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Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)
 
 
 
 
 

Characterisation of a unique ceftazidime-hydrolysing beta-lactamase, TEM-E2.

A strain of Klebsiella oxytoca, originally isolated in Liverpool in 1982, has been found to produce a novel transferable beta-lactamase, TEM-E2. This enzyme confers resistance to ceftazidime and focused as a doublet band with an iso-electric point (pI) of 5. 3. The strain also produced the TEM-1 beta-lactamase. Both TEM-1 and TEM-E2 beta-lactamases were encoded by a transferable 103 kb plasmid; these two enzymes also had similar molecular weights, were inhibited by clavulanic acid, and hydrolysed ampicillin, carbenicillin and cephaloridine at similar rates. However, unlike the TEM-1 enzyme, the TEM-E2 beta-lactamase hydrolysed ceftazidime and cefotaxime with similar efficiency, although it conferred much greater resistance to ceftazidime in the host strain. This is the earliest documented example of a TEM-like enzyme which confers transferable resistance to ceftazidime and related cephalosporins.[1]

References

  1. Characterisation of a unique ceftazidime-hydrolysing beta-lactamase, TEM-E2. Payne, D.J., Marriott, M.S., Amyes, S.G. J. Med. Microbiol. (1990) [Pubmed]
 
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