Role of the Zn1 and Zn2 sites in metallo-beta-lactamase L1 - Wikidata - awgldk - TriplyDB

Role of the Zn1 and Zn2 sites in metallo-beta-lactamase L1

Role of the Zn1 and Zn2 sites in metallo-beta-lactamase L1

http://www.wikidata.org/entity/Q37182382

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Metallo-β-lactamases withstand low Zn(II) conditions by tuning metal-ligand interactions Iron(III) located in the dinuclear metallo-β-lactamase IMP-1 by pseudocontact shifts Use of ferrous iron by metallo-β-lactamases Overcoming differences: The catalytic mechanism of metallo-β-lactamases Spectroscopic and mechanistic studies of heterodimetallic forms of metallo-β-lactamase NDM-1.QM/MM studies of monozinc β-lactamase CphA suggest that the crystal structure of an enzyme-intermediate complex represents a minor pathway.Biapenem inactivation by B2 metallo β-lactamases: energy landscape of the hydrolysis reaction.Biochemical, mechanistic, and spectroscopic characterization of metallo-β-lactamase VIM-2.Differential binding of Co(II) and Zn(II) to metallo-beta-lactamase Bla2 from Bacillus anthracis.Human glyoxalase II contains an Fe(II)Zn(II) center but is active as a mononuclear Zn(II) enzyme Motion of the zinc ions in catalysis by a dizinc metallo-beta-lactamase Probing substrate binding to the metal binding sites in metallo-β-lactamase L1 during catalysis Investigating the position of the hairpin loop in New Delhi metallo-β-lactamase, NDM-1, during catalysis and inhibitor binding Structure and mechanism of copper- and nickel-substituted analogues of metallo-beta-lactamase L1 Catalytic role of the metal ion in the metallo-beta-lactamase GOB.A general reaction mechanism for carbapenem hydrolysis by mononuclear and binuclear metallo-β-lactamases.An unexpected similarity between antibiotic-resistant NDM-1 and beta-lactamase II from Erythrobacter litoralis Properties and distribution of a metallo-β-lactamase (ALI-1) from the fish pathogen Aliivibrio salmonicida LFI1238.Exploring the conformational and reactive dynamics of biomolecules in solution using an extended version of the glycine reactive force field.The Continuing Challenge of Metallo-β-Lactamase Inhibition: Mechanism Matters.Hydrolysis of cephalexin and meropenem by New Delhi metallo-β-lactamase: the substrate protonation mechanism is drug dependent.A DNA nanoribbon as a potent inhibitor of metallo-β-lactamases.

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Role of the Zn1 and Zn2 sites in metallo-beta-lactamase L1

http://www.wikidata.org/entity/Q37182382

description

article científic

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article scientifique

@fr

articolo scientifico

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artigo científico

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bilimsel makale

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scientific article published on 03 October 2008

@en

vedecký článok

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vetenskaplig artikel

@sv

videnskabelig artikel

@da

vědecký článek

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name

Role of the Zn1 and Zn2 sites in metallo-beta-lactamase L1

@en

Role of the Zn1 and Zn2 sites in metallo-beta-lactamase L1.

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type

label

Role of the Zn1 and Zn2 sites in metallo-beta-lactamase L1

@en

Role of the Zn1 and Zn2 sites in metallo-beta-lactamase L1.

@nl

prefLabel

Role of the Zn1 and Zn2 sites in metallo-beta-lactamase L1

@en

Role of the Zn1 and Zn2 sites in metallo-beta-lactamase L1.

@nl

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Journal of the American Chemical Society

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Role of the Zn1 and Zn2 sites in metallo-beta-lactamase L1

@en

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Brian Bennett

http://www.w3.org/2001/XMLSchema#string

Gopalraj Periyannan

http://www.w3.org/2001/XMLSchema#string

Michael W Crowder

http://www.w3.org/2001/XMLSchema#string

Zhenxin Hu

http://www.w3.org/2001/XMLSchema#string

P2860

The 3-D structure of a zinc metallo-beta-lactamase from Bacillus cereus reveals a new type of protein fold

Probing substrate binding to metallo-beta-lactamase L1 from Stenotrophomonas maltophilia by using site-directed mutagenesis

The Zn2 position in metallo-beta-lactamases is critical for activity: a study on chimeric metal sites on a conserved protein scaffold

Structural insights into the design of inhibitors for the L1 metallo-beta-lactamase from Stenotrophomonas maltophilia

Crystal structure of the zinc-dependent beta-lactamase from Bacillus cereus at 1.9 A resolution: binuclear active site with features of a mononuclear enzyme

The crystal structure of the L1 metallo-beta-lactamase from Stenotrophomonas maltophilia at 1.7 A resolution

Femtomolar sensitivity of metalloregulatory proteins controlling zinc homeostasis

Zinc coordination sphere in biochemical zinc sites.

On the mechanism of the metallo-beta-lactamase from Bacteroides fragilis.

Intermediate in beta-lactam hydrolysis catalyzed by a dinuclear zinc(II) complex: relevance to the mechanism of metallo-beta-lactamase.

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14207-14216

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scholarly article

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10.1021/JA8035916

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43

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130

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2008-10-03T00:00:00Z

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23296181

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18831550

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2678235

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