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Antimicrobial Agents and Chemotherapy, February 2002, p. 575-577, Vol. 46, No. 2
0066-4804/01/$04.00+0     DOI: 10.1128/AAC.46.2.575-577.2002
Copyright © 2002, American Society for Microbiology. All Rights Reserved.

Stability of New Carbapenem DA-1131 to Renal Dipeptidase (Dehydropeptidase I)

Sung Wook Park,1 Jeoung Soon We,1 Gye Won Kim,2 Seong Hak Choi,2 and Haeng Soon Park1*

Department of Pharmacy, College of Pharmacy, Chonnam National University, Kwangju,1 and Research Laboratory, Dong-A Pharmaceutical Co., Ltd., Yongin, Kyunggi-Do, Korea2

Received 7 September 2000/ Returned for modification 27 February 2001/ Accepted 4 November 2001

The stability of DA-1131 to renal dipeptidase (RDPase) (EC 3.4.13.19) was compared with that of imipenem and meropenem by Vmax/Km ratios as an index of the enzyme's preference for substrates. Our results showed a decreasing order of imipenem (6.24), meropenem (2.41), and DA-1131 (1.39). The biochemical evaluation of DA-1131 as the least preferred substrate of RDPase suggests its potential use as a novel ß-lactam antibiotic which may be usable without coadministration of RDPase inhibitors once its clinical suitability is proven.

* Corresponding author. Mailing address: Department of Pharmacy, College of Pharmacy, Chonnam National University, Kwangju 500-757, Korea. Phone: 82 62 530-2923. Fax: 82 62 530-2949. E-mail: haspark{at}chonnam.chonnam.ac.kr..

Antimicrobial Agents and Chemotherapy, February 2002, p. 575-577, Vol. 46, No. 2
0066-4804/01/$04.00+0     DOI: 10.1128/AAC.46.2.575-577.2002
Copyright © 2002, American Society for Microbiology. All Rights Reserved.





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