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 mailto [Université de Liège - ULg > > > >]
Leyh-Bouille, Mélina [Université de Liège - ULG > > > >]
Nguyen-Distèche, Martine mailto [Université de Liège - ULg > > > >]
Coyette, Jacques mailto [Université de Liège - ULg > > > >]
Dusart, Jean [Université de Liège - ULg > > > > >]
Joris, Bernard mailto [Université de Liège - ULg > > > >]
Duez, Colette mailto [Université de Liège - ULg > > > >]
Dideberg, Otto [Université de Liège - ULg > > > > >]
Charlier, Paulette mailto [Université de Liège - ULg > > > >]
Dive, Georges mailto [Université de Liège - ULg > > > >]
Lamotte-Brasseur, Josette mailto [Université de Liège - ULg > > > >]
1984
Scandinavian Journal of Infectious Diseases
Taylor & Francis
42
17-37
Yes (verified by ORBi)
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

There is no file associated with this reference.

Bookmark and Share SFX Query

All documents in ORBi are protected by a user license.