form as well as in an unexpected oxidised form.
The Three-Dimensional Structure of VIM-2, a Zn-β-Lactamase …
Jan 18, 2008 · VIM-2 enzyme is a monomer with a molecular mass of 25,515 Da and with 240 residues in its mature form. Purified VIM-2 has a broad substrate hydrolysis range, which includes penicillins, cephalosporins, cephamycins, oxacephamycins and carbapenems but not monobactams. Amongst the carbapenems, VIM-2 better …
Inhibitors of VIM-2 by screening pharmacologically active and …
Jul 15, 2009 · VIM-2 is an Ambler class B metallo-β-lactamase (MBL) capable of hydrolyzing a broad-spectrum of β-lactam antibiotics. Although the discovery and development of MBL inhibitors continue to be an area of active research, an array of potent, small molecule inhibitors is yet to be fully characterized for VIM-2.
VIM-2型金属β内酰胺酶的序列分析、原核表达及纯化
Oct 16, 2006 · 摘要:目的 对铜绿假单胞菌所产blaVIM-2进行基因重组表达及纯化.方法 以产blaVIM-2铜绿假单胞菌总基因组DNA为模板,PCR扩增blaVIM-2,将其克隆入pUCm-T载体后测定该核苷酸序列,再将blaVIM-2克隆入表达载体pET-41b (+),然后在大肠埃希菌BL21 (DE3)中表达,表达产物再过Ni-NTA柱纯化 ...
The structure of the metallo-β-lactamase VIM-2 in complex
Nov 1, 2016 · Verona integron-encoded metallo-β-lactamase 2 (VIM-2) is a widespread MBL with a broad substrate spectrum and hence is an interesting drug target for the treatment of β-lactam-resistant infections. In this study, three triazolylthioacetamides were tested as inhibitors of VIM-2.
Comprehensive exploration of the translocation, stability and
Jun 8, 2020 · We generate a series of comprehensive and high-quality datasets, and develop a global understanding of VIM-2 by identifying residues that are critical for its function, stability and/or substrate specificity. We also examine VIM-2’s signal peptide—an often overlooked feature despite its importance in expression and transport.
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