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

Authors :
Christelle Prosperi-Meys
Dominique de Seny
Maria Hernandez Valladares
Jean-Marie Frère
Netza Laraki
Moreno Galleni
Raquel Paul Soto
Gabriel Llabres
Source :
FEBS letters. 443(2)
Publication Year :
1999

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.

Details

ISSN :
00145793
Volume :
443
Issue :
2
Database :
OpenAIRE
Journal :
FEBS letters
Accession number :
edsair.doi.dedup.....5a230a8896cbfe1eb938418ac3add50f