Substitution of lysine at position 104 or 240 of TEM-1 sub(pTZ18R) beta -lactamase enhances the effect of serine-164 substitution on hydrolysis or affinity for cephalosporins and the monobactam aztreonam

By site-directed mutagenesis, TEM-1 beta -lactamase was altered to contain single amino acid changes of E104K, R164S, and E240K, in addition to double changes of E104K/R164S or R164S/E240K and the triple changes of E104K/R164S/E240K. Hydrolysis rates for cephaloridine and benzylpenicillin were lower...

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Published inBiochemistry (Easton) Vol. 30; no. 13; pp. 3179 - 3188
Main Authors Sowek, JA, Singer, S B, Ohringer, S, Malley, M F, Dougherty, T J, Gougoutas, J Z, Bush, K
Format Journal Article
LanguageEnglish
Published 01.01.1991
Subjects
lysine
serine
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Summary:By site-directed mutagenesis, TEM-1 beta -lactamase was altered to contain single amino acid changes of E104K, R164S, and E240K, in addition to double changes of E104K/R164S or R164S/E240K and the triple changes of E104K/R164S/E240K. Hydrolysis rates for cephaloridine and benzylpenicillin were lowered at least 1 order of magnitude for all enzymes containing R164S substitutions.
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ISSN:0006-2960