Structure-Activity relationship of human serum Paraoxonase PON1

Rakesh Bargota, Mahmoud Akhtar, K Biggadike, David Gani, Rudolf Allemann

Research output: Contribution to journalArticle

17 Citations (Scopus)

Abstract

Substrate analogues based on the parent compounds paraoxon and phenyl acetate were tested on human serum paraoxonase (PON1) to explore the active site of the enzyme. Replacement of the nitro group of paraoxon with an amine or hydrogen, as well as electronic changes to the parent compound, converted these analogues into inhibitors. Introduction of either electron-withdrawing or donating groups onto phenyl acetate resulted in reduction in their rate of hydrolysis by PON1.
Original languageEnglish
Pages (from-to)1623-1626
Number of pages4
JournalBioorganic & Medicinal Chemistry Letters
Volume13
Issue number10
DOIs
Publication statusPublished - 19 May 2003

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