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

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Properties of mutant SHV-5 beta-lactamases constructed by substitution of isoleucine or valine for methionine at position 69.

The effect of replacement of Met-69 by Ile or Val on the properties of the extended-spectrum beta-lactamase SHV-5 was studied. Mutant enzymes were constructed by site-specific mutagenesis and expressed under isogenic conditions in Escherichia coli DH5alpha cells. Compared with SHV-5, the mutant beta-lactamases conferred lower levels of beta-lactam resistance and were less efficient in hydrolyzing ampicillin, cephalothin, and cefotaxime. The substitutions rendered SHV-5 less susceptible to inhibition by clavulanate, sulbactam, and tazobactam; however, the MICs of penicillin-inhibitor combinations remained similar, suggesting an attenuation of penicillinase activity.[1]

References

  1. Properties of mutant SHV-5 beta-lactamases constructed by substitution of isoleucine or valine for methionine at position 69. Giakkoupi, P., Miriagou, V., Gazouli, M., Tzelepi, E., Legakis, N.J., Tzouvelekis, L.S. Antimicrob. Agents Chemother. (1998) [Pubmed]
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