Site-directed mutagenesis of glutamate-166 in beta-lactamase leads to a branched path mechanism.
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EstB from Burkholderia gladioli: A novel esterase with a β-lactamase fold reveals steric factors to discriminate between esterolytic and β-lactam cleaving activityThe Acylation Mechanism of CTX-M β-Lactamase at 0.88 Å ResolutionStructural and Biochemical Evidence That a TEM-1 -Lactamase N170G Active Site Mutant Acts via Substrate-assisted CatalysisThe active site protonation states of perdeuterated Toho-1 β-lactamase determined by neutron diffraction support a role for Glu166 as the general base in acylationAnalysis of the Binding Forces Driving the Tight Interactions between -Lactamase Inhibitory Protein-II (BLIP-II) and Class A -LactamasesNeutron and X-ray Crystal Structures of a Perdeuterated Enzyme Inhibitor Complex Reveal the Catalytic Proton Network of the Toho-1 -Lactamase for the Acylation ReactionX-ray evidence of a native state with increased compactness populated by tryptophan-less B. licheniformis β-lactamaseA triple mutant in the Ω-loop of TEM-1 β-lactamase changes the substrate profile via a large conformational change and an altered general base for catalysisRoles of amino acids 161 to 179 in the PSE-4 omega loop in substrate specificity and in resistance to ceftazidimeX-ray crystallographic analysis of 6-aminohexanoate-dimer hydrolase: molecular basis for the birth of a nylon oligomer-degrading enzyme.Extended-spectrum and inhibitor-resistant TEM-type beta-lactamases: mutations, specificity, and three-dimensional structure.Cytoplasmic-membrane anchoring of a class A beta-lactamase and its capacity in manifesting antibiotic resistanceLigand-Induced Proton Transfer and Low-Barrier Hydrogen Bond Revealed by X-ray Crystallography.A point mutation leads to altered product specificity in beta-lactamase catalysisActive-Site Protonation States in an Acyl-Enzyme Intermediate of a Class A β-Lactamase with a Monobactam SubstrateThe structure of Toho1 β-lactamase in complex with penicillin reveals the role of Tyr105 in substrate recognition.Role of residues 104, 164, 166, 238 and 240 in the substrate profile of PER-1 beta-lactamase hydrolysing third-generation cephalosporins.pKa, MM, and QM studies of mechanisms of beta-lactamases and penicillin-binding proteins: acylation step.Mechanisms of proton relay and product release by Class A β-lactamase at ultrahigh resolution.Export and folding of signal-sequenceless Bacillus licheniformisβ-lactamase in Escherichia coli
P2860
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P2860
Site-directed mutagenesis of glutamate-166 in beta-lactamase leads to a branched path mechanism.
description
1994 nî lūn-bûn
@nan
1994年の論文
@ja
1994年学术文章
@wuu
1994年学术文章
@zh
1994年学术文章
@zh-cn
1994年学术文章
@zh-hans
1994年学术文章
@zh-my
1994年学术文章
@zh-sg
1994年學術文章
@yue
1994年學術文章
@zh-hant
name
Site-directed mutagenesis of g ...... to a branched path mechanism.
@en
Site-directed mutagenesis of g ...... to a branched path mechanism.
@nl
type
label
Site-directed mutagenesis of g ...... to a branched path mechanism.
@en
Site-directed mutagenesis of g ...... to a branched path mechanism.
@nl
prefLabel
Site-directed mutagenesis of g ...... to a branched path mechanism.
@en
Site-directed mutagenesis of g ...... to a branched path mechanism.
@nl
P2093
P356
P1433
P1476
Site-directed mutagenesis of g ...... to a branched path mechanism.
@en
P2093
P304
P356
10.1021/BI00190A015
P407
P577
1994-06-01T00:00:00Z