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Antimicrobial Agents and Chemotherapy, June 2002, p. 2014-2016, Vol. 46, No. 6
0066-4804/02/$04.00+0     DOI: 10.1128/AAC.46.6.2014-2016.2002
Copyright © 2002, American Society for Microbiology. All Rights Reserved.

Detection of a Variant Metallo-ß-Lactamase, IMP-10, from Two Unrelated Strains of Pseudomonas aeruginosa and an Alcaligenes xylosoxidans Strain

Shizuko Iyobe,1* Haruko Kusadokoro,2 Ayako Takahashi,3 Sachie Yomoda,3 Toyoji Okubo,1 Akio Nakamura,4 and Koji O'Hara4

Laboratory of Drug Resistance in Bacteria,1 Clinical Laboratory Center, Gunma University School of Medicine, Maebashi,3 Division of Microbial Chemistry, Faculty of Pharmaceutical Sciences, Chiba University, Chiba,2 Department of Microbial Chemistry, Faculty of Pharmaceutical Sciences, Science University of Tokyo, Tokyo, Japan4

Received 21 June 2001/ Returned for modification 5 October 2001/ Accepted 16 March 2002

The gene blaIMP-10 of a variant metallo-ß-lactamase, IMP-10, had a single base replacement of G by T at nucleotide 145, which led to an amino acid alteration of Val49 to Phe compared to the IMP-1 enzyme, indicating that IMP-10 was a point mutation derivative of IMP-1. Highly purified enzymes revealed that IMP-10 was different from IMP-1 in its extremely low hydrolyzing activities for penicillins, such as benzylpenicillin, ampicillin, and piperacillin.

* Corresponding author. Mailing address: Laboratory of Drug Resistance in Bacteria, Gunma University School of Medicine, 3-39-22 Showa-Machi, Maebashi 371-8511, Japan. Phone: 81-27-220-8087. Fax: 81-27-220-8088. E-mail: siyobe{at}med.gunma-u.ac.jp.

Antimicrobial Agents and Chemotherapy, June 2002, p. 2014-2016, Vol. 46, No. 6
0066-4804/02/$04.00+0     DOI: 10.1128/AAC.46.6.2014-2016.2002
Copyright © 2002, American Society for Microbiology. All Rights Reserved.



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