Crystal structures clarify cofactor binding of plant tyrosine decarboxylase

Hang Wang, Jian Yu, Yasuharu Satoh, Yusuke Nakagawa, Ryusuke Tanaka, Koji Kato, Min Yao

Research output: Contribution to journalArticle

Abstract

Plant tyrosine decarboxylase (TyrDC) is a group II pyridoxal 5′-phosphate (PLP)-dependent decarboxylase that mainly catalyzes the decarboxylation of tyrosine to tyramine. This is biologically important for diverting essential primary metabolites into secondary metabolic pathways. Intensive studies have characterized the effective of PLP-binding and the substrate specificity of mammalian 3,4-dihydroxyphenyl-L-alanine (Dopa) decarboxylases, a member of group II PLP-dependent decarboxylase. However, the characteristics of PLP binding and substrate specificity of plant TyrDCs remain unknown. In this study, we focus on the PLP binding manner, and determined the crystal structures of the apo and PLP binding form of type II TyrDC from Papaver somniferum (PsTyrDCII and PsTyrDCII-PLP). The structures showed that, unlike mammalian Dopa decarboxylase, the binding of PLP does not induce distinct conformational changes of PsTyrDCII regarding the overall structure, but the PLP binding pocket displays conformational changes at Phe124, His203 and Thr262. Combining structural comparation and the obtained biochemical findings, it is demonstrated that PsTyrDCII does not binds PLP tightly. Such characteristics of PLP binding may be required by its catalytic reaction and substrate binding. The activity of TyrDC probably regulated by the concentration of PLP in cells.

Original languageEnglish
Pages (from-to)500-505
Number of pages6
JournalBiochemical and Biophysical Research Communications
Volume523
Issue number2
DOIs
Publication statusPublished - Mar 5 2020

Keywords

  • Aromatic amino acid decarboxylases
  • PLP-dependent
  • Plant tyrosine decarboxylase
  • Structure

ASJC Scopus subject areas

  • Biophysics
  • Biochemistry
  • Molecular Biology
  • Cell Biology

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