IQUIR   05412
INSTITUTO DE QUIMICA ROSARIO
Unidad Ejecutora - UE
artículos
Título:
A Minimalistic Approach to Identify Substrate Binding Features in B1 Metallo–b–Lactamases
Autor/es:
ANDRES A. POEYLAUT-PALENA; PABLO E. TOMATIS; ANDREAS I. KARSISIOTIS; CHRISTIAN DAMBLON; ERNESTO G. MATA; ALEJANDRO J. VILA
Revista:
BIOORGANIC & MEDICINAL CHEMISTRY LETTERS
Editorial:
Elsevier
Referencias:
Año: 2007 vol. 17 p. 5171 - 5174
ISSN:
0960-894X
Resumen:
The 2-oxoazetidinylacetate sodium salt was synthesized as a model of a minimal â-lactam drug. This compound and the monobactam aztreonam were assayed as substrates of the Metallo-â-lactamase BcII. None of them was hydrolyzed by the enzyme. While the azetidinone was not able to bind BcII, aztreonam was shown to bind in a nonproductive mode. These results provide an explanation for the unability of Metallo-â-lactamases to inactive monobactams and give some clues for inhibitor design.