Kinetic study of interaction between BRL 42715, beta-lactamases, and D-alanyl-D-alanine peptidases.
A detailed kinetic study of the interactions between BRL 42715, a beta-lactamase-inhibiting penem, and various beta-lactamases (EC 3.5.2.6) and D-alanyl-D-alanine peptidases (DD-peptidases, EC 3.4.16.4) is presented. The compound was a very efficient inactivator of all active-site serine beta-lactamases but was hydrolyzed by the class B, Zn(2+)-containing enzymes, with very different kcat values. Inactivation of the Streptomyces sp. strain R61 extracellular DD-peptidase was not observed, and the Actinomadura sp. strain R39 DD-peptidase exhibited a low level of sensitivity to the compound.
Matagne
A
A
Laboratoire d'Enzymologie, Université de Liège, Sart-Tilman, Belgium.
Ledent
P
P
Monnaie
D
D
Felici
A
A
Jamin
M
M
Raquet
X
X
Galleni
M
M
Klein
D
D
François
I
I
Frère
J M
JM
D000900:Anti-Bacterial Agents / Q000494:pharmacology*; D004347:Drug Interactions; D007700:Kinetics; D007769:Lactams; D002267:Muramoylpentapeptide Carboxypeptidase / Q000187:drug effects* / Q000378:metabolism; D013302:Streptomyces / Q000187:drug effects / Q000201:enzymology; D065093:beta-Lactamase Inhibitors; D001618:beta-Lactamases / Q000378:metabolism; D047090:beta-Lactams
D000900:Anti-Bacterial Agents; D007769:Lactams; D065093:beta-Lactamase Inhibitors; D047090:beta-Lactams; C061593:C6-(N1-methyl-1,2,3-trazolylmethylene)penem; D002267:Muramoylpentapeptide Carboxypeptidase; D001618:beta-Lactamases