Structural determinants of substrate binding to Bacillus cereus metallo-beta-lactamase.
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Asp-120 locates Zn2 for optimal metallo-beta-lactamase activityMetallo-β-lactamases withstand low Zn(II) conditions by tuning metal-ligand interactionsHis224 Alters the R2 Drug Binding Site and Phe218 Influences the Catalytic Efficiency of the Metallo- -Lactamase VIM-7Overcoming differences: The catalytic mechanism of metallo-β-lactamasesMimicking natural evolution in metallo-beta-lactamases through second-shell ligand mutations.Evolution of Metallo-β-lactamases: Trends Revealed by Natural Diversity and in vitro EvolutionHost-specific enzyme-substrate interactions in SPM-1 metallo-β-lactamase are modulated by second sphere residues.Quantitative Description of a Protein Fitness Landscape Based on Molecular Features.Clinical characteristics and antimicrobial susceptibility of Bacillus cereus blood stream infections.Probing the role of Met221 in the unusual metallo-β-lactamase GOB-18.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.Bisthiazolidines: A Substrate-Mimicking Scaffold as an Inhibitor of the NDM-1 Carbapenemase.Metallo-β-lactamase structure and function.A variety of roles for versatile zinc in metallo-β-lactamases.Catalytic role of the metal ion in the metallo-beta-lactamase GOB.The Role of Active Site Flexible Loops in Catalysis and of Zinc in Conformational Stability of Bacillus cereus 569/H/9 β-Lactamase.A general reaction mechanism for carbapenem hydrolysis by mononuclear and binuclear metallo-β-lactamases.The activity of the dinuclear cobalt-beta-lactamase from Bacillus cereus in catalysing the hydrolysis of beta-lactams.Role of zinc content on the catalytic efficiency of B1 metallo beta-lactamases.A potential substrate binding conformation of β-lactams and insight into the broad spectrum of NDM-1 activityShaping substrate selectivity in a broad spectrum metallo-β-lactamase.Hydrolysis of cephalexin and meropenem by New Delhi metallo-β-lactamase: the substrate protonation mechanism is drug dependent.On the active site of mononuclear B1 metallo β-lactamases: a computational study
P2860
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P2860
Structural determinants of substrate binding to Bacillus cereus metallo-beta-lactamase.
description
2004 nî lūn-bûn
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2004年の論文
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2004年学术文章
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2004年学术文章
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2004年学术文章
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2004年学术文章
@zh-my
2004年学术文章
@zh-sg
2004年學術文章
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2004年學術文章
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2004年學術文章
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name
Structural determinants of substrate binding to Bacillus cereus metallo-beta-lactamase.
@en
Structural determinants of substrate binding to Bacillus cereus metallo-beta-lactamase.
@nl
type
label
Structural determinants of substrate binding to Bacillus cereus metallo-beta-lactamase.
@en
Structural determinants of substrate binding to Bacillus cereus metallo-beta-lactamase.
@nl
prefLabel
Structural determinants of substrate binding to Bacillus cereus metallo-beta-lactamase.
@en
Structural determinants of substrate binding to Bacillus cereus metallo-beta-lactamase.
@nl
P2860
P356
P1476
Structural determinants of substrate binding to Bacillus cereus metallo-beta-lactamase.
@en
P2093
Alejandro J Vila
P2860
P304
26046-26051
P356
10.1074/JBC.M311373200
P407
P577
2004-03-31T00:00:00Z