Properties of Mutant SHV-5 β-Lactamases Constructed by Substitution of Isoleucine or Valine for Methionine at Position 69 | Zendy

Panagiota Giakkoupi | Zendy; Vivì Miriagou | Zendy; Maria Gazouli | Zendy; Εva Tzelepi | Zendy; N.J. Legakis | Zendy; L. S. Tzouvelekis | Zendy

Open Access

Properties of Mutant SHV-5 β-Lactamases Constructed by Substitution of Isoleucine or Valine for Methionine at Position 69

Author(s) -

Panagiota Giakkoupi,

Vivì Miriagou,

Maria Gazouli,

Εva Tzelepi,

N.J. Legakis,

L. S. Tzouvelekis

Publication year - 1998

Publication title -

antimicrobial agents and chemotherapy

Language(s) - English

Resource type - Journals

SCImago Journal Rank - 2.07

H-Index - 259

eISSN - 1070-6283

pISSN - 0066-4804

DOI - 10.1128/aac.42.5.1281

Subject(s) - sulbactam , mutant , cefotaxime , isoleucine , escherichia coli , valine , penicillin , biology , tazobactam , amp resistance , microbiology and biotechnology , methionine , mutagenesis , chemistry , ampicillin , biochemistry , antibiotics , amino acid , antibiotic resistance , leucine , gene , imipenem

The effect of replacement of Met-69 by Ile or Val on the properties of the extended-spectrum β-lactamase SHV-5 was studied. Mutant enzymes were constructed by site-specific mutagenesis and expressed under isogenic conditions inEscherichia coli DH5α cells. Compared with SHV-5, the mutant β-lactamases conferred lower levels of β-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.

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