A New Mechanism for β-Lactamases: Class D Enzymes Degrade 1β-Methyl Carbapenems through Lactone Formation

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A New Mechanism for β-Lactamases: Class D Enzymes Degrade 1β-Methyl Carbapenems through Lactone Formation

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im Januar 2018 veröffentlichter wissenschaftlicher Artikel

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wetenschappelijk artikel

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наукова стаття, опублікована в січні 2018

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A New Mechanism for β-Lactamas ...... nems through Lactone Formation

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A New Mechanism for β-Lactamas ...... nems through Lactone Formation

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A New Mechanism for β-Lactamas ...... nems through Lactone Formation

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A New Mechanism for β-Lactamas ...... nems through Lactone Formation

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A New Mechanism for β-Lactamas ...... nems through Lactone Formation

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A New Mechanism for β-Lactamas ...... nems through Lactone Formation

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P1476

A New Mechanism for β-Lactamas ...... nems through Lactone Formation

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P2093

Catherine L. Tooke

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Christopher J. Schofield

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Christopher T. Lohans

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Emma van Groesen

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James Spencer

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Jürgen Brem

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Robert S. Paton

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P2860

"Stormy waters ahead": global emergence of carbapenemases

Carbapenemases: the versatile beta-lactamases

The 1.4 Å Crystal Structure of the Class D β-Lactamase OXA-1 Complexed with Doripenem

Structures of the Class D Carbapenemase OXA-24 from Acinetobacter baumannii in Complex with Doripenem

Structural Basis for Carbapenemase Activity of the OXA-23 β-Lactamase from Acinetobacter baumannii

The basis for carbapenem hydrolysis by class A β-lactamases: a combined investigation using crystallography and simulations

The structure of a doripenem-bound OXA-51 class D β-lactamase variant with enhanced carbapenemase activity

Structural basis for carbapenem-hydrolyzing mechanisms of carbapenemases conferring antibiotic resistance

Geometrical reaction coordinates. II. Nucleophilic addition to a carbonyl group

Avibactam is a covalent, reversible, non-β-lactam β-lactamase inhibitor

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1296-1299

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scholarly article

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10.1002/ANGE.201711308

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P433

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P478

130

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Kiran Kumar

P577

2018-01-05T00:00:00Z

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