Stability of new carbapenem DA-1131 to renal dipeptidase (dehydropeptidase I).
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.
Park
Sung Wook
SW
Department of Pharmacy, College of Pharmacy, Chonnam National University, Kwangju, Korea.
We
Jeoung Soon
JS
Kim
Gye Won
GW
Choi
Seong Hak
SH
Park
Haeng Soon
HS
D000818:Animals; D015780:Carbapenems / Q000494:pharmacology*; D004150:Dipeptidases / Q000187:drug effects / Q000378:metabolism*; D004795:Enzyme Stability / Q000187:drug effects; D015378:Imipenem / Q000494:pharmacology; D000077731:Meropenem; D013379:Substrate Specificity / Q000187:drug effects; D013845:Thienamycins / Q000494:pharmacology
D015780:Carbapenems; C099230:DA 1131; D013845:Thienamycins; D015378:Imipenem; D004150:Dipeptidases; C038937:dipeptidase; D000077731:Meropenem