The metallo-beta-lactamase GOB is a mono-Zn(II) enzyme with a novel active site. - Wikidata - wikimedia - TriplyDB

The metallo-beta-lactamase GOB is a mono-Zn(II) enzyme with a novel active site.

The metallo-beta-lactamase GOB is a mono-Zn(II) enzyme with a novel active site.

http://www.wikidata.org/entity/Q48080395

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Adaptive protein evolution grants organismal fitness by improving catalysis and flexibility The Structure of the Dizinc Subclass B2 Metallo- -Lactamase CphA Reveals that the Second Inhibitory Zinc Ion Binds in the Histidine Site Mutagenesis of Zinc Ligand Residue Cys221 Reveals Plasticity in the IMP-1 Metallo- -Lactamase Active Site Structure of Apo- and Monometalated Forms of NDM-1—A Highly Potent Carbapenem-Hydrolyzing Metallo-β-Lactamase Use of ferrous iron by metallo-β-lactamases Overcoming differences: The catalytic mechanism of metallo-β-lactamases Trapping and characterization of a reaction intermediate in carbapenem hydrolysis by B. cereus metallo-beta-lactamase.Insights from the genome annotation of Elizabethkingia anophelis from the malaria vector Anopheles gambiae.Biapenem inactivation by B2 metallo β-lactamases: energy landscape of the hydrolysis reaction.Whole-genome sequence of Chryseobacterium oranimense, a colistin-resistant bacterium isolated from a cystic fibrosis patient in France.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.Spectroscopic studies on Arabidopsis ETHE1, a glyoxalase II-like protein.Engineered mononuclear variants in Bacillus cereus metallo-beta-lactamase BcII are inactive.Cross-class metallo-β-lactamase inhibition by bisthiazolidines reveals multiple binding modes.Role of the Zn1 and Zn2 sites in metallo-beta-lactamase L1 Secretion of GOB metallo-beta-lactamase in Escherichia coli depends strictly on the cooperation between the cytoplasmic DnaK chaperone system and the Sec machinery: completion of folding and Zn(II) ion acquisition occur in the bacterial periplasm.Crystal Structure of the Metallo-β-Lactamase GOB in the Periplasmic Dizinc Form Reveals an Unusual Metal Site.Metal content of metallo-beta-lactamase L1 is determined by the bioavailability of metal ions.Common mechanistic features among metallo-beta-lactamases: a computational study of Aeromonas hydrophila CphA enzyme.A variety of roles for versatile zinc in metallo-β-lactamases.Antibiotic resistance in Zn(II)-deficient environments: metallo-β-lactamase activation in the periplasm.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.Crystal structure and kinetic analysis of the class B3 di-zinc metallo-β-lactamase LRA-12 from an Alaskan soil metagenome.In vivo impact of Met221 substitution in GOB metallo-β-lactamase.Low-molecular-mass penicillin binding protein 6b (DacD) is required for efficient GOB-18 metallo-β-lactamase biogenesis in Salmonella enterica and Escherichia coli.Carbapenem resistance in Elizabethkingia meningoseptica is mediated by metallo-β-lactamase BlaB A convenient microbiological assay employing cell-free extracts for the rapid characterization of Gram-negative carbapenemase producers.Identification and characterization of an unusual metallo-β-lactamase from Serratia proteamaculans.On the active site of mononuclear B1 metallo β-lactamases: a computational study

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The metallo-beta-lactamase GOB is a mono-Zn(II) enzyme with a novel active site.

http://www.wikidata.org/entity/Q48080395

description

2007 nî lūn-bûn

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2007年の論文

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2007年学术文章

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2007年学术文章

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2007年学术文章

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2007年学术文章

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2007年学术文章

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2007年学术文章

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2007年學術文章

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name

The metallo-beta-lactamase GOB is a mono-Zn

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The metallo-beta-lactamase GOB is a mono-Zn(II) enzyme with a novel active site.

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type

label

The metallo-beta-lactamase GOB is a mono-Zn

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The metallo-beta-lactamase GOB is a mono-Zn(II) enzyme with a novel active site.

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prefLabel

The metallo-beta-lactamase GOB is a mono-Zn

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The metallo-beta-lactamase GOB is a mono-Zn(II) enzyme with a novel active site.

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Journal of Biological Chemistry

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The metallo-beta-lactamase GOB is a mono-Zn(II) enzyme with a novel active site

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Adriana S Limansky

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Alejandro J Vila

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Alejandro M Viale

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Alison L Costello

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Brian Bennett

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David L Tierney

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Jorgelina Morán-Barrio

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Matteo Dal Peraro

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P2860

Cleavage of structural proteins during the assembly of the head of bacteriophage T4

Real-space multiple-scattering calculation and interpretation of x-ray-absorption near-edge structure

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

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

Calculation of protein extinction coefficients from amino acid sequence data

Quick measurement of protein sulfhydryls with Ellman's reagent and with 4,4'-dithiodipyridine

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25

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282

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María-Natalia Lisa

Javier M González

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2007-04-02T00:00:00Z

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