Substrate-activated zinc binding of metallo-beta -lactamases: physiological importance of mononuclear enzymes. - Wikidata - awgldk - TriplyDB

Substrate-activated zinc binding of metallo-beta -lactamases: physiological importance of mononuclear enzymes.

Substrate-activated zinc binding of metallo-beta -lactamases: physiological importance of mononuclear enzymes.

http://www.wikidata.org/entity/Q43967747

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Crystal structures of a purple acid phosphatase, representing different steps of this enzyme's catalytic cycle The 1.5-A structure of Chryseobacterium meningosepticum zinc beta-lactamase in complex with the inhibitor, D-captopril The Structure of the Dizinc Subclass B2 Metallo- -Lactamase CphA Reveals that the Second Inhibitory Zinc Ion Binds in the Histidine Site The Role of Zn 2+ on the Structure and Stability of Murine Adenosine Deaminase †Glycolytic and Non-glycolytic Functions of Mycobacterium tuberculosis Fructose-1,6-bisphosphate Aldolase, an Essential Enzyme Produced by Replicating and Non-replicating Bacilli Metallo-β-lactamases withstand low Zn(II) conditions by tuning metal-ligand interactions Trapping and characterization of a reaction intermediate in carbapenem hydrolysis by B. cereus metallo-beta-lactamase.Zinc ion-induced domain organization in metallo-beta-lactamases: a flexible "zinc arm" for rapid metal ion transfer?Grafting a new metal ligand in the cocatalytic site of B. cereus metallo-beta-lactamase: structural flexibility without loss of activity.X-ray absorption spectroscopy of metal site speciation in the metallo-β-lactamase BcII from Bacillus cereus.Membrane anchoring stabilizes and favors secretion of New Delhi metallo-β-lactamase Role of the Zn1 and Zn2 sites in metallo-beta-lactamase L1 Metal content of metallo-beta-lactamase L1 is determined by the bioavailability of metal ions.Metallo-β-lactamase structure and function.The mechanisms of catalysis by metallo beta-lactamases.Antibiotic resistance in Zn(II)-deficient environments: metallo-β-lactamase activation in the periplasm.The Role of Active Site Flexible Loops in Catalysis and of Zinc in Conformational Stability of Bacillus cereus 569/H/9 β-Lactamase.The activity of the dinuclear cobalt-beta-lactamase from Bacillus cereus in catalysing the hydrolysis of beta-lactams.Low-molecular-mass penicillin binding protein 6b (DacD) is required for efficient GOB-18 metallo-β-lactamase biogenesis in Salmonella enterica and Escherichia coli.Clinical Variants of New Delhi Metallo-β-Lactamase Are Evolving To Overcome Zinc Scarcity.Zinc- and iron-dependent cytosolic metallo-beta-lactamase domain proteins exhibit similar zinc-binding affinities, independent of an atypical glutamate at the metal-binding site.In vivo folding of recombinant metallo-beta-lactamase L1 requires the presence of Zn(II).Structural studies on New Delhi Metallo-β-lactamase (NDM-2) suggest old β-lactam, penicillin to be better antibiotic for NDM-2-harbouring Acinetobacter baumanni.Coordination geometries of metal ions in d- or l-captopril-inhibited metallo-beta-lactamases.The inhibitor thiomandelic acid binds to both metal ions in metallo-beta-lactamase and induces positive cooperativity in metal binding.Metal binding Asp-120 in metallo-beta-lactamase L1 from Stenotrophomonas maltophilia plays a crucial role in catalysis.68Zn isotope exchange experiments reveal an unusual kinetic lability of the metal ions in the di-zinc form of IMP-1 metallo-beta-lactamase.Structural determinants of substrate binding to Bacillus cereus metallo-beta-lactamase.On the competition for available zinc.A convenient microbiological assay employing cell-free extracts for the rapid characterization of Gram-negative carbapenemase producers.Probing the Interaction of Aspergillomarasmine A with Metallo-β-lactamases NDM-1, VIM-2, and IMP-7.The metallo-beta-lactamase GOB is a mono-Zn(II) enzyme with a novel active site.Studies on ternary metallo-beta lactamase-inhibitor complexes using electrospray ionization mass spectrometry.On Burkholderiales order microorganisms and cystic fibrosis in Russia.

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P2860

Substrate-activated zinc binding of metallo-beta -lactamases: physiological importance of mononuclear enzymes.

http://www.wikidata.org/entity/Q43967747

description

2002 nî lūn-bûn

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2002年の論文

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2002年学术文章

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2002年学术文章

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Substrate-activated zinc bindi ...... rtance of mononuclear enzymes.

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Journal of Biological Chemistry

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Substrate-activated zinc bindi ...... ortance of mononuclear enzymes

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Bodil Rasmussen

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Hans-Werner Adolph

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Jean-Marie Frere

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Moreno Galleni

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Rogert Bauer

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Sandra Wommer

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Sandrine Rival

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Uwe Heinz

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P2860

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

The Legionella (Fluoribacter) gormanii metallo-beta-lactamase: a new member of the highly divergent lineage of molecular-subclass B3 beta-lactamases.

Metallo-beta-lactamase: structure and mechanism.

Inhibitory sites in enzymes: zinc removal and reactivation by thionein

Zinc-dependent protein folding.

Differential fluorescence labeling of cysteinyl clusters uncovers high tissue levels of thionein.

Mono- and binuclear Zn2+-beta-lactamase. Role of the conserved cysteine in the catalytic mechanism.

Standard numbering scheme for class B beta-lactamases

Characterization and sequence of the Chryseobacterium (Flavobacterium) meningosepticum carbapenemase: a new molecular class B beta-lactamase showing a broad substrate profile.

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24142-24147

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10.1074/JBC.M202467200

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27

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277

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Gianfranco Amicosante

Nicola Franceschini

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2002-04-19T00:00:00Z

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11967267

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