The Deacylation Mechanism of AmpC β-Lactamase at Ultrahigh Resolution-Reference-Cited by-同舟云学术

The Deacylation Mechanism of AmpC β-Lactamase at Ultrahigh Resolution

Published:2006-02-09 Issue:9 Volume:128 Page:2970-2976
ISSN:0002-7863
Container-title:Journal of the American Chemical Society
language:en
Short-container-title:J. Am. Chem. Soc.

Author:

Chen Yu¹,Minasov George¹,Roth Tomer A.¹,Prati Fabio¹,Shoichet Brian K.¹

Affiliation:

1. Contribution from the Department of Pharmaceutical Chemistry, University of California San Francisco, QB3 Building Room 508D, 1700 4th Street, San Francisco, California 94143-2550, Department of Molecular Pharmacology & Biological Chemistry, Northwestern University, 303 East Chicago Avenue, Chicago, Illinois 60611-3008, and Dipartimento di Chimica, Universitá degli studi di Modena e Reggio Emilia, via Campi 183, Modena, Italy

Publisher

American Chemical Society (ACS)

Subject

Colloid and Surface Chemistry,Biochemistry,General Chemistry,Catalysis

Link

https://pubs.acs.org/doi/pdf/10.1021/ja056806m

Reference40 articles.

1. Bacterial Resistance to β-Lactam Antibiotics: Compelling Opportunism, Compelling Opportunity

2. Inactivation of Antibiotics and the Dissemination of Resistance Genes

3. A functional classification scheme for beta-lactamases and its correlation with molecular structure

4. Evolution of an enzyme activity: crystallographic structure at 2-A resolution of cephalosporinase from the ampC gene of Enterobacter cloacae P99 and comparison with a class A penicillinase

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