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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

J OsunaX Soberón

PMID: 7822310

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

Mentioned in this Paper

Asparagine
Aspartic Acid, Magnesium-Potassium (2:1:2) Salt
Beta-Lactamase
Oligonucleotide Primers
Catalysis
Hydrogen-Ion Concentration
Mutagenesis Process
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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

J OsunaX 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

Mentioned in this Paper

Asparagine
Aspartic Acid, Magnesium-Potassium (2:1:2) Salt
Beta-Lactamase
Oligonucleotide Primers
Catalysis
Hydrogen-Ion Concentration
Mutagenesis Process

Similar Papers Found In These Feeds

ASBMB Publications

The American Society for Biochemistry and Molecular Biology (ASBMB) includes the Journal of Biological Chemistry, Molecular & Cellular Proteomics, and the Journal of Lipid Research. Discover the latest research from ASBMB here.

Related Papers

Paper Details
References
  • References
  • Citations10
  • finger pointing at paper

    References currently unavailable

    We're still populating references for this paper, please check back later.
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  • Citations10
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