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Antimicrobial Agents and Chemotherapy, December 2001, p. 3591-3594, Vol. 45, No. 12
Laboratoire de Bactériologie,
Hôpital Universitaire du Bocage, 21034 Dijon
Cedex,1 and Unité FRE 2125, CNRS,
UBO, MNHN, 29000 Quimper,2 France
Received 20 February 2001/Returned for modification 29 May
2001/Accepted 28 August 2001
TEM-89 (CMT-3) is the first complex mutant
0066-4804/01/$04.00+0 DOI: 10.1128/AAC.45.12.3591-3594.2001
Copyright © 2001, American Society for Microbiology. All rights reserved.
TEM-89
-Lactamase Produced by a Proteus
mirabilis Clinical Isolate: New Complex Mutant (CMT 3) with
Mutations in both TEM-59 (IRT-17) and TEM-3
-lactamase produced
by a clinical strain of Proteus mirabilis (strain Pm
631). This new enzyme, which has a pI of 6.28, is derived from TEM-3 and has a single amino acid substitution also encountered in TEM-59 (inhibitor-resistant TEM
-lactamase IRT-17): Ser-130 to Gly. TEM-89
hydrolyzed penicillins to the same extent that TEM-3 did but
lost almost all hydrolytic activity for cephalosporins and, like TEM-59, was highly resistant to inhibitors.
*
Corresponding author. Mailing address: Laboratoire de
Bactériologie, Hôpital Universitaire du Bocage, BP 1542, 21034 Dijon Cedex, France. Phone: 33-3 80 29 32 60. Fax: 33-3 80 29 36 67. E-mail: catherine.neuwirth{at}chu-dijon.fr.
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