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FEBS Lett. 1999 Jan 25;443(2):109-11.

Interaction between class B beta-lactamases and suicide substrates of active-site serine beta-lactamases.

Author information

1
Centre d'Ingénierie des Protéines (B6), Université de Liège, Belgium. christelle.prosperi@ulg.ac.be

Abstract

The most widely used inactivators of active-site serine beta-lactamases behave as substrates of four class B metallo-beta-lactamases, but the efficiency of the catalytic process can vary by several orders of magnitude. A comparison of the kinetic parameters for the alpha and beta isomers of 6-iodopenicillanic acid shows that there is no general preference for the alpha isomer and that the efficient hydrolysis of imipenem by these enzymes must rest on other factors.

PMID:
9989585
DOI:
10.1016/s0014-5793(98)01689-5
[Indexed for MEDLINE]
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