Site-directed mutagenesis at the active site of Escherichia coli TEM-1 beta-lactamase. Suicide inhibitor-resistant mutants reveal the role of arginine 244 and methionine 69 in catalysis.-Reference-Cited by-同舟云学术

Site-directed mutagenesis at the active site of Escherichia coli TEM-1 beta-lactamase. Suicide inhibitor-resistant mutants reveal the role of arginine 244 and methionine 69 in catalysis.

Published:1992-10 Issue:29 Volume:267 Page:20600-20606
ISSN:0021-9258
Container-title:Journal of Biological Chemistry
language:en
Short-container-title:Journal of Biological Chemistry

Author:

Delaire M,Labia R,Samama J.P.,Masson J.M.

Publisher

Elsevier BV

Subject

Cell Biology,Molecular Biology,Biochemistry

Reference34 articles.

1. Molecular evolution of ubiquitous ?-lactamases towards extended-spectrum enzymes active against newer ?-lactam antibiotics

2. Belaaouai, A., Lapoumeroulie, C., Vedel, G., Nevot, P., Krishnamoorthy, R., and Paul, G. (1991) 31st Interscience Conference on Antimicrobiol Agents and Chemotherapy, p. 256, Abstr. 944

3. The structure of β-lactamases

4. The active-site-serine penicillin-recognizing enzymes as members of the Streptomyces R61 dd-peptidase family

5. β-lactamase TEM1 ofE. coliCrystal structure determination at 2.5 Å resolution

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