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| Reference : Bacterial wall peptidoglycan, DD-peptidases and beta-lactam antibiotics |
| Scientific journals : Article | |||
| Life sciences : Microbiology | |||
| http://hdl.handle.net/2268/66941 | |||
| Bacterial wall peptidoglycan, DD-peptidases and beta-lactam antibiotics | |
| English | |
| Ghuysen, Jean-Marie [Université de Liège - ULg > > > > >] | |
Frère, Jean-Marie  [Université de Liège - ULg > > > >] | |
| Leyh-Bouille, Mélina [Université de Liège - ULG > > > >] | |
| Nguyen-Distèche, Martine [Université de Liège - ULg > > > >] | |
| Coyette, Jacques [Université de Liège - ULg > > > >] | |
| Dusart, Jean [Université de Liège - ULg > > > > >] | |
| Joris, Bernard [Université de Liège - ULg > > > >] | |
| Duez, Colette [Université de Liège - ULg > > > >] | |
| Dideberg, Otto [Université de Liège - ULg > > > > >] | |
| Charlier, Paulette [Université de Liège - ULg > > > >] | |
| Dive, Georges [Université de Liège - ULg > > > >] | |
| Lamotte-Brasseur, Josette [Université de Liège - ULg > > > >] | |
| 1984 | |
| Scandinavian Journal of Infectious Diseases | |
| Taylor & Francis | |
| 42 | |
| 17-37 | |
| International | |
| 0036-5548 | |
| Stockholm | |
| Sweden | |
| [en] Amino Acyl-tRNA Synthetases/metabolism ; Anti-Bacterial Agents/pharmacology ; Bacteria/drug effects/metabolism ; Cell Wall/metabolism ; Chymotrypsin/metabolism ; Dipeptidases/antagonists & inhibitors/metabolism ; Models, Biological ; Peptidoglycan/metabolism ; Peptidyl Transferases/metabolism ; Structure-Activity Relationship ; beta-Lactams | |
| [en] Wall peptidoglycan expansion in bacteria rests upon a cytoplasmic D-Ala: D-Ala ligase (ADP) which catalyses synthesis of a D-Ala-D-Ala dipeptide (with accompanying hydrolysis of one molecule of ATP) and a set of DD-peptidases which utilize this D-Ala-D-Ala dipeptide--once it has been translocated at the outer face of the plasma membrane as the C-terminal portion of a disaccharide peptide unit--as carbonyl donor for transpeptidation and carboxypeptidation reactions (without additional energy expenditure). Four DD-peptidases have been selected which differ from each other with respect to the effects that amino compounds exert on the fate and rate of consumption of a D-Ala-D-Ala terminated amide carbonyl donor analogue. They serve as models to understand the different mechanisms by which the DD-peptidases perform catalysis and show widely varying responses to the action of beta-lactams, from extreme sensitivity to very high resistance. | |
| Researchers ; Professionals | |
| http://hdl.handle.net/2268/66941 |
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