Clavulanic acid inactivation of SHV-1 and the inhibitor-resistant S130G SHV-1 beta-lactamase. Insights into the mechanism of inhibition. - Wikidata - wikimedia - TriplyDB

Clavulanic acid inactivation of SHV-1 and the inhibitor-resistant S130G SHV-1 beta-lactamase. Insights into the mechanism of inhibition.

Clavulanic acid inactivation of SHV-1 and the inhibitor-resistant S130G SHV-1 beta-lactamase. Insights into the mechanism of inhibition.

http://www.wikidata.org/entity/Q33218209

about

Three decades of beta-lactamase inhibitors Asp-120 locates Zn2 for optimal metallo-beta-lactamase activity Strategic Design of an Effective -Lactamase Inhibitor: LN-1-255, A 6-ALKYLIDENE-2'-SUBSTITUTED PENICILLIN SULFONE Design, Synthesis, and Crystal Structures of 6-Alkylidene-2′-Substituted Penicillanic Acid Sulfones as Potent Inhibitors of Acinetobacter baumannii OXA-24 Carbapenemase Design and Exploration of Novel Boronic Acid Inhibitors Reveals Important Interactions with a Clavulanic Acid-Resistant Sulfhydryl-Variable (SHV) β-Lactamase The Importance of thetrans-Enamine Intermediate as a β-Lactamase Inhibition Strategy Probed in Inhibitor-Resistant SHV β-Lactamase Variants β-Lactamase Inhibition by 7-Alkylidenecephalosporin Sulfones: Allylic Transposition and Formation of an Unprecedented Stabilized Acyl-Enzyme Insight into the effect of inhibitor resistant S130G mutant on physico-chemical properties of SHV type beta-lactamase: a molecular dynamics study Trapping and characterization of a reaction intermediate in carbapenem hydrolysis by B. cereus metallo-beta-lactamase.Why the extended-spectrum beta-lactamases SHV-2 and SHV-5 are "hypersusceptible" to mechanism-based inhibitors Inhibition of OXA-1 beta-lactamase by penems.Different intermediate populations formed by tazobactam, sulbactam, and clavulanate reacting with SHV-1 beta-lactamases: Raman crystallographic evidence Enhancing resistance to cephalosporins in class C beta-lactamases: impact of Gly214Glu in CMY-2.The role of a second-shell residue in modifying substrate and inhibitor interactions in the SHV beta-lactamase: a study of ambler position Asn276.Penicillin sulfone inhibitors of class D beta-lactamases Exploring the inhibition of CTX-M-9 by beta-lactamase inhibitors and carbapenems.Identification of products of inhibition of GES-2 beta-lactamase by tazobactam by x-ray crystallography and spectrometry.Avibactam and inhibitor-resistant SHV β-lactamases The Lys234Arg substitution in the enzyme SHV-72 is a determinant for resistance to clavulanic acid inhibition.Engineered mononuclear variants in Bacillus cereus metallo-beta-lactamase BcII are inactive.Molecular and biochemical characterization of SHV-56, a novel inhibitor-resistant beta-lactamase from Klebsiella pneumoniae.Common mechanistic features among metallo-beta-lactamases: a computational study of Aeromonas hydrophila CphA enzyme.The different inhibition mechanisms of OXA-1 and OXA-24 β-lactamases are determined by the stability of active site carboxylated lysine.The role of IgE recognition in allergic reactions to amoxicillin and clavulanic acid.Structural/mechanistic insights into the efficacy of non-classical β-lactamase inhibitors against extensively drug resistant Stenotrophomonas maltophilia clinical isolates.Homology modeling and virtual screening of inhibitors against TEM- and SHV-type-resistant mutants: A multilayer filtering approach.Rational design of a beta-lactamase inhibitor achieved via stabilization of the trans-enamine intermediate: 1.28 A crystal structure of wt SHV-1 complex with a penam sulfone Irreversible inhibition of the Mycobacterium tuberculosis beta-lactamase by clavulanate.Following drug uptake and reactions inside Escherichia coli cells by Raman microspectroscopy.Importance of position 170 in the inhibition of GES-type β-lactamases by clavulanic acid.Probing active site chemistry in SHV beta-lactamase variants at Ambler position 244. Understanding unique properties of inhibitor resistance.High resolution crystal structures of the trans-enamine intermediates formed by sulbactam and clavulanic acid and E166A SHV-1 {beta}-lactamase.A fluorescein-labeled AmpC β-lactamase allows rapid characterization of β-lactamase inhibitors by real-time fluorescence monitoring of the β-lactamase-inhibitor interactions.

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Clavulanic acid inactivation of SHV-1 and the inhibitor-resistant S130G SHV-1 beta-lactamase. Insights into the mechanism of inhibition.

http://www.wikidata.org/entity/Q33218209

description

2005 nî lūn-bûn

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2005 թուականի Յունիսին հրատարակուած գիտական յօդուած

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2005 թվականի հունիսին հրատարակված գիտական հոդված

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2005年の論文

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Clavulanic acid inactivation o ...... o the mechanism of inhibition.

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Clavulanic acid inactivation o ...... o the mechanism of inhibition.

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Journal of Biological Chemistry

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Clavulanic acid inactivation o ...... o the mechanism of inhibition.

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P2093

Christopher R Bethel

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Deley Sulton

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Doritza Pagan-Rodriguez

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Jodi M Thomson

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John D Buynak

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Lily M Ng

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Marion S Helfand

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Vernon E Anderson

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Xiang Zhou

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Yiding Liu

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P2860

X-ray structure of the Asn276Asp variant of the Escherichia coli TEM-1 beta-lactamase: direct observation of electrostatic modulation in resistance to inactivation by clavulanic acid

Inhibition of the SHV-1 beta-lactamase by sulfones: crystallographic observation of two reaction intermediates with tazobactam

The structural bases of antibiotic resistance in the clinically derived mutant beta-lactamases TEM-30, TEM-32, and TEM-34

Inhibition of class A and class C beta-lactamases by penems: crystallographic structures of a novel 1,4-thiazepine intermediate

Tazobactam forms a stoichiometric trans-enamine intermediate in the E166A variant of SHV-1 beta-lactamase: 1.63 A crystal structure

Tazobactam inactivation of SHV-1 and the inhibitor-resistant Ser130 -->Gly SHV-1 beta-lactamase: insights into the mechanism of inhibition.

Following the reactions of mechanism-based inhibitors with beta-lactamase by Raman crystallography.

Beta-lactamases: a survey of protein diversity.

Extended-spectrum and inhibitor-resistant TEM-type beta-lactamases: mutations, specificity, and three-dimensional structure.

Molecular dynamics at the root of expansion of function in the M69L inhibitor-resistant TEM beta-lactamase from Escherichia coli.

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35528-35536

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10.1074/JBC.M501251200

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42

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280

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Robert A Bonomo

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2005-06-29T00:00:00Z

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15987690

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