Reference : The penicillin Target in Bacteria
Scientific congresses and symposiums : Paper published in a book
Life sciences : Biochemistry, biophysics & molecular biology
http://hdl.handle.net/2268/89103
The penicillin Target in Bacteria
English
Ghuysen, Jean-Marie [Université de Liège - ULg > Faculté de Médecine, Institut de Botanique > Service de Microbiologie > >]
Leyh-Bouille, Mélina [Université de Liège - ULg > Faculté de Médecine, Institut de Botanique > Service de Microbiologie > >]
Frère, Jean-Marie mailto [Université de Liège - ULg > Faculté de Médecine, Institut de Botanique > Service de Microbiologie > >]
Dusart, Jean [Université de Liège - ULg > Faculté de Médecine, Institut de Botanique > Service de Microbiologie > >]
Marquet, A. [National Institute for Medical Research - London > > > >]
Perkins, Harold R. [National Institut for Medical research > > > >]
Nieto, M. [National Institut for Medical research > > > >]
1974
Industrial Aspects of Biochemistry (FEBS Proceedings)
Spencer, B.
Elsevier
FEBS Proceedings, vol. 30
579-605
Yes
International
044410593X
978-0720443301
FEBS Special Meeting
1973
FEBS
Dublin
Germany
[en] The bacterial target of beta-lactam antibiotics consists of a set of multiple, membrane-bound receptors. Some of them have been characterized as DD-carboxypeptidases. The DD-carboxypeptidases catalyse the opening of amide bonds and transfer the carbonyl carbon to an exogenous nucleophile, and are specifically designed to operate on the D-Ala-D-Ala linkageof L-R-D-Ala-D-Ala terminated peptides (where R is most often a diamino acid residue). The R61, R39 and several Bacilli DD-carboxypeptidases are known to be serine-enzymes and the G DD-carboxypeptidase has been characterized as a metallo (Zn ions) enzyme. Both the R61 and the G enzymes have been crystallized. In turn, the S. faecalis 43,000-Mr DD-carboxypeptidase, which is inhibited by low dose levels of pCMB, might be a thiol-enzyme. The goal pursued is the understanding of the mechanistic properties and functioning of the active centers of the DD-carboxypeptidases at the molecular and atomic levels. The research program involves 1) further characterization of the S. faecalis enzyme (which can be obtained in a water-soluble form); 2) isolation of various Streptomyces membrane-bound enzymes in a truly water-soluble form; 3) sequencing of the G and R61 enzymes; 4) the 2.8 A structure analysis of the G enzyme. (A similar study is conducted by Dr. J.R. Knox at the University of Connecticut, on the R61 enzyme, which enzyme is prepared and purified in this laboratory and then sent to Storrs); 5) conformational studies and quantitative structure activity relationships (QSAR). Source du résumé : http://www.researchcrossroads.org/index.php?view=article&id=50%3Agrant-details&option=com_content&Itemid=64&grant_id=4296130
Fonds de la Recherche Fondamentale Collective - FRFC
Researchers ; Professionals
http://hdl.handle.net/2268/89103
10.1002/food.19750190412

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