Serine racemases from barley, Hordeum vulgare L., and other plant species represent a distinct eukaryotic group: Gene cloning and recombinant protein characterization

Yoshiyuki Fujitani, Terumi Horiuchi, Kazutoshi Ito, Manabu Sugimoto

Research output: Contribution to journalArticle

26 Citations (Scopus)

Abstract

Several d-amino acids have been identified in plants. However, the biosynthetic pathway to them is unclear. In this study, we cloned and sequenced a cDNA encoding a serine racemase from barley which contained an open reading frame encoding 337 amino acid residues. The deduced amino acid sequence showed significant identity to plant and mammalian serine racemases and contained conserved pyridoxal 5-phosphate (PLP)-binding lysine and PLP-interacting amino acid residues. The purified gene product catalyzed not only racemization of serine but also dehydration of serine to pyruvate. The enzyme requires PLP and divalent cations such as Ca2+, Mg2+, or Mn2+, but not ATP, whereas mammalian serine racemase activity is increased by ATP. In addition to the results regarding the effect of ATP on enzyme activity and the phylogenetic analysis of eukaryotic serine racemases, the antiserum against Arabidopsis serine racemase did not form a precipitate with barley and rice serine racemases. This suggests that plant serine racemases represent a distinct group in the eukaryotic serine racemase family and can be clustered into monocot and dicot types.

Original languageEnglish
Pages (from-to)1530-1536
Number of pages7
JournalPhytochemistry
Volume68
Issue number11
DOIs
Publication statusPublished - Jun 1 2007

Keywords

  • Gramineae
  • Hordeum vulgare L.
  • Oryza sativa
  • Pyridoxal 5-phosphate
  • Serine dehydratase
  • Serine racemase
  • d-Amino acid

ASJC Scopus subject areas

  • Biochemistry
  • Molecular Biology
  • Plant Science
  • Horticulture

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