Biochemical analysis of phytolacca DOPA dioxygenase

Kana Takahashi, Kazuko Yoshida, Kei Yura, Hiroshi Ashihara, Masaaki Sakuta

Research output: Contribution to journalArticlepeer-review

2 Citations (Scopus)


The biochemical analysis of Phytolacca americana DOPA dioxygenases (PaDOD1 and PaDOD2) was carried out. The recombinant protein of PaDOD1 catalyzed the conversion of DOPA to betalamic acid, whereas DOD activity was not detected in PaDOD2 in vitro. While the reported motif conserved in DODs from betalain-producing plants was found in PaDOD1, a single amino acid residue alteration was detected in PaDOD2. A mutated PaDOD1 protein with a change of 177 Asn to Gly showed reduced specific activity compared with PaDOD1, while DOPA dioxygenase activity was not observed for a mutated PaDOD2 protein which had its conserved motif replaced with that of PaDOD1. A three-dimensional (3D) structural model of PaDOD1 and PaDOD2 showed that the conserved motif in DODs was located in the N-terminal side of a loop, which was found close to the putative active site. The difference in stability of the loop may affect the enzymatic activity of PaDOD2.

Original languageEnglish
Pages (from-to)717-719
Number of pages3
JournalNatural Product Communications
Issue number5
Publication statusPublished - 2015 May
Externally publishedYes


  • Betalains
  • Betalamic acid
  • Caryophyllales
  • DOPA dioxygenase
  • Phytolacca Americana

ASJC Scopus subject areas

  • Pharmacology
  • Plant Science
  • Drug Discovery
  • Complementary and alternative medicine


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