BIOMAT Database Logo BIOMAT Database Logo

Evolution of enzymatic mechanisms of resistance among beta-lactam antibiotics. 1990

L Gutmann, and M D Kitzis, and J F Acar
Medical Microbiology Laboratory, Broussais Hospital, Paris, France.

Resistance to third-generation cephalosporins occurs as a result of either the production of high concentrations of chromosomal cephalosporinase or, increasingly, the presence of broad-spectrum plasmid-mediated beta-lactamases. Both cases represent the response of bacteria in the hospital setting to the selection pressure brought to bear by the use of these antibiotics. Continued evolution of the plasmid-mediated enzymes is occurring as new antibiotics are introduced, probably reflecting the process that began when the first beta-lactamase apparently evolved from the penicillin-binding proteins. beta-Lactamase inhibitors offer one approach to dealing with the evolution of resistance to previously beta-lactamase-stable antibiotics.

UI MeSH Term Description Entries
D008969 Molecular Sequence Data Descriptions of specific amino acid, carbohydrate, or nucleotide sequences which have appeared in the published literature and/or are deposited in and maintained by databanks such as GENBANK, European Molecular Biology Laboratory (EMBL), National Biomedical Research Foundation (NBRF), or other sequence repositories. Sequence Data, Molecular,Molecular Sequencing Data,Data, Molecular Sequence,Data, Molecular Sequencing,Sequencing Data, Molecular
D011550 Pseudomonas aeruginosa A species of gram-negative, aerobic, rod-shaped bacteria commonly isolated from clinical specimens (wound, burn, and urinary tract infections). It is also found widely distributed in soil and water. P. aeruginosa is a major agent of nosocomial infection. Bacillus aeruginosus,Bacillus pyocyaneus,Bacterium aeruginosum,Bacterium pyocyaneum,Micrococcus pyocyaneus,Pseudomonas polycolor,Pseudomonas pyocyanea
D002510 Cephalosporinase beta-Lactamase II,Cephalexin Amidase,Cephalosporin Amido-beta-Lactam Hydrolase,Cephalosporin beta-Lactamase,Amidase, Cephalexin,Amido-beta-Lactam Hydrolase, Cephalosporin,Cephalosporin Amido beta Lactam Hydrolase,Cephalosporin beta Lactamase,Hydrolase, Cephalosporin Amido-beta-Lactam,beta Lactamase II,beta-Lactamase, Cephalosporin
D002511 Cephalosporins A group of broad-spectrum antibiotics first isolated from the Mediterranean fungus ACREMONIUM. They contain the beta-lactam moiety thia-azabicyclo-octenecarboxylic acid also called 7-aminocephalosporanic acid. Antibiotics, Cephalosporin,Cephalosporanic Acid,Cephalosporin,Cephalosporin Antibiotic,Cephalosporanic Acids,Acid, Cephalosporanic,Acids, Cephalosporanic,Antibiotic, Cephalosporin,Cephalosporin Antibiotics
D002876 Chromosomes, Bacterial Structures within the nucleus of bacterial cells consisting of or containing DNA, which carry genetic information essential to the cell. Bacterial Chromosome,Bacterial Chromosomes,Chromosome, Bacterial
D004352 Drug Resistance, Microbial The ability of microorganisms, especially bacteria, to resist or to become tolerant to chemotherapeutic agents, antimicrobial agents, or antibiotics. This resistance may be acquired through gene mutation or foreign DNA in transmissible plasmids (R FACTORS). Antibiotic Resistance,Antibiotic Resistance, Microbial,Antimicrobial Resistance, Drug,Antimicrobial Drug Resistance,Antimicrobial Drug Resistances,Antimicrobial Resistances, Drug,Drug Antimicrobial Resistance,Drug Antimicrobial Resistances,Drug Resistances, Microbial,Resistance, Antibiotic,Resistance, Drug Antimicrobial,Resistances, Drug Antimicrobial
D004755 Enterobacteriaceae A family of gram-negative, facultatively anaerobic, rod-shaped bacteria that do not form endospores. Its organisms are distributed worldwide with some being saprophytes and others being plant and animal parasites. Many species are of considerable economic importance due to their pathogenic effects on agriculture and livestock. Coliform Bacilli,Enterobacteria,Ewingella,Leclercia,Paracolobactrum,Sodalis
D000595 Amino Acid Sequence The order of amino acids as they occur in a polypeptide chain. This is referred to as the primary structure of proteins. It is of fundamental importance in determining PROTEIN CONFORMATION. Protein Structure, Primary,Amino Acid Sequences,Sequence, Amino Acid,Sequences, Amino Acid,Primary Protein Structure,Primary Protein Structures,Protein Structures, Primary,Structure, Primary Protein,Structures, Primary Protein
D000900 Anti-Bacterial Agents Substances that inhibit the growth or reproduction of BACTERIA. Anti-Bacterial Agent,Anti-Bacterial Compound,Anti-Mycobacterial Agent,Antibacterial Agent,Antibiotics,Antimycobacterial Agent,Bacteriocidal Agent,Bacteriocide,Anti-Bacterial Compounds,Anti-Mycobacterial Agents,Antibacterial Agents,Antibiotic,Antimycobacterial Agents,Bacteriocidal Agents,Bacteriocides,Agent, Anti-Bacterial,Agent, Anti-Mycobacterial,Agent, Antibacterial,Agent, Antimycobacterial,Agent, Bacteriocidal,Agents, Anti-Bacterial,Agents, Anti-Mycobacterial,Agents, Antibacterial,Agents, Antimycobacterial,Agents, Bacteriocidal,Anti Bacterial Agent,Anti Bacterial Agents,Anti Bacterial Compound,Anti Bacterial Compounds,Anti Mycobacterial Agent,Anti Mycobacterial Agents,Compound, Anti-Bacterial,Compounds, Anti-Bacterial
D001618 beta-Lactamases Enzymes found in many bacteria which catalyze the hydrolysis of the amide bond in the beta-lactam ring. Well known antibiotics destroyed by these enzymes are penicillins and cephalosporins. beta-Lactamase,beta Lactamase,beta Lactamases

Related Publications

L Gutmann, and M D Kitzis, and J F Acar
[Mechanisms of action of beta-lactam antibiotics and mechanisms of non-enzymatic resistance].
December 1986, Presse medicale (Paris, France : 1983),
L Gutmann, and M D Kitzis, and J F Acar
[Mechanism of enzymatic resistance to beta-lactam antibiotics].
December 1986, Presse medicale (Paris, France : 1983),
L Gutmann, and M D Kitzis, and J F Acar
Mechanisms of resistance to beta-lactam antibiotics.
February 1985, Chemioterapia : international journal of the Mediterranean Society of Chemotherapy,
L Gutmann, and M D Kitzis, and J F Acar
[Mechanisms of resistance to beta-lactam antibiotics].
January 1993, Infection,
L Gutmann, and M D Kitzis, and J F Acar
Mechanisms of resistance to beta-lactam antibiotics.
January 1991, Scandinavian journal of infectious diseases. Supplementum,
L Gutmann, and M D Kitzis, and J F Acar
[Mechanisms of microorganism resistance to beta-lactam antibiotics].
January 2014, Zhurnal mikrobiologii, epidemiologii i immunobiologii,
L Gutmann, and M D Kitzis, and J F Acar
Mutational enzymatic resistance of Enterobacter species to beta-lactam antibiotics.
April 1982, Antimicrobial agents and chemotherapy,
L Gutmann, and M D Kitzis, and J F Acar
Cooperative evolution of mechanisms of beta-lactam resistance.
January 2000, Clinical microbiology and infection : the official publication of the European Society of Clinical Microbiology and Infectious Diseases,
L Gutmann, and M D Kitzis, and J F Acar
Mechanisms of resistance of enterococci to beta-lactam antibiotics.
February 1990, European journal of clinical microbiology & infectious diseases : official publication of the European Society of Clinical Microbiology,
L Gutmann, and M D Kitzis, and J F Acar
Diversity of the mechanisms of resistance to beta-lactam antibiotics.
January 1991, Research in microbiology,
Copied contents to your clipboard!