Penicillin-binding Proteins and the Future of -Lactam Antibiotics: The Seventh Fleming Lecture
MicrobiologyPublished 1 May 1983
Brian G. Spratt
Citations190
SJR quartileQ2
SJR score0.95
SNIP0.73
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Abstract
Microbiology Society journals contain high-quality research papers and topical review articles. We are a not-for-profit publisher and we support and invest in the microbiology community, to the benefit of everyone. This supports our principal goal to develop, expand and strengthen the networks available to our members so that they can generate new knowledge about microbes and ensure that it is shared with other communities.
Keywords
Immunology and MicrobiologyMedicineBiochemistry, Genetics and Molecular Biology
NaturePenicillin-binding proteins and cell shape in E. coli
366 Citations1975Brian G. Spratt, Arthur B. Pardee
The identification of a minor penicillin binding protein is reported which is believed to be the target at which the amidinopenicillanic acid designated FL1060 acts to affect the shape of Escherichia coli.
SciencePenicillin Target Enzyme and the Antibiotic Binding Site
81 Citations1982Judith A. Kelly, Paul C. Moews +3 more
These findings constitute direct observation of the interaction of beta-lactams with a transpeptidase enzyme and establish the feasibility of defining the molecular stereochemistry of this interaction for purposes of drug design.
International journal of peptide & protein researchSECONDARY STRUCTURE RELATIONS BETWEEN BETA‐LACTAMASES AND PENICILLIN‐SENSITIVE D—ALANINE—CARBOXYPEPTIDASES
25 Citations1981Paul C. Moews, James R. Knox +2 more
Although the 40- to 70-residue amino-terminal sequences examined contain a common serine reactive with penicillins and an R-D-alanyl- D-alanine substrate analog, no homology in secondary structure or hydration potential could be found with a serine protease such as alpha-chymotrypsin.
Philosophical transactions of the Royal Society of London. Series B, Biological sciencesThe active centres in penicillin-sensitive enzymes
19 Citations1980Jean-Marie Ghuysen, Jean‐Marie Frère +3 more
The interaction between beta-lactam antibiotics and the penicillin-sensitive enzymes is a multiple-step process and enzymes are known that form a transitory L-X-D-Ala-enzyme complex where the acyl group is ester-linked to the same serine residue as that involved in the formation of thePenicilloyl-en enzyme complex.
