Accueil > Publications > Recherche par années > Années 1990 > 1993

Jamin, M ; Damblon, C ; Millier, S ; Hakenbeck, R ; Frère, JM

Penicillin-binding protein 2x of streptococcus-pneumoniae - enzymatic-activities and interactions with ß-lactams

Biochemical Journal 292 735-741

par Administrateur - publié le

Abstract :

The high-molecular-mass penicillin-binding protein (PBP) 2x, one of the primary targets of ß-lactam antibiotics in Streptococcus pneumoniae, has been produced as a soluble form and purified in large amounts. It has been shown to catalyse hydrolysis and transfer reactions with different ester and thiolester substrates and its catalytic behaviour was often similar to that of the soluble DD-peptidase from Streptomyces R61. This provided an easy method to monitor the activity of the PBP. For the first time, a reliable kinetic study of the interaction between a lethal target and ß-lactam antibiotics has been performed. Characteristic kinetic parameters were obtained with different ß-lactam compounds. These results not only validated the mechanism established with non-essential extracellular enzymes, but will also constitute the basis for comparative studies of the low-affinity variants from penicillin-resistant strains.