A survey of the kinetic parameters of class C beta-lactamases. Penicillins.
about
Crystal structure of a cold-adapted class C beta-lactamaseStructure of ADC-68, a novel carbapenem-hydrolyzing class C extended-spectrum β-lactamase isolated from Acinetobacter baumanniiIdentification of residues critical for catalysis in a class C beta-lactamase by combinatorial scanning mutagenesis.Saturation mutagenesis of Asn152 reveals a substrate selectivity switch in P99 cephalosporinaseCloning and expression of a cloxacillin-hydrolyzing enzyme and a cephalosporinase from Aeromonas sobria AER 14M in Escherichia coli: requirement for an E. coli chromosomal mutation for efficient expression of the class D enzymeGenetic and biochemical characterization of TRU-1, the endogenous class C beta-lactamase from Aeromonas enteropelogenesCENTA as a chromogenic substrate for studying beta-lactamases.Kinetic study of two novel enantiomeric tricyclic beta-lactams which efficiently inactivate class C beta-lactamases.Chemical complementation: a reaction-independent genetic assay for enzyme catalysis.Structural basis for the extended substrate spectrum of CMY-10, a plasmid-encoded class C beta-lactamase.Characterization of the chromosomal cephalosporinases produced by Acinetobacter lwoffii and Acinetobacter baumannii clinical isolatesA novel family VIII carboxylesterase hydrolysing third- and fourth-generation cephalosporins.Characterization of a Carbapenem-Hydrolyzing Enzyme, PoxB, in Pseudomonas aeruginosa PAO1.Permeation rates of penicillins indicate that Escherichia coli porins function principally as nonspecific channelsAmpC beta-lactamases.Modifications of the C6-substituent of penicillin sulfones with the goal of improving inhibitor recognition and efficacy.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 908RCharacterization of beta-lactamases.Contributions of the AmpC beta-lactamase and the AcrAB multidrug efflux system in intrinsic resistance of Escherichia coli K-12 to beta-lactams.Method for estimation of low outer membrane permeability to beta-lactam antibiotics.Purification and characterization of a new beta-lactamase from Bacteroides uniformis.Carbapenem-hydrolyzing beta-lactamases.The beta-lactamase secreted by the antarctic psychrophile Psychrobacter immobilis A8Novel beta-lactamase from Capnocytophaga sp.Kinetic parameters of efflux of penicillins by the multidrug efflux transporter AcrAB-TolC of Escherichia coli.When drug inactivation renders the target irrelevant to antibiotic resistance: a case story with beta-lactams.Beta-lactam resistance in anaerobic bacteria: a review.Kinetic properties of four plasmid-mediated AmpC beta-lactamases.A survey of the kinetic parameters of class C beta-lactamases. Cephalosporins and other beta-lactam compounds.Purification of a class C A-type beta-lactamase from a derepressed strain of Enterobacter cloacae. Comparison of the wild-type and mutant enzyme with those from strains P99, 208 and GN7471.The diversity of the catalytic properties of class A beta-lactamases.A comparative study of class-D beta-lactamases.Use of electrospray mass spectrometry to directly observe an acyl enzyme intermediate in beta-lactamase catalysis.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.Importance of the two tryptophan residues in the Streptomyces R61 exocellular DD-peptidase.Interactions between active-site-serine beta-lactamases and compounds bearing a methoxy side chain on the alpha-face of the beta-lactam ring: kinetic and molecular modelling studies.Kinetic properties of the Bacillus licheniformis penicillin-binding proteinsCatalytic mechanism of active-site serine beta-lactamases: role of the conserved hydroxy group of the Lys-Thr(Ser)-Gly triad.The role of lysine-67 in a class C beta-lactamase is mainly electrostatic.
P2860
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P2860
A survey of the kinetic parameters of class C beta-lactamases. Penicillins.
description
1988 nî lūn-bûn
@nan
1988年の論文
@ja
1988年論文
@yue
1988年論文
@zh-hant
1988年論文
@zh-hk
1988年論文
@zh-mo
1988年論文
@zh-tw
1988年论文
@wuu
1988年论文
@zh
1988年论文
@zh-cn
name
A survey of the kinetic parameters of class C beta-lactamases. Penicillins.
@en
A survey of the kinetic parameters of class C beta-lactamases. Penicillins.
@nl
type
label
A survey of the kinetic parameters of class C beta-lactamases. Penicillins.
@en
A survey of the kinetic parameters of class C beta-lactamases. Penicillins.
@nl
prefLabel
A survey of the kinetic parameters of class C beta-lactamases. Penicillins.
@en
A survey of the kinetic parameters of class C beta-lactamases. Penicillins.
@nl
P2860
P356
P1433
P1476
A survey of the kinetic parameters of class C beta-lactamases. Penicillins.
@en
P2093
P2860
P304
P356
10.1042/BJ2550119
P407
P577
1988-10-01T00:00:00Z