Pages that link to "Q43967747"

The following pages link to Substrate-activated zinc binding of metallo-beta -lactamases: physiological importance of mononuclear enzymes. (Q43967747):

Displaying 48 items.

• Crystal structures of a purple acid phosphatase, representing different steps of this enzyme's catalytic cycle (Q21256411) (← links)
• 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 (Q27640258) (← links)
• The 1.5-A structure of Chryseobacterium meningosepticum zinc beta-lactamase in complex with the inhibitor, D-captopril (Q27640947) (← links)
• The Structure of the Dizinc Subclass B2 Metallo- -Lactamase CphA Reveals that the Second Inhibitory Zinc Ion Binds in the Histidine Site (Q27656866) (← links)
• The Role of Zn2+on the Structure and Stability of Murine Adenosine Deaminase (Q27664258) (← links)
• Glycolytic and Non-glycolytic Functions of Mycobacterium tuberculosis Fructose-1,6-bisphosphate Aldolase, an Essential Enzyme Produced by Replicating and Non-replicating Bacilli (Q27674487) (← links)
• Metallo-β-lactamases withstand low Zn(II) conditions by tuning metal-ligand interactions (Q27681358) (← links)
• Trapping and characterization of a reaction intermediate in carbapenem hydrolysis by B. cereus metallo-beta-lactamase (Q30486102) (← links)
• The binding of iron and zinc to glyoxalase II occurs exclusively as di-metal centers and is unique within the metallo-beta-lactamase family (Q33201101) (← links)
• Zinc ion-induced domain organization in metallo-beta-lactamases: a flexible "zinc arm" for rapid metal ion transfer? (Q33435167) (← links)
• Molecular dynamics simulations of metalloproteins (Q35053362) (← links)
• Grafting a new metal ligand in the cocatalytic site of B. cereus metallo-beta-lactamase: structural flexibility without loss of activity. (Q36572122) (← links)
• X-ray absorption spectroscopy of metal site speciation in the metallo-β-lactamase BcII from Bacillus cereus. (Q36607755) (← links)
• When all's zed and done: the structure and function of RNase Z in prokaryotes (Q36761180) (← links)
• Membrane anchoring stabilizes and favors secretion of New Delhi metallo-β-lactamase (Q37017171) (← links)
• Role of the Zn1 and Zn2 sites in metallo-beta-lactamase L1 (Q37182382) (← links)
• Metal content of metallo-beta-lactamase L1 is determined by the bioavailability of metal ions. (Q37361336) (← links)
• Metallo-β-lactamase structure and function (Q38060809) (← links)
• The mechanisms of catalysis by metallo beta-lactamases (Q39019943) (← links)
• Antibiotic resistance in Zn(II)-deficient environments: metallo-β-lactamase activation in the periplasm. (Q39375052) (← links)
• The Role of Active Site Flexible Loops in Catalysis and of Zinc in Conformational Stability of Bacillus cereus 569/H/9 β-Lactamase (Q39729538) (← links)
• The activity of the dinuclear cobalt-beta-lactamase from Bacillus cereus in catalysing the hydrolysis of beta-lactams (Q41083962) (← links)
• Low-molecular-mass penicillin binding protein 6b (DacD) is required for efficient GOB-18 metallo-β-lactamase biogenesis in Salmonella enterica and Escherichia coli (Q41907542) (← links)
• Clinical Variants of New Delhi Metallo-β-Lactamase Are Evolving To Overcome Zinc Scarcity. (Q41992585) (← links)
• 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. (Q42044939) (← links)
• In vivo folding of recombinant metallo-beta-lactamase L1 requires the presence of Zn(II). (Q43094802) (← links)
• IMP-1 metallo-beta-lactamase: effect of chelators and assessment of metal requirement by electrospray mass spectrometry. (Q44045664) (← links)
• 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 (Q44099218) (← links)
• Coordination geometries of metal ions in d- or l-captopril-inhibited metallo-beta-lactamases (Q44385766) (← links)
• The inhibitor thiomandelic acid binds to both metal ions in metallo-beta-lactamase and induces positive cooperativity in metal binding (Q44425130) (← links)
• Metal binding Asp-120 in metallo-beta-lactamase L1 from Stenotrophomonas maltophilia plays a crucial role in catalysis. (Q44628472) (← links)
• 68Zn isotope exchange experiments reveal an unusual kinetic lability of the metal ions in the di-zinc form of IMP-1 metallo-beta-lactamase. (Q44864754) (← links)
• Structural determinants of substrate binding to Bacillus cereus metallo-beta-lactamase (Q44894410) (← links)
• On the competition for available zinc (Q45145749) (← links)
• A convenient microbiological assay employing cell-free extracts for the rapid characterization of Gram-negative carbapenemase producers (Q46611886) (← links)
• Loss of enzyme activity during turnover of the Bacillus cereus beta-lactamase catalysed hydrolysis of beta-lactams due to loss of zinc ion. (Q46617087) (← links)
• Site-selective binding of Zn(II) to metallo-beta-lactamase L1 from Stenotrophomonas maltophilia (Q46953056) (← links)
• Probing the Interaction of Aspergillomarasmine A with Metallo-β-lactamases NDM-1, VIM-2, and IMP-7. (Q47722687) (← links)
• The metallo-beta-lactamase GOB is a mono-Zn(II) enzyme with a novel active site. (Q48080395) (← links)
• Studies on ternary metallo-beta lactamase-inhibitor complexes using electrospray ionization mass spectrometry (Q51197571) (← links)
• On Burkholderiales order microorganisms and cystic fibrosis in Russia. (Q52367440) (← links)
• Kinetic and mechanistic studies of the reactivity of Zn–OHn (n=1 or 2) species in small molecule analogs of zinc-containing metalloenzymes (Q59591249) (← links)
• The metal ion requirements of Arabidopsis thaliana Glx2-2 for catalytic activity (Q84735970) (← links)
• Bioinformatic Exploration of Metal-Binding Proteome of Zoonotic Pathogen Orientia tsutsugamushi (Q90681398) (← links)
• Structural and biochemical analysis of the metallo-β-lactamase L1 from emerging pathogen Stenotrophomonas maltophilia revealed the subtle but distinct di-metal scaffold for catalytic activity (Q92040874) (← links)
• Antibiotic resistance breakers: current approaches and future directions (Q92441701) (← links)
• β-Lactamases and β-Lactamase Inhibitors in the 21st Century (Q92930337) (← links)
• Studies on ternary metallo-β lactamase-inhibitor complexes using electrospray ionization mass spectrometry (Q95790923) (← links)