Reference : Interaction between monobactams and model D-alanyl-D-alanine-cleaving peptidases
Scientific journals : Article
Life sciences : Microbiology
http://hdl.handle.net/2268/91748
Interaction between monobactams and model D-alanyl-D-alanine-cleaving peptidases
English
Frère, Jean-Marie mailto [Université de Liège - ULiège > Institut de Chimie > Service de Microbiologie > > > >]
Klein, Daniel [Université de Liège - ULiège > Institut de Chimie > Service de Microbiologie > > > >]
Kelly, Judith A [University of Connecticut - UCONN > Institute of Materials Science > > >]
Ghuysen, Jean-Marie [Université de Liège - ULiège > Institut de Chimie > Service de Microbiologie > > > >]
1984
FEMS Microbiology Letters
Blackwell Publishing
21
213-217
Yes (verified by ORBi)
International
0378-1097
1574-6968
Oxford
United Kingdom
[en] Mode of action of β-lactam antibiotics ; Zn2+dd-carboxypeptidase ; serine dd-carboxypeptidase/transpeptidase
[en] Several monobactams reacted with the serine dd-peptidases of Streptomyces R61 and Actinomadura R39 in a manner similar to that of bicyclic penicillins and cephalosporins. The dissociation constants of the Michaelis complexes formed between the R61 enzyme and sulfazecin (32 μM) and between the R39 peptidase and SQ 26324 (0.35 μM) had the lowest values ever observed with any β-lactam compound, suggesting an excellent fit of these two monobactams with the active sites of the respective enzymes. Azthreonam had a very poor inactivating potency, confirming its high selective reactivity towards the penicillin binding protein No. 3 of Escherichia coli. The Zn2+dd-peptidase (from Streptomyces albus G) had a high intrinsic resistance to β-lactam compounds whether they possessed a mono- or a bicyclic structure.
Fonds de la Recherche Scientifique Médicale - FRSM
Researchers ; Professionals
http://hdl.handle.net/2268/91748
10.1111/j.1574-6968.1984.tb00213.x

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