Inactivation of TEM-1 β-lactamase by 6-acetylmethylenepenicillanic acid
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چکیده
منابع مشابه
Dynamical Aspects of TEM-1 β-Lactamase Probed by Molecular Dynamics
The dynamical aspects of the fully hydrated TEM-1 beta-lactamase have been determined by a 5 ns Molecular Dynamics simulation. Starting from the crystallographic coordinates, the protein shows a relaxation in water with an overall root mean square deviation from the crystal structure increasing up to 0.17 nm, within the first nanosecond. Then a plateau is reached and the molecule fluctuates aro...
متن کاملPurification of TEM-1 beta-lactamase by immunoaffinity chromatography.
A monoclonal antibody prepared against TEM-1 beta-lactamase was found to compete with penicillins and cephalosporins for binding to the enzyme. The purified antibody preparation was linked to Sepharose 4B and used for immunoaffinity-chromatography purification of TEM-1 beta-lactamase. Elution with either benzylpenicillin or cloxacillin yielded a highly purified, concentrated and active enzyme p...
متن کاملIdentification of Amino Acid Substitutions That Alter the Substrate Specificity of TEM - 1 1 - Lactamase TIMOTHY
TEM-1 1-lactamase is the most prevalent plasmid-mediated 13-lactamase in gram-negative bacteria. Recently, TEM I-lactamase variants with amino acid substitutions in the active-site pocket of the enzyme have been identified in natural isolates with increased resistance to extended-spectrum cephalosporins. To identify other amino acid substitutions that alter the activity of TEM-1 towards extende...
متن کاملRole of pleiotropy during adaptation of TEM-1 β-lactamase to two novel antibiotics
Pleiotropy is a key feature of the genotype-phenotype map, and its form and extent have many evolutionary implications, including for the dynamics of adaptation and the evolution of specialization. Similarly, pleiotropic effects of antibiotic resistance mutations may affect the evolution of antibiotic resistance in the simultaneous or fluctuating presence of different antibiotics. Here, we stud...
متن کاملEvolvability as a Function of Purifying Selection in TEM-1 β-Lactamase
Evolvability—the capacity to generate beneficial heritable variation—is a central property of biological systems. However, its origins and modulation by environmental factors have not been examined systematically. Here, we analyze the fitness effects of all single mutations in TEM-1 β-lactamase (4,997 variants) under selection for the wild-type function (ampicillin resistance) and for a new fun...
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ژورنال
عنوان ژورنال: Biochemical Journal
سال: 1983
ISSN: 0264-6021
DOI: 10.1042/bj2090609