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Substitution of Asp for Asn at position 132 in the active site of TEM beta-lactamase. Activity toward different substrates and effects of neighboring residues

The Journal of Biological Chemistry

Jan 13, 1995

Joel OsunaXavier Soberón

PMID: 7822310

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Abstract

Using a random, combinatorial scheme of mutagenesis directed against the conserved SDN region of TEM beta-lactamase, and selective screening in ampicillin-plates, we obtained the N132D mutant enzyme. The kinetic characterization of this mutant indicated relatively small effects compared...read more

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  • Substitution of Asp for Asn at position 132 in the active site of TEM beta-lactamase. Activity toward different substrates and effects of neighboring residues

    The Journal of Biological Chemistry

    Jan 13, 1995

    Joel OsunaXavier Soberón

    PMID: 7822310

    DOI:

    Abstract

    Using a random, combinatorial scheme of mutagenesis directed against the conserved SDN region of TEM beta-lactamase, and selective screening in ampicillin-plates, we obtained the N132D mutant enzyme. The kinetic characterization of this mutant indicated relatively small effects compared...read more

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