Rational Design of a β-Lactamase Inhibitor Achieved via Stabilization of the trans-Enamine Intermediate: 1.28 Å Crystal Structure of wt SHV-1 Complex with a Penam Sulfone-Reference-Cited by-同舟云学术

Rational Design of a β-Lactamase Inhibitor Achieved via Stabilization of the trans-Enamine Intermediate: 1.28 Å Crystal Structure of wt SHV-1 Complex with a Penam Sulfone

Published:2006-09-20 Issue:40 Volume:128 Page:13235-13242
ISSN:0002-7863
Container-title:Journal of the American Chemical Society
language:en
Short-container-title:J. Am. Chem. Soc.

Author:

Padayatti Pius S.¹,Sheri Anjaneyulu¹,Totir Monica A.¹,Helfand Marion S.¹,Carey Marianne P.¹,Anderson Vernon E.¹,Carey Paul R.¹,Bethel Christopher R.¹,Bonomo Robert A.¹,Buynak John D.¹,van den Akker Focco¹

Affiliation:

1. Contribution from the Departments of Biochemistry, Chemistry, and Pharmacology, Case Western Reserve University, Cleveland, Ohio 44106, Department of Chemistry, Southern Methodist University, Dallas, Texas 75275-0314, and Research Division, Louis Stokes Cleveland Veterans Affairs Medical Center, Cleveland, Ohio 44106

Publisher

American Chemical Society (ACS)

Subject

Colloid and Surface Chemistry,Biochemistry,General Chemistry,Catalysis

Link

https://pubs.acs.org/doi/pdf/10.1021/ja063715w

Reference47 articles.

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3. Understanding the longevity of the β-lactam antibiotics and of antibiotic/β-lactamase inhibitor combinations

4. Molecular basis of antibiotic resistance and β-lactamase inhibition by mechanism-based inactivators: perspectives and future directions

5. β-Lactamase inhibitors: evolving compounds for evolving resistance targets

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