Selection and Characterization of Amino Acid Substitutions at Residues 237-240 of TEM-1 β-Lactamase with Altered Substrate Specificity for Aztreonam and Ceftazidime-Reference-Cited by-同舟云学术

Selection and Characterization of Amino Acid Substitutions at Residues 237-240 of TEM-1 β-Lactamase with Altered Substrate Specificity for Aztreonam and Ceftazidime

Published:1996-09 Issue:37 Volume:271 Page:22538-22545
ISSN:0021-9258
Container-title:Journal of Biological Chemistry
language:en
Short-container-title:Journal of Biological Chemistry

Author:

Cantu Carlos,Huang Wanzhi,Palzkill Timothy

Publisher

Elsevier BV

Subject

Cell Biology,Molecular Biology,Biochemistry

Reference31 articles.

1. Transferable resistance to cefotaxime, cefoxitin, cefamandole and cefuroxime in clinical isolates of Klebsiella pneumoniae and Serratia marcescens

2. TEM- and SHV-derived extended-spectrum β-lactamases: relationship between selection, structure and function

3. Role of Ser-238 and Lys-240 in the hydrolysis of third-generation cephalosporins by SHV-type beta-lactamases probed by site-directed mutagenesis and three-dimensional modeling.

4. TEM β-Lactamase Mutants Hydrolysing Third-generation Cephalosporins

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

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