Details

Autor(en) / Beteiligte

• Haruta, Shin
• Yamamoto, Elise Tie
• Eriguchi, Yoshiro
• Sawai, Tetsuo

Titel

Characterization of the active-site residues asparagine 167 and lysine 161 of the IMP-1 metallo β-lactamase

Ist Teil von

• FEMS microbiology letters, 2001-04, Vol.197 (1), p.85-89

Ort / Verlag

Oxford, UK: Blackwell Publishing Ltd

Erscheinungsjahr

2001

Quelle

Wiley Online Library - AutoHoldings Journals

Beschreibungen/Notizen

• Abstract The roles of lysine at position 161 and asparagine at position 167 in IMP-1 metallo β-lactamase were studied by site-directed mutagenesis. These residues are highly conserved in metallo β-lactamases and are thought to be present in the active-site cavity. Mutant enzymes with alanine or aspartic acid at position 167 showed almost the same properties as the wild-type enzyme. Kinetic parameters for the mutant enzymes differing at position 161 indicated that the positive charge of lysine 161 is required for electrostatic interaction with the carboxyl moiety of the substrate, i.e. C-3 of penicillins or C-4 of cephalosporins.