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Inhibition of bacterial aminopropyltransferases by S ‐adenosyl‐1,8‐diamino‐3‐thiooctane and by dicyclohexylamine
Author(s) -
Pegg Anthony E.,
Bitonti Alan J.,
McCann Peter P.,
Coward James K.
Publication year - 1983
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(82)80600-5
Subject(s) - spermidine , serratia marcescens , in vivo , escherichia coli , in vitro , pseudomonas aeruginosa , bacteria , chemistry , biochemistry , enzyme , microbiology and biotechnology , biology , genetics , gene
Bacterial aminopropyltransferases from Escherichia coli, Serratia marcescens and Pseudomonas aeruginosa were strongly inhibited by S ‐adenosyl‐1,8‐diamino‐3‐thiooctane (AdoDATO) and by dicyclohexylamine. The sensitivity to these drugs in vitro was comparable to that of mammalian spermidine synthase, but AdoDATO was much less potent in reducing spermidine content in the bacteria than in mammalian cells. Although AdoDATO was a stronger inhibitor than dicyclohexylamine in vitro, dicyclohexylamine was more active in reducing bacterial spermidine levels in vivo, suggesting that it is take up better or is more stable in the cell and is the preferable compound for in vivo studies in microorganisms. The strong inhibition of spermidine synthases by AdoDATO which is a transition state analog supports the concept that these enzymes proceed by a single displacement reaction, rather than by a ping‐pong mechanism.