Synthesis of 1-piperideine-6-carboxylic acid produced by L-lysine-ε-aminotransferase from the Streptomyces clavuligerus gene expressed in Escherichia coli

Mei Li Wu, Jun Hao Chen, Chi Tang Ho, Tzou Chi Huang

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9 Scopus citations

Abstract

The gene (laf) encoding L-lysine ε-aminotransferase (LAT) in Streptomyces clavuligerus was cloned and expressed in Escherichia coli. Nucleotide sequence analysis of lat predicted a single open reading frame (ORF) of 1371 bp, encoding a polypeptide of 457 amino acids with calculated molecular mass of 49.89 kDa. S. clavuligerus LAT was grouped into aminotransferase subfamily II of a family on the basis of sequence homology. A model system composed of the recombinant LAT in phosphate buffer was set up to study the biosynthesis of 2-acetyltetrahydropyridine. Lysine was found to be transformed to 1-piperideine-6-carboxylic acid. 2-Acetyltetrahydropyridine was characterized from the mixture of 1-piperideine-6-carboxylic acid and methylglyoxal. For the first time, we demonstrated that the L-lysine ε-aminotransferase is responsible for the formation of 1-piperideine-6-carboxylic acid, which may react with methylglyoxal to generate the acylated N-heterocyclic odorant 2-acetyltetrahydropyridine.

Original languageEnglish (US)
Pages (from-to)1767-1772
Number of pages6
JournalJournal of agricultural and food chemistry
Volume55
Issue number5
DOIs
StatePublished - Mar 7 2007

All Science Journal Classification (ASJC) codes

  • Chemistry(all)
  • Agricultural and Biological Sciences(all)

Keywords

  • 1-piperideine-6-carboxylic acid
  • 2-acetyltetrahydropyridine
  • Biosynthesis
  • L-lysine ε-aminotransferase
  • Methylglyoxal
  • Streptomyces clavuligerus

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