An Ultrahigh Resolution Structure of TEM-1 β-Lactamase Suggests a Role for Glu166 as the General Base in Acylation
Author:
Affiliation:
1. Contribution from the Department of Molecular Pharmacology & Biological Chemistry, Northwestern University, 303 East Chicago Avenue, Chicago, Illinois 60611-3008
Publisher
American Chemical Society (ACS)
Subject
Colloid and Surface Chemistry,Biochemistry,General Chemistry,Catalysis
Link
https://pubs.acs.org/doi/pdf/10.1021/ja0259640
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4. Penicillin resistance: the chemistry of .beta.-lactamase inhibition
5. Site-directed mutagenesis on TEM-1 ß-lactamase: role of Glul66 in catalysis and substrate binding
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