Mechanism-based inactivation of L-pipecolate oxidase by a sulfur-containing substrate analog, 5-THIA-L-pipecolic acid

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Abstract

5-Thia-L-pipecolic acid, (S)-1,3-thiazane-4-carboxylic acid (6), was synthesized and found to serve as an excellent substrate for Rhesus monkey liver L-pipecolate oxidase (L-PO) and also to cause time-dependent, irreversible inactivation of the enzyme. Data are presented demonstrating 6 is a mechanism-based inactivator of L-PO and one of the enzyme turnover products is identified as homocysteine.

Original languageEnglish (US)
Pages (from-to)457-462
Number of pages6
JournalBioorganic and Medicinal Chemistry Letters
Volume7
Issue number4
DOIs
StatePublished - Feb 18 1997

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ASJC Scopus subject areas

  • Biochemistry
  • Molecular Medicine
  • Molecular Biology
  • Pharmaceutical Science
  • Drug Discovery
  • Clinical Biochemistry
  • Organic Chemistry

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