β-Amyrin synthase from Euphorbia tirucalli. Steric bulk, not the π-electrons of Phe, at position 474 has a key role in affording the correct folding of the substrate to complete the normal polycyclization cascade

Ryousuke Ito, Yukari Masukawa, Chika Nakada, Kanako Amari, Chiaki Nakano, Tsutomu Hoshino
  • Organic & Biomolecular Chemistry, January 2014, Royal Society of Chemistry
  • DOI: 10.1039/c4ob00064a

?-Amyrin synthase from Euphorbia tirucalli. Steric bulk, not the ?-electrons of Phe, at position 474

What is it about?

Triterpne is frequently found in Nature. This paper deals with beta-amyrin synthase. beta-Amyrin constitutes the fundamental core of glycyrrhizin, and is also a major bioactive compound derived from the underground parts of Glycyrrhiza (licorice) plants. beta-Amyrin scaffold is constructed from 2,3-oxidosqualene.

Why is it important?

Aromatic amino acids are conserved in many triterpene cyclases. Up to now, the function of the conserved amino acid has been believed to confer the pi-electrons to the intermediary cattions generated during the cycliztion of oxidosqualene. Howere, this is the first report describing that the steric bulk of the conserved amino acid is critical to the cycliztion reaction.

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http://dx.doi.org/10.1039/c4ob00064a

The following have contributed to this page: Tsutomu Hoshino