Skip to main navigation Skip to search Skip to main content

Plant phenylacetaldehyde synthase is a bifunctional homotetrameric enzyme that catalyzes phenylalanine decarboxylation and oxidation

  • Yasuhisa Kaminaga
  • , Jennifer Schnepp
  • , Greg Peel
  • , Christine M. Kish
  • , Gili Ben-Nissan
  • , David Weiss
  • , Irina Orlova
  • , Orly Lavie
  • , David Rhodes
  • , Karl Wood
  • , D. Marshall Porterfield
  • , Arthur J.L. Cooper
  • , John V. Schloss
  • , Eran Pichersky
  • , Alexander Vainstein
  • , Natalia Dudareva*
  • *Corresponding author for this work

Research output: Contribution to journalArticlepeer-review

276 Scopus citations

Abstract

We have isolated and characterized Petunia hybrida cv. Mitchell phenylacetaldehyde synthase (PAAS), which catalyzes the formation of phenylacetaldehyde, a constituent of floral scent. PAAS is a cytosolic homotetrameric enzyme that belongs to group II pyridoxal 5′-phosphate- dependent amino-acid decarboxylases and shares extensive amino acid identity (∼65%) with plant L-tyrosine/3,4-dihydroxy-L-phenylalanine and L-tryptophan decarboxylases. It displays a strict specificity for phenylalanine with an apparent Km of 1.2 mM. PAAS is a bifunctional enzyme that catalyzes the unprecedented efficient coupling of phenylalanine decarboxylation to oxidation, generating phenylacetaldehyde, CO2, ammonia, and hydrogen peroxide in stoichiometric amounts.

Original languageEnglish
Pages (from-to)23357-23366
Number of pages10
JournalJournal of Biological Chemistry
Volume281
Issue number33
DOIs
StatePublished - 18 Aug 2006

Fingerprint

Dive into the research topics of 'Plant phenylacetaldehyde synthase is a bifunctional homotetrameric enzyme that catalyzes phenylalanine decarboxylation and oxidation'. Together they form a unique fingerprint.

Cite this