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Role of the Ser-287-Asn replacement in the hydrolysis spectrum extension of AmpC beta-lactamases in Escherichia coli.
- Source :
-
Antimicrobial agents and chemotherapy [Antimicrob Agents Chemother] 2009 Jan; Vol. 53 (1), pp. 323-6. Date of Electronic Publication: 2008 Nov 10. - Publication Year :
- 2009
-
Abstract
- Two AmpC variants harboring the S287N substitution were obtained by mutagenesis from cephalosporinases representative of the phylogenetic groups A and B2 of Escherichia coli. Their biochemical characterization revealed that the S287N replacement led to an important increase in the catalytic efficiency toward extended-spectrum cephalosporins in the AmpC beta-lactamase of group A only.
- Subjects :
- Asparagine genetics
Bacterial Proteins chemistry
Bacterial Proteins genetics
Bacterial Proteins metabolism
Cephalosporins pharmacology
Escherichia coli drug effects
Escherichia coli Proteins chemistry
Escherichia coli Proteins genetics
Escherichia coli Proteins metabolism
Escherichia coli Proteins physiology
Hydrolysis
Microbial Sensitivity Tests
Models, Molecular
Mutagenesis, Site-Directed
Protein Structure, Secondary
Serine genetics
beta-Lactamases chemistry
beta-Lactamases genetics
beta-Lactamases metabolism
Asparagine physiology
Bacterial Proteins physiology
Escherichia coli enzymology
Escherichia coli genetics
Serine physiology
beta-Lactamases physiology
Subjects
Details
- Language :
- English
- ISSN :
- 1098-6596
- Volume :
- 53
- Issue :
- 1
- Database :
- MEDLINE
- Journal :
- Antimicrobial agents and chemotherapy
- Publication Type :
- Academic Journal
- Accession number :
- 19001118
- Full Text :
- https://doi.org/10.1128/AAC.00608-08