Catalytic role of the metal ion in the metallo-beta-lactamase GOB. - Wikidata - wikimedia - TriplyDB

Catalytic role of the metal ion in the metallo-beta-lactamase GOB.

Catalytic role of the metal ion in the metallo-beta-lactamase GOB.

http://www.wikidata.org/entity/Q39541312

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Carbapenems: past, present, and future Mechanisms of resistance and clinical relevance of resistance to β-lactams, glycopeptides, and fluoroquinolones Structure of Apo- and Monometalated Forms of NDM-1—A Highly Potent Carbapenem-Hydrolyzing Metallo-β-Lactamase 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.Draft Genome Sequence of Strain ATCC 33958, Reported To Be Elizabethkingia miricola.Probing the role of Met221 in the unusual metallo-β-lactamase GOB-18.Crystal Structure of the Metallo-β-Lactamase GOB in the Periplasmic Dizinc Form Reveals an Unusual Metal Site.A variety of roles for versatile zinc in metallo-β-lactamases.A general reaction mechanism for carbapenem hydrolysis by mononuclear and binuclear metallo-β-lactamases.In vivo impact of Met221 substitution in GOB metallo-β-lactamase.Carbapenem resistance in Elizabethkingia meningoseptica is mediated by metallo-β-lactamase BlaB Properties and distribution of a metallo-β-lactamase (ALI-1) from the fish pathogen Aliivibrio salmonicida LFI1238.Label-free measurements of reaction kinetics using a droplet-based optofluidic device.

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P2860

Catalytic role of the metal ion in the metallo-beta-lactamase GOB.

http://www.wikidata.org/entity/Q39541312

description

2009 nî lūn-bûn

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2009年の論文

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2009年論文

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2009年論文

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2009年論文

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2009年論文

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2009年論文

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2009年论文

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2009年论文

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2009年论文

@zh-cn

name

Catalytic role of the metal ion in the metallo-beta-lactamase GOB.

@en

Catalytic role of the metal ion in the metallo-beta-lactamase GOB.

@nl

type

label

Catalytic role of the metal ion in the metallo-beta-lactamase GOB.

@en

Catalytic role of the metal ion in the metallo-beta-lactamase GOB.

@nl

prefLabel

Catalytic role of the metal ion in the metallo-beta-lactamase GOB.

@en

Catalytic role of the metal ion in the metallo-beta-lactamase GOB.

@nl

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JBC.M109.063743

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Journal of Biological Chemistry

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Catalytic role of the metal ion in the metallo-beta-lactamase GOB

@en

P2093

Alejandro J Vila

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P2860

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

Succinic acids as potent inhibitors of plasmid-borne IMP-1 metallo-beta-lactamase

Three-dimensional structure of FEZ-1, a monomeric subclass B3 metallo-beta-lactamase from Fluoribacter gormanii, in native form and in complex with D-captopril

The 1.5-A structure of Chryseobacterium meningosepticum zinc beta-lactamase in complex with the inhibitor, D-captopril

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

Adaptive protein evolution grants organismal fitness by improving catalysis and flexibility

Crystal structure of the wide-spectrum binuclear zinc beta-lactamase from Bacteroides fragilis

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

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4570-4577

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scholarly article

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10.1074/JBC.M109.063743

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7

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285

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Lars Hemmingsen

María-Natalia Lisa

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2009-12-10T00:00:00Z

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20007696

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2836117

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