The different inhibition mechanisms of OXA-1 and OXA-24 β-lactamases are determined by the stability of active site carboxylated lysine. - Wikidata - wikimedia - TriplyDB

The different inhibition mechanisms of OXA-1 and OXA-24 β-lactamases are determined by the stability of active site carboxylated lysine.

The different inhibition mechanisms of OXA-1 and OXA-24 β-lactamases are determined by the stability of active site carboxylated lysine.

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Detecting a quasi-stable imine species on the reaction pathway of SHV-1 β-lactamase and 6β-(hydroxymethyl)penicillanic acid sulfone Detection of OXA-48-type carbapenemase-producing Enterobacteriaceae in diagnostic laboratories can be enhanced by addition of bicarbonates to cultivation media or reaction buffers.Rapid Identification of OXA-48 and OXA-163 Subfamilies in Carbapenem-Resistant Gram-Negative Bacilli with a Novel Immunochromatographic Lateral Flow Assay.New techniques in antibiotic discovery and resistance: Raman spectroscopy.Coping with inevitable accidents in metabolism.Activity of the β-Lactamase inhibitor LN-1-255 against carbapenem-hydrolyzing class D β-lactamases from Acinetobacter baumannii.Proteome-wide alterations in an industrial clavulanic acid producing strain of Streptomyces clavuligerus.

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The different inhibition mechanisms of OXA-1 and OXA-24 β-lactamases are determined by the stability of active site carboxylated lysine.

http://www.wikidata.org/entity/Q37608564

description

article científic

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article scientifique

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articolo scientifico

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artigo científico

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bilimsel makale

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scientific article published on 17 January 2014

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vedecký článok

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vetenskaplig artikel

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videnskabelig artikel

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vědecký článek

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name

The different inhibition mecha ...... tive site carboxylated lysine.

@en

The different inhibition mecha ...... tive site carboxylated lysine.

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type

label

The different inhibition mecha ...... tive site carboxylated lysine.

@en

The different inhibition mecha ...... tive site carboxylated lysine.

@nl

prefLabel

The different inhibition mecha ...... tive site carboxylated lysine.

@en

The different inhibition mecha ...... tive site carboxylated lysine.

@nl

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JBC.M113.533562

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Journal of Biological Chemistry

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The different inhibition mecha ...... tive site carboxylated lysine.

@en

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Christopher R Bethel

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Marianne Pusztai-Carey

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Paul R Carey

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Tao Che

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P2860

Three decades of beta-lactamase inhibitors

Critical involvement of a carbamylated lysine in catalytic function of class D -lactamases

Comparison of -lactamases of classes A and D: 1.5-A crystallographic structure of the class D OXA-1 oxacillinase

Crystal structure of the sensor domain of the BlaR penicillin receptor from Bacillus licheniformis

Strategic Design of an Effective -Lactamase Inhibitor: LN-1-255, A 6-ALKYLIDENE-2'-SUBSTITUTED PENICILLIN SULFONE

Critical role of tryptophan 154 for the activity and stability of class D beta-lactamases

Design, Synthesis, and Crystal Structures of 6-Alkylidene-2′-Substituted Penicillanic Acid Sulfones as Potent Inhibitors of Acinetobacter baumannii OXA-24 Carbapenemase

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

Lysine N -Decarboxylation Switch and Activation of the -Lactam Sensor Domain of BlaR1 Protein of Methicillin-resistant Staphylococcus aureus

Structures of SHV-1 β-Lactamase with Penem and Penam Sulfone Inhibitors That Form Cyclic Intermediates Stabilized by Carbonyl Conjugation

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10.1074/JBC.M113.533562

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9

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Robert A Bonomo

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2014-01-17T00:00:00Z

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24443569

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3937681

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