Reference : Penicillin target enzyme and the antibiotic binding site
Scientific journals : Article
Life sciences : Microbiology
Life sciences : Biochemistry, biophysics & molecular biology
http://hdl.handle.net/2268/93325
Penicillin target enzyme and the antibiotic binding site
English
Kelly, Judith A. [University of Connecticut - UCONN > Biologicale Sciences Group - Institut of Material Science > > >]
Moews, Paul C. [University of Connecticut - UCONN > Biologicale Sciences Group - Institut of Material Science > > > >]
Knox, James R. [University of Connecticut - UCONN > Biologicale Sciences Group - Institut of Material Science > > >]
Frère, Jean-Marie mailto [Université de Liège - ULg > Faculté de Médecine > Service de Microbiologie > >]
Ghuysen, Jean-Marie [Université de Liège - ULg > Faculté de Médecine > Service de Microbiologie > > >]
29-Oct-1982
Science
American Association for the Advancement of Science
218
4571
479-481
Yes (verified by ORBi)
International
0036-8075
1095-9203
Washington
DC
[en] binding sites ; carboxypeptidases ; cephalosporins ; crystallography ; models, molecular ; muramoylpentapeptide carboxypeptidase ; penicillins ; protein conformation ; x-ray diffraction
[en] The three-dimensional structure of a penicillin-sensitive D-alanyl-carboxypeptidase-transpeptidase has been determined by x-ray crystallography to a resolution of 2.8 angstroms. The site of binding of the beta-lactam antibiotics penicillin and cephalosporin has been located. 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.
Researchers ; Professionals
http://hdl.handle.net/2268/93325

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