Beta-lactamases as fully efficient enzymes. Determination of all the rate constants in the acyl-enzyme mechanism.
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Structural and Biochemical Evidence That a TEM-1 -Lactamase N170G Active Site Mutant Acts via Substrate-assisted CatalysisAnalysis of the Binding Forces Driving the Tight Interactions between -Lactamase Inhibitory Protein-II (BLIP-II) and Class A -LactamasesIdentification and characterization of beta-lactamase inhibitor protein-II (BLIP-II) interactions with beta-lactamases using phage display.Enzyme Efficiency but Not Thermostability Drives Cefotaxime Resistance Evolution in TEM-1 β-Lactamase.Class C beta-lactamases operate at the diffusion limit for turnover of their preferred cephalosporin substrates.Multiple global suppressors of protein stability defects facilitate the evolution of extended-spectrum TEM β-lactamases.Biochemical characterization of beta-lactamases Bla1 and Bla2 from Bacillus anthracis.Activation of BlaR1 protein of methicillin-resistant Staphylococcus aureus, its proteolytic processing, and recovery from induction of resistance.Modelling non-Markovian dynamics in biochemical reactions.Cytoplasmic-membrane anchoring of a class A beta-lactamase and its capacity in manifesting antibiotic resistanceAvibactam is a covalent, reversible, non-β-lactam β-lactamase inhibitorElectrostatic steering and ionic tethering in enzyme-ligand binding: insights from simulations.TEM-1 beta-lactamase as a scaffold for protein recognition and assayMore extended-spectrum beta-lactamasesSite-directed mutagenesis of beta-lactamase I: role of Glu-166.A dramatic change in the rate-limiting step of beta-lactam hydrolysis results from the substitution of the active-site serine residue by a cysteine in the class-C beta-lactamase of Enterobacter cloacae 908RActive-site serine mutants of the Streptomyces albus G beta-lactamase.Efficient catalysis by beta-lactamase from Staphylococcus aureus PC1 accompanied by accumulation of an acyl-enzyme.The mechanism of action of DD-peptidases: the role of tyrosine-159 in the Streptomyces R61 DD-peptidase.Predicting allosteric mutants that increase activity of a major antibiotic resistance enzyme.Functional analyses of AmpC beta-lactamase through differential stability.Substrate-induced inactivation of the OXA2 beta-lactamase.Relative specificities of a series of beta-lactam-recognizing enzymes towards the side-chains of penicillins and of acyclic thioldepsipeptides.Analysis of the plasticity of location of the Arg244 positive charge within the active site of the TEM-1 beta-lactamaseKinetic parameters of the acyl-enzyme mechanism and conditions for quasi-equilibrium and for optimal catalytic characteristics.Site-directed mutagenesis and substrate-induced inactivation of beta-lactamase I.The kinetics of non-stoichiometric bursts of beta-lactam hydrolysis catalysed by class C beta-lactamases.The mechanism of action of DD-peptidases: the role of Threonine-299 and -301 in the Streptomyces R61 DD-peptidase.The analysis of rate limitation within enzymes: relations between flux control coefficients of rate constants and unidirectional rates, rate constants and thermodynamic parameters of single isolated enzymesSite-directed mutagenesis of beta-lactamase I. Single and double mutants of Glu-166 and Lys-73.Irreversible inactivation of beta-lactamase I from Bacillus cereus by chlorinated 6-spiroepoxypenicillins.Peptidase activity of beta-lactamases.NMR dynamics of PSE-4 beta-lactamase: an interplay of ps-ns order and mus-ms motions in the active site.Kinetic parameters of the acyl-enzyme mechanism.Structural and Mechanistic Basis for Extended-Spectrum Drug-Resistance Mutations in Altering the Specificity of TEM, CTX-M, and KPC β-lactamases.
P2860
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P2860
Beta-lactamases as fully efficient enzymes. Determination of all the rate constants in the acyl-enzyme mechanism.
description
1990 nî lūn-bûn
@nan
1990年の論文
@ja
1990年論文
@yue
1990年論文
@zh-hant
1990年論文
@zh-hk
1990年論文
@zh-mo
1990年論文
@zh-tw
1990年论文
@wuu
1990年论文
@zh
1990年论文
@zh-cn
name
Beta-lactamases as fully effic ...... in the acyl-enzyme mechanism.
@en
type
label
Beta-lactamases as fully effic ...... in the acyl-enzyme mechanism.
@en
prefLabel
Beta-lactamases as fully effic ...... in the acyl-enzyme mechanism.
@en
P2093
P2860
P1433
P1476
Beta-lactamases as fully effic ...... in the acyl-enzyme mechanism.
@en
P2093
H Christensen
M T Martin
P2860
P304
P407
P577
1990-03-01T00:00:00Z