Catalytic and structural properties of IRT-21 beta-lactamase (TEM-77) from a co-amoxiclav-resistant Proteus mirabilis isolate.

Abstract:

:Proteus mirabilis strain MAG1, a clinical isolate that is resistant to broad-spectrum penicillins and co-amoxiclav, produces inhibitor-resistant TEM (IRT)-21, a novel mutant of TEM beta-lactamase. This enzyme has a pI of 5.2 and is derived from the bla(TEM-1a) gene ancestor. It contains two major amino acid substitutions specific for co-amoxiclav resistance (Leu-69 for Met and Ser-244 for Arg) that have never been found together previously. The dramatic loss of sensitivity to clavulanic acid, the enhancement of K(m) for all beta-lactams and markedly for ticarcillin, and the decrease in the catalytic efficiency makes IRT-21 comparable to the other IRTs with substitutions at position 244 or double substitutions.

journal_name

FEMS Microbiol Lett

authors

Mammeri H,Gilly L,Laurans G,Vedel G,Eb F,Paul G

doi

10.1111/j.1574-6968.2001.tb10945.x

keywords:

subject

Has Abstract

pub_date

2001-12-18 00:00:00

pages

185-9

issue

2

eissn

0378-1097

issn

1574-6968

pii

S037810970100461X

journal_volume

205

pub_type

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