Monoamine Biosynthesis via a Noncanonical Calcium-Activatable Aromatic Amino Acid Decarboxylase in Psilocybin Mushroom
ACS Chemical Biology November 28, 2018 Michael P. Torrens-Spence, Chun‐ting Liu, Tomáš Pluskal et al. 40 citations
A newly characterized enzyme from the psilocybin mushroom Psilocybe cubensis, called PcncAAAD, can decarboxylate several aromatic amino acids—including L-tryptophan, L-phenylalanine, and L-tyrosine—as well as chloro-tryptophan derivatives. Unlike previously known aromatic L-amino acid decarboxylases (AAADs) in mammals and plants, this enzyme belongs to a different protein family and contains a unique C-terminal double-β-barrel domain that binds calcium, which is required for its activity and thermal stability. The enzyme likely contributes to psilocybin biosynthesis and offers a new tool for engineering production of aromatic-amino-acid-derived natural products.