Vinylogous Amide Analogues of Diaminopimelic Acid (DAP) as Inhibitors of Enzymes Involved in Bacterial Lysine Biosynthesis

Jennifer F. Caplan, Renjian Zheng, John S. Blanchard, John C. Vederas

Research output: Contribution to journalArticle

22 Scopus citations

Abstract

Equation Presented Vinylogous amides 5 and 6 have been synthesized from L-propargyl glycine and tested against diaminopimelate (DAP) enzymes involved in bacterial lysine biosynthesis. Both are reversible inhibitors of DAP D-dehydrogenase and DAP epimerase with IC50 values in the 500 μM range. Compound 5 shows competitive inhibition against the L-dihydrodipicolinate (DHDP) reductase with a Ki value of 32 μM, which is comparable to the planar dipicolinate 16 (Ki = 26 μM), the best known inhibitor of the enzyme.

Original languageEnglish (US)
Pages (from-to)3857-3860
Number of pages4
JournalOrganic Letters
Volume2
Issue number24
DOIs
StatePublished - Nov 30 2000

ASJC Scopus subject areas

  • Biochemistry
  • Physical and Theoretical Chemistry
  • Organic Chemistry

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