Structural basis for the inactivation of the P54 mutant of beta-lactamase from Staphylococcus aureus PC1
about
EstB from Burkholderia gladioli: A novel esterase with a β-lactamase fold reveals steric factors to discriminate between esterolytic and β-lactam cleaving activityLigand-Dependent Disorder of the Loop Observed in Extended-Spectrum SHV-Type -LactamaseExploring the role of a conserved class A residue in the Ω-Loop of KPC-2 β-lactamase: a mechanism for ceftazidime hydrolysisRoles of amino acids 161 to 179 in the PSE-4 omega loop in substrate specificity and in resistance to ceftazidimeNovel SHV-derived extended-spectrum beta-lactamase, SHV-57, that confers resistance to ceftazidime but not cefazolin.Effects of Asp-179 mutations in TEMpUC19 beta-lactamase on susceptibility to beta-lactamsExtended-spectrum and inhibitor-resistant TEM-type beta-lactamases: mutations, specificity, and three-dimensional structure.Evolution of extended-spectrum beta-lactam resistance (SHV-8) in a strain of Escherichia coli during multiple episodes of bacteremia.Systematic mutagenesis of the active site omega loop of TEM-1 beta-lactamaseSubstitution of Asp for Asn at position 132 in the active site of TEM beta-lactamase. Activity toward different substrates and effects of neighboring residues.Site-directed mutagenesis of beta-lactamase I: role of Glu-166.Structural basis of extended spectrum TEM beta-lactamases. Crystallographic, kinetic, and mass spectrometric investigations of enzyme mutants.The bla gene of the cephamycin cluster of Streptomyces clavuligerus encodes a class A beta-lactamase of low enzymatic activity.Catalytic properties of class A beta-lactamases: efficiency and diversity.Efficient catalysis by beta-lactamase from Staphylococcus aureus PC1 accompanied by accumulation of an acyl-enzyme.Multiple substitutions at position 104 of beta-lactamase TEM-1: assessing the role of this residue in substrate specificity.pKa calculations for class A beta-lactamases: methodological and mechanistic implications.Klebsiella pneumoniae Carbapenemase-2 (KPC-2), Substitutions at Ambler Position Asp179, and Resistance to Ceftazidime-Avibactam: Unique Antibiotic-Resistant Phenotypes Emerge from β-Lactamase Protein Engineering.Effects on substrate profile by mutational substitutions at positions 164 and 179 of the class A TEM(pUC19) beta-lactamase from Escherichia coli.A new TEM beta-lactamase double mutant with broadened specificity reveals substrate-dependent functional interactions.Evolution of antibiotic resistance: several different amino acid substitutions in an active site loop alter the substrate profile of beta-lactamase.
P2860
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P2860
Structural basis for the inactivation of the P54 mutant of beta-lactamase from Staphylococcus aureus PC1
description
1991 nî lūn-bûn
@nan
1991 թուականի Հոկտեմբերին հրատարակուած գիտական յօդուած
@hyw
1991 թվականի հոտեմբերին հրատարակված գիտական հոդված
@hy
1991年の論文
@ja
1991年論文
@yue
1991年論文
@zh-hant
1991年論文
@zh-hk
1991年論文
@zh-mo
1991年論文
@zh-tw
1991年论文
@wuu
name
Structural basis for the inact ...... from Staphylococcus aureus PC1
@ast
Structural basis for the inact ...... from Staphylococcus aureus PC1
@en
Structural basis for the inact ...... from Staphylococcus aureus PC1
@nl
type
label
Structural basis for the inact ...... from Staphylococcus aureus PC1
@ast
Structural basis for the inact ...... from Staphylococcus aureus PC1
@en
Structural basis for the inact ...... from Staphylococcus aureus PC1
@nl
prefLabel
Structural basis for the inact ...... from Staphylococcus aureus PC1
@ast
Structural basis for the inact ...... from Staphylococcus aureus PC1
@en
Structural basis for the inact ...... from Staphylococcus aureus PC1
@nl
P2093
P356
P1433
P1476
Structural basis for the inact ...... from Staphylococcus aureus PC1
@en
P2093
P304
P356
10.1021/BI00103A017
P407
P577
1991-10-01T00:00:00Z