Estrogen esters as substrates for human paraoxonases

John F. Teiber, Scott S. Billecke, Bert N. La Du, Dragomir I. Draganov

Research output: Contribution to journalArticlepeer-review

33 Scopus citations


Mammalian paraoxonases (PONs 1, 2 and 3) are a highly conserved family of esterases, with uncertain physiological functions and natural substrates. Here we characterize the ability of purified recombinant human PONs to hydrolyze estrogen esters, a class of compounds previously not known to be PON substrates. PONs hydrolyzed estrogen mono- and diesters at position 3 of the steroid A-ring. Diesters were better substrates for the PONs and were very efficiently hydrolyzed, particularly by PON3. Esters at position 17 were not cleaved by the PONs unless an adjacent double bound was present. Purified human serum butyryl cholinesterase also hydrolyzed estrogen esters, however it preferably hydrolyzed the mono-esters. The ability of the PONs' to effectively hydrolyze a variety of estrogen esters provides further insight into the structure of their active sites and suggests that natural compounds with aromatic ester groups might be relevant substrates for the PONs.

Original languageEnglish (US)
Pages (from-to)24-29
Number of pages6
JournalArchives of Biochemistry and Biophysics
Issue number1
StatePublished - May 1 2007


  • Butyrylcholinesterase
  • Estrogen esters
  • LDL oxidation
  • PON1
  • PON2
  • PON3

ASJC Scopus subject areas

  • Biophysics
  • Biochemistry
  • Molecular Biology


Dive into the research topics of 'Estrogen esters as substrates for human paraoxonases'. Together they form a unique fingerprint.

Cite this