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. 2002 Feb;46(2):575-7.
doi: 10.1128/AAC.46.2.575-577.2002.

Stability of new carbapenem DA-1131 to renal dipeptidase (dehydropeptidase I)

Sung Wook Park  1 , Jeoung Soon We, Gye Won Kim, Seong Hak Choi, Haeng Soon Park
Affiliations

Stability of new carbapenem DA-1131 to renal dipeptidase (dehydropeptidase I)

Sung Wook Park et al. Antimicrob Agents Chemother. 2002 Feb.

Abstract

The stability of DA-1131 to renal dipeptidase (RDPase) (EC 3.4.13.19) was compared with that of imipenem and meropenem by V(max)/K(m) 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 beta-lactam antibiotic which may be usable without coadministration of RDPase inhibitors once its clinical suitability is proven.

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Figures

FIG. 1.
FIG. 1.
Lineweaver-Burk plots of imipenem (A), meropenem (B), and DA-1131 (C). [I] represents the inhibitor concentration employed. Each data point represents the average of triplicate assays (mean ± standard deviation), and the lines were drawn using the least-squares fit method.
See this image and copyright information in PMC

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