Covering their bases: The phosphobase methylation pathway in plants

J Biol Chem. 2017 Dec 29;292(52):21703-21704. doi: 10.1074/jbc.H117.000712.

Abstract

Phosphoethanolamine methyltransferases add three methyl groups successively to their substrate to produce phosphocholine, an important precursor for phospholipid biosynthesis in diverse organisms. New work from Lee and Jez reveals critical domain movements that explain how multiple methylation reactions are uniquely coordinated by plant methyltransferases and provides insights into the evolution of this class of enzymes. As opposed to closely related family members, the intermediates in this pathway are likely shuttled between two tethered domains to ensure complete methylation.

Keywords: Arabidopsis thaliana; X-ray crystallography; enzyme kinetics; methyltransferase; phosphatidylcholine; phosphocholine; plant biochemistry.

Publication types

  • Research Support, N.I.H., Extramural

MeSH terms

  • Amino Acid Sequence
  • Crystallography, X-Ray
  • Methylation
  • Methyltransferases / metabolism*
  • Methyltransferases / physiology*
  • Phosphatidylcholines / biosynthesis
  • Phosphorylcholine / metabolism
  • Plants / metabolism

Substances

  • Phosphatidylcholines
  • Phosphorylcholine
  • Methyltransferases
  • phosphoethanolamine methyltransferase