Purification, characterization, and kinetic studies of a soluble Bacteroides fragilis metallo-beta-lactamase that provides multiple antibiotic resistance.
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Overcoming differences: The catalytic mechanism of metallo-β-lactamasesIdentification of residues critical for metallo-beta-lactamase function by codon randomization and selectionMetallo-beta-lactamases: the quiet before the storm?Biochemical, mechanistic, and spectroscopic characterization of metallo-β-lactamase VIM-2.Azolylthioacetamide: A Highly Promising Scaffold for the Development of Metallo-β-lactamase Inhibitors.Amino Acid Thioester Derivatives: A Highly Promising Scaffold for the Development of Metallo-β-lactamase L1 Inhibitors.Meropenem and chromacef intermediates observed in IMP-25 metallo-β-lactamase-catalyzed hydrolysis.Differential binding of Co(II) and Zn(II) to metallo-beta-lactamase Bla2 from Bacillus anthracis.Conformational dynamics of metallo-β-lactamase CcrA during catalysis investigated by using DEER spectroscopyTriazolylthioacetamide: A Valid Scaffold for the Development of New Delhi Metallo-β-Lactmase-1 (NDM-1) InhibitorsInvestigating the position of the hairpin loop in New Delhi metallo-β-lactamase, NDM-1, during catalysis and inhibitor bindingThe quorum-quenching metallo-gamma-lactonase from Bacillus thuringiensis exhibits a leaving group thio effectFolding strategy to prepare Co(II)-substituted metallo-beta-lactamase L1.Mechanistic studies on the mononuclear ZnII-containing metallo-beta-lactamase ImiS from Aeromonas sobria.Role of the Zn1 and Zn2 sites in metallo-beta-lactamase L1New β-phospholactam as a carbapenem transition state analog: Synthesis of a broad-spectrum inhibitor of metallo-β-lactamasesMetal content of metallo-beta-lactamase L1 is determined by the bioavailability of metal ions.Characterization of monomeric L1 metallo-beta -lactamase and the role of the N-terminal extension in negative cooperativity and antibiotic hydrolysis.Mono- and binuclear Zn2+-beta-lactamase. Role of the conserved cysteine in the catalytic mechanism.The mechanisms of catalysis by metallo beta-lactamases.Structural and functional studies of a metallo-β-lactamase unveil a new type of structurally encoded nickel-containing heterodinuclear site.The activity of the dinuclear cobalt-beta-lactamase from Bacillus cereus in catalysing the hydrolysis of beta-lactams.Properties and distribution of a metallo-β-lactamase (ALI-1) from the fish pathogen Aliivibrio salmonicida LFI1238.Role of a solvent-exposed tryptophan in the recognition and binding of antibiotic substrates for a metallo-beta-lactamase.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.Structural determinants of substrate binding to Bacillus cereus metallo-beta-lactamase.Probing the role of Asp-120(81) of metallo-beta-lactamase (IMP-1) by site-directed mutagenesis, kinetic studies, and X-ray crystallography.Catalytic mechanism of class B2 metallo-beta-lactamase.Characterization of a potential β-lactamase inhibitory metabolite from a marine Streptomyces sp. PM49 active against multidrug-resistant pathogens.Label-free measurements of reaction kinetics using a droplet-based optofluidic device.
P2860
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P2860
Purification, characterization, and kinetic studies of a soluble Bacteroides fragilis metallo-beta-lactamase that provides multiple antibiotic resistance.
description
1998 nî lūn-bûn
@nan
1998年の論文
@ja
1998年学术文章
@wuu
1998年学术文章
@zh-cn
1998年学术文章
@zh-hans
1998年学术文章
@zh-my
1998年学术文章
@zh-sg
1998年學術文章
@yue
1998年學術文章
@zh
1998年學術文章
@zh-hant
name
Purification, characterization ...... ultiple antibiotic resistance.
@en
type
label
Purification, characterization ...... ultiple antibiotic resistance.
@en
prefLabel
Purification, characterization ...... ultiple antibiotic resistance.
@en
P2860
P356
P1476
Purification, characterization ...... ultiple antibiotic resistance.
@en
P2093
P2860
P304
22402-22408
P356
10.1074/JBC.273.35.22402
P407
P577
1998-08-01T00:00:00Z